We are currently updating the database - data may be missing for the next 10 minutes. We apologize for any inconvenience.

Human Metabolome Database Version 2.5

 

Showing metabocard for Beta-Alanine (HMDB00056)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2009-07-05 13:25:58
Accession Number HMDB00056
Secondary Accession Numbers Not Available
Common Name Beta-Alanine
Description Beta-alanine is the only naturally occurring beta-amino acid - the amino group is at the β-position from the carboxylate group. It is formed in vivo by the degradation of dihydrouracil and carnosine. It is a component of the naturally occurring peptides carnosine and anserine and also of pantothenic acid (Vitamin B-5) which itself is a component of coenzyme A. Under normal conditions, beta-alanine is metabolized into acetic acid. Since neuronal uptake and neuronal receptor sensitivity to beta-alanine have been demonstrated, the compound may be a false transmitter replacing gamma-aminobutyric acid. A rare genetic disorder, hyper-beta-alaninemia, has been reported.
Synonyms
  1. 2-Carboxyethylamine
  2. 3-Aminopropanoate
  3. 3-Aminopropanoic acid
  4. 3-Aminopropionate
  5. 3-Aminopropionic acid
  6. 3-amino-Propanoate
  7. 3-amino-Propanoic acid
  8. Abufene
  9. B-Alanine
  10. b-Aminopropanoate
  11. b-Aminopropanoic acid
  12. b-Aminopropionate
  13. b-Aminopropionic acid
  14. beta Alanine
  15. beta-Alanine
  16. beta-Aminopropionate
  17. beta-Aminopropionic acid
  18. omega-Aminopropionate
  19. omega-Aminopropionic acid
  20. beta-Aminopropanoate
  21. beta-Aminopropanoic acid
Chemical IUPAC Name 3-aminopropanoic acid
Chemical Formula C3H7NO2
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Amino acids and Amino Acid conjugates
Class
  • Amino Acids
Sub Class
  • NA
Family
  • Mammalian Metabolite
Species
  • primary amine
  • primary aliphatic amine (alkylamine)
  • carboxylic acid
Biofunction
  • Component of beta-Alanine metabolism
  • Component of Pantothenate and CoA biosynthesis
  • Component of Pyrimidine metabolism
Application
—
Source
  • Endogenous
Average Molecular Weight 89.093
Monoisotopic Molecular Weight 89.047676
Isomeric SMILES NCCC(O)=O
Canonical SMILES NCCC(O)=O
KEGG Compound ID C00099 Link Image
BioCyc ID B-ALANINE Link Image
BiGG ID 33848 Link Image
Wikipedia Link beta-Alanine Link Image
NuGOwiki Link HMDB00056 Link Image
Metagene Link HMDB00056 Link Image
METLIN ID 5119 Link Image
PubChem Compound 239 Link Image
PubChem Substance 11113405 Link Image
ChEBI ID 16958 Link Image
CAS Registry Number 107-95-9
InChI Identifier InChI=1/C3H7NO2/c4-2-1-3(5)6/h1-2,4H2,(H,5,6)
Synthesis Reference Buc, Saul R.; Ford, Jared H.; Wise, E. C. Improved synthesis of b-alanine. Journal of the American Chemical Society (1945), 67 92-4.
Melting Point (Experimental) 200 oC
Experimental Water Solubility 545.0 mg/mL [YALKOWSKY,SH & DANNENFELSER,RM (1992)] Source: PhysProp
Predicted Water Solubility 494.0 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge 0
State Solid
Experimental LogP/Hydrophobicity -3.05 [TSAI,RS ET AL. (1991)] Source: PhysProp
Predicted LogP/Hydrophobicity -3.26 [Predicted by ALOGPS]; -1 [Predicted by PubChem via XLOGP] Calculated using ALOGPS
Material Safety Data Sheet (MSDS)
MOL File Show
SDF File Show
PDB File Show
2D Structure
3D Structure
Experimental PDB ID Not Available
Experimental 1H NMR Spectrum Download Spectrum
Download FID (Varian)
Show Experimental Conditions Link Image
Experimental 13C NMR Spectrum Download Spectrum
Download FID (Bruker)
Show Experimental Conditions Link Image
Experimental 13C HSQC Spectrum Download Spectrum
Download FID (Bruker)
Show Experimental Conditions Link Image
Predicted 1H NMR Spectrum Show Image
Show Peaklist
Predicted 13C NMR Spectrum Show Image
Show Peaklist
Mass Spectrum
Low Energy
Download File
Show Experimental Conditions Link Image
Medium Energy
Download File
Show Experimental Conditions Link Image
High Energy
Download File
Show Experimental Conditions Link Image
Simplified TOCSY Spectrum Show Image
Show Peaklist
BMRB Spectrum Show Image
Show Peaklist
Cellular Location
  • Cytoplasm
  • Extracellular
  • mitochondria
Biofluid Location
  • Blood
  • Cerebrospinal Fluid
  • Urine
Tissue Location
Tissue References
Kidney —
Muscle —
Pancreas —
Placenta —
Concentrations (Normal)
Biofluid Blood
Value 3.8 +/- 2.9 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Van Kuilenburg AB, Stroomer AE, Van Lenthe H, Abeling NG, Van Gennip AH: New insights in dihydropyrimidine dehydrogenase deficiency: a pivotal role for beta-aminoisobutyric acid? Biochem J. 2004 Apr 1;379(Pt 1):119-24. [PubMed Link Image]
Biofluid Blood
Value 3.00 +/- 0.85 uM
Age Adult:>18 yrs old
Sex Male
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 80-95. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp., Basel, Switzerland c1981-1992.
Biofluid Blood
Value 1.76 +/- 0.74 uM
Age Adult:>18 yrs old
Sex Female
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 80-95. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp., Basel, Switzerland c1981-1992.
Biofluid Blood
Value 3.0 (1.3-20.0) uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Van Kuilenburg AB, Stroomer AE, Van Lenthe H, Abeling NG, Van Gennip AH: New insights in dihydropyrimidine dehydrogenase deficiency: a pivotal role for beta-aminoisobutyric acid? Biochem J. 2004 Apr 1;379(Pt 1):119-24. [PubMed Link Image]
Biofluid Blood
Value 3.0 +/- 0.85 uM
Age Adult:>18 yrs old
Sex Male
Patient information Normal
Comments Not Available
References
  • Kuo KC, Cole TF, Gehrke CW, Waalkes TP, Borek E: Dual-column cation-exchange chromatographic method for beta-aminoisobutyric acid and beta-alanine in biological samples. Clin Chem. 1978 Aug;24(8):1373-80. [PubMed Link Image]
Biofluid Blood
Value 5.00 (0.00-10.00) uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
Biofluid CSF
Value 0.024 +/- 0.013 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Van Kuilenburg AB, Stroomer AE, Van Lenthe H, Abeling NG, Van Gennip AH: New insights in dihydropyrimidine dehydrogenase deficiency: a pivotal role for beta-aminoisobutyric acid? Biochem J. 2004 Apr 1;379(Pt 1):119-24. [PubMed Link Image]
Biofluid CSF
Value 0.03 (0.00-0.06) uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
Biofluid CSF
Value 0.03 (0.00-0.06) uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
Biofluid Urine
Value 2.4 +/- 3.0 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Van Kuilenburg AB, Stroomer AE, Van Lenthe H, Abeling NG, Van Gennip AH: New insights in dihydropyrimidine dehydrogenase deficiency: a pivotal role for beta-aminoisobutyric acid? Biochem J. 2004 Apr 1;379(Pt 1):119-24. [PubMed Link Image]
Biofluid Urine
Value 0.23 +/- 0.73 umol/mmol creatinine
Age Infant:0-1 yr old
Sex Both
Patient information Normal
Comments Not Available
References
  • Shoemaker JD, Elliott WH: Automated screening of urine samples for carbohydrates, organic and amino acids after treatment with urease. J Chromatogr. 1991 Jan 2;562(1-2):125-38. [PubMed Link Image]
Biofluid Urine
Value 0.00068 +/- 0.00049 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Male
Patient information Normal
Comments Not Available
References
  • Kuo KC, Cole TF, Gehrke CW, Waalkes TP, Borek E: Dual-column cation-exchange chromatographic method for beta-aminoisobutyric acid and beta-alanine in biological samples. Clin Chem. 1978 Aug;24(8):1373-80. [PubMed Link Image]
Biofluid Urine
Value 0.0007 +/- 0.00075 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Female
Patient information Normal
Comments Not Available
References
  • Kuo KC, Cole TF, Gehrke CW, Waalkes TP, Borek E: Dual-column cation-exchange chromatographic method for beta-aminoisobutyric acid and beta-alanine in biological samples. Clin Chem. 1978 Aug;24(8):1373-80. [PubMed Link Image]
Biofluid Urine
Value 1.76 +/- 0.74 uM
Age Adult:>18 yrs old
Sex Female
Patient information Normal
Comments Not Available
References
  • Kuo KC, Cole TF, Gehrke CW, Waalkes TP, Borek E: Dual-column cation-exchange chromatographic method for beta-aminoisobutyric acid and beta-alanine in biological samples. Clin Chem. 1978 Aug;24(8):1373-80. [PubMed Link Image]
Biofluid Urine
Value 5.0 (0.00-10.0) uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
Concentrations (Abnormal)
Biofluid Blood
Value 2.7 +/- 1.3 uM
Age Adult:>18 yrs old
Sex Both
Condition Dihydropyrimidine dehydrogenase deficiency
Comments Not Available
References
  • Van Kuilenburg AB, Stroomer AE, Van Lenthe H, Abeling NG, Van Gennip AH: New insights in dihydropyrimidine dehydrogenase deficiency: a pivotal role for beta-aminoisobutyric acid? Biochem J. 2004 Apr 1;379(Pt 1):119-24. [PubMed Link Image]
Biofluid Blood
Value 4.0 (0.9-6.2) uM
Age Adult:>18 yrs old
Sex Both
Condition Dihydropyrimidine dehydrogenase deficiency
Comments Not Available
References
  • Van Kuilenburg AB, Stroomer AE, Van Lenthe H, Abeling NG, Van Gennip AH: New insights in dihydropyrimidine dehydrogenase deficiency: a pivotal role for beta-aminoisobutyric acid? Biochem J. 2004 Apr 1;379(Pt 1):119-24. [PubMed Link Image]
Biofluid Blood
Value 23.0 uM
Age Adult:>18 yrs old
Sex Both
Comments Not Available
References
Biofluid Blood
Value 107.5 (15.00-200.00) uM
Age Adult:>18 yrs old
Sex Both
Comments Not Available
References
Biofluid CSF
Value 0.036 +/- 0.034 uM
Age Adult:>18 yrs old
Sex Both
Condition Dihydropyrimidine dehydrogenase deficiency
Comments Not Available
References
  • Van Kuilenburg AB, Stroomer AE, Van Lenthe H, Abeling NG, Van Gennip AH: New insights in dihydropyrimidine dehydrogenase deficiency: a pivotal role for beta-aminoisobutyric acid? Biochem J. 2004 Apr 1;379(Pt 1):119-24. [PubMed Link Image]
Biofluid CSF
Value 0.48 uM
Age Adult:>18 yrs old
Sex Both
Comments Not Available
References
Biofluid CSF
Value 22.5 (0.00-45.00) uM
Age Adult:>18 yrs old
Sex Both
Comments Not Available
References
Biofluid Urine
Value 1.4 +/- 1.4 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Condition Dihydropyrimidine dehydrogenase deficiency
Comments Not Available
References
  • Van Kuilenburg AB, Stroomer AE, Van Lenthe H, Abeling NG, Van Gennip AH: New insights in dihydropyrimidine dehydrogenase deficiency: a pivotal role for beta-aminoisobutyric acid? Biochem J. 2004 Apr 1;379(Pt 1):119-24. [PubMed Link Image]
Associated Disorders
Condition References
Dihydropyrimidine dehydrogenase deficiency
  • Van Kuilenburg AB, Stroomer AE, Van Lenthe H, Abeling NG, Van Gennip AH: New insights in dihydropyrimidine dehydrogenase deficiency: a pivotal role for beta-aminoisobutyric acid? Biochem J. 2004 Apr 1;379(Pt 1):119-24. [PubMed Link Image]
OMIM ID
  • 274270 Link Image (Dihydropyrimidine dehydrogenase deficiency)
Pathways
Name SMPDB Link KEGG Link
Aspartate Metabolism SMP00067 Link Image map00250 Link Image
Beta-Alanine Metabolism SMP00007 Link Image map00410 Link Image
Propanoate Metabolism SMP00016 Link Image map00640 Link Image
Pyrimidine Metabolism SMP00046 Link Image map00240 Link Image
General References
  1. Van Kuilenburg AB, Stroomer AE, Van Lenthe H, Abeling NG, Van Gennip AH: New insights in dihydropyrimidine dehydrogenase deficiency: a pivotal role for beta-aminoisobutyric acid? Biochem J. 2004 Apr 1;379(Pt 1):119-24. [PubMed Link Image]
  2. Malet-Martino MC, Bernadou J, Martino R, Armand JP: 19F NMR spectrometry evidence for bile acid conjugates of alpha-fluoro-beta-alanine as the main biliary metabolites of antineoplastic fluoropyrimidines in humans. Drug Metab Dispos. 1988 Jan-Feb;16(1):78-84. [PubMed Link Image]
  3. Klebanov GI, Teselkin YuO, Babenkova IV, Lyubitsky OB, Rebrova OYu, Boldyrev AA, Vladimirov YuA: Effect of carnosine and its components on free-radical reactions. Membr Cell Biol. 1998;12(1):89-99. [PubMed Link Image]
  4. Aznar J, Gilabert J, Estelles A, Fernandez MA, Villa P, Aznar JA: Evaluation of the soluble fibrin monomer complexes and other coagulation parameters in obstetric patients. Thromb Res. 1982 Sep 15;27(6):691-701. [PubMed Link Image]
  5. Champion EE, Mann SJ, Glazier JD, Jones CJ, Rawlings JM, Sibley CP, Greenwood SL: System beta and system A amino acid transporters in the feline endotheliochorial placenta. Am J Physiol Regul Integr Comp Physiol. 2004 Dec;287(6):R1369-79. Epub 2004 Jul 29. [PubMed Link Image]
  6. Kuo KC, Cole TF, Gehrke CW, Waalkes TP, Borek E: Dual-column cation-exchange chromatographic method for beta-aminoisobutyric acid and beta-alanine in biological samples. Clin Chem. 1978 Aug;24(8):1373-80. [PubMed Link Image]
  7. van Kuilenburg AB, Meinsma R, Beke E, Assmann B, Ribes A, Lorente I, Busch R, Mayatepek E, Abeling NG, van Cruchten A, Stroomer AE, van Lenthe H, Zoetekouw L, Kulik W, Hoffmann GF, Voit T, Wevers RA, Rutsch F, van Gennip AH: beta-Ureidopropionase deficiency: an inborn error of pyrimidine degradation associated with neurological abnormalities. Hum Mol Genet. 2004 Nov 15;13(22):2793-801. Epub 2004 Sep 22. [PubMed Link Image]
  8. Heggie GD, Sommadossi JP, Cross DS, Huster WJ, Diasio RB: Clinical pharmacokinetics of 5-fluorouracil and its metabolites in plasma, urine, and bile. Cancer Res. 1987 Apr 15;47(8):2203-6. [PubMed Link Image]
  9. Gibson KM, Schor DS, Gupta M, Guerand WS, Senephansiri H, Burlingame TG, Bartels H, Hogema BM, Bottiglieri T, Froestl W, Snead OC, Grompe M, Jakobs C: Focal neurometabolic alterations in mice deficient for succinate semialdehyde dehydrogenase. J Neurochem. 2002 Apr;81(1):71-9. [PubMed Link Image]
  10. Holm B, Nilsen DW, Kierulf P, Godal HC: Purification and characterization of 3 fibrinogens with different molecular weights obtained from normal human plasma. Thromb Res. 1985 Jan 1;37(1):165-76. [PubMed Link Image]
  11. Chen Y, Getchell TV, Sparks DL, Getchell ML: Cellular localization of carnosinase in the human nasal mucosa. Acta Otolaryngol. 1994 Mar;114(2):193-8. [PubMed Link Image]
  12. Milasta S, Pediani J, Appelbe S, Trim S, Wyatt M, Cox P, Fidock M, Milligan G: Interactions between the Mas-related receptors MrgD and MrgE alter signalling and trafficking of MrgD. Mol Pharmacol. 2006 Feb;69(2):479-91. Epub 2005 Nov 9. [PubMed Link Image]
  13. Harris RC, Tallon MJ, Dunnett M, Boobis L, Coakley J, Kim HJ, Fallowfield JL, Hill CA, Sale C, Wise JA: The absorption of orally supplied beta-alanine and its effect on muscle carnosine synthesis in human vastus lateralis. Amino Acids. 2006 May;30(3):279-89. Epub 2006 Mar 24. [PubMed Link Image]
  14. Hibbard JU, Pridjian G, Whitington PF, Moawad AH: Taurine transport in the in vitro perfused human placenta. Pediatr Res. 1990 Jan;27(1):80-4. [PubMed Link Image]
  15. Karmanskii IM: [Effect of pepsin on low density serum lipoproteins] Vopr Med Khim. 1977 Jul-Aug;23(4):530-4. [PubMed Link Image]
  16. Johnson MR, Barnes S, Sweeny DJ, Diasio RB: 2-Fluoro-beta-alanine, a previously unrecognized substrate for bile acid coenzyme A:amino acid:N-acyltransferase from human liver. Biochem Pharmacol. 1990 Sep 15;40(6):1241-6. [PubMed Link Image]
  17. Wikipedia Link Image
Metabolic Enzymes
  1. 4-aminobutyrate aminotransferase, mitochondrial precursor
  2. 4-trimethylaminobutyraldehyde dehydrogenase
  3. Alpha-aminoadipic semialdehyde dehydrogenase
  4. Aldehyde dehydrogenase 1A3
  5. Aldehyde dehydrogenase, mitochondrial precursor
  6. Fatty aldehyde dehydrogenase
  7. Aldehyde dehydrogenase X, mitochondrial precursor
  8. Beta-Ala-His dipeptidase precursor
  9. Beta-ureidopropionase
  10. Glutamate decarboxylase 2
  11. Hypothetical protein GAD1
  12. cDNA FLJ75643, highly similar to Homo sapiens 4-aminobutyrate aminotransferase
  13. UPB1 protein
  14. Transporter
  15. Solute carrier family 6 (Neurotransmitter transporter, taurine), member 6 (Solute carrier family 6 (Neurotransmitter transporter, taurine), member 6, isoform CRA_a)
  16. cDNA FLJ60211, highly similar to Sodium- and chloride-dependent taurine transporter
Enzyme 1 [top]
Enzyme 1 ID 5480
Enzyme 1 Name 4-aminobutyrate aminotransferase, mitochondrial precursor
Enzyme 1 Synonyms
  1. (S-3-amino-2-methylpropionate transaminase
  2. Gamma-amino-N-butyrate transaminase
  3. GABA transaminase
  4. GABA aminotransferase
  5. GABA-AT
  6. GABA-T
  7. L-AIBAT
Enzyme 1 Gene Name ABAT
Enzyme 1 Protein Sequence >4-aminobutyrate aminotransferase, mitochondrial precursor 
MASMLLAQRLACSFQHSYRLLVPGSRHISQAAAKVDVEFDYDGPLMKTEVPGPRSQELMK
QLNIIQNAEAVHFFCNYEESRGNYLVDVDGNRMLDLYSQISSVPIGYSHPALLKLIQQPQ
NASMFVNRPALGILPPENFVEKLRQSLLSVAPKGMSQLITMACGSCSNENALKTIFMWYR
SKERGQRGFSQEELETCMINQAPGCPDYSILSFMGAFHGRTMGCLATTHSKAIHKIDIPS
FDWPIAPFPRLKYPLEEFVKENQQEEARCLEEVEDLIVKYRKKKKTVAGIIVEPIQSEGG
DNHASDDFFRKLRDIARKHGCAFLVDEVQTGGGCTGKFWAHEHWGLDDPADVMTFSKKMM
TGGFFHKEEFRPNAPYRIFNTWLGDPSKNLLLAEVINIIKREDLLNNAAHAGKALLTGLL
DLQARYPQFISRVRGRGTFCSFDTPDDSIRNKLILIARNKGVVLGGCGDKSIRFRPTLVF
RDHHAHLFLNIFSDILADFK
Enzyme 1 Number of Residues 500
Enzyme 1 Molecular Weight 56440
Enzyme 1 Theoretical pI 8.04
Enzyme 1 GO Classification
Function
  • 4-aminobutyrate transaminase activity
  • binding
  • catalytic activity
  • pyridoxal phosphate binding
  • transaminase activity
  • transferase activity
  • transferase activity, transferring nitrogenous groups
  • vitamin binding
Process
  • amino acid and derivative metabolism
  • amino acid derivative metabolism
  • cellular metabolism
  • gamma-aminobutyric acid metabolism
  • metabolism
  • physiological process
Component
—
Enzyme 1 General Function Amino acid transport and metabolism
Enzyme 1 Specific Function Catalyzes the conversion of gamma-aminobutyrate and L- beta-aminoisobutyrate to succinate semialdehyde and methylmalonate semialdehyde, respectively. Can also convert delta-aminovalerate and beta-alanine
Enzyme 1 Pathways
  • Valine, Leucine and Isoleucine Degradation (map00280 Link Image)
Enzyme 1 Reactions
  • (S)-3-amino-2-methylpropanoate + 2-oxoglutarate = 2-methyl-3-oxopropanoate + L-glutamate
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 602705 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID P80404 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name GABT_HUMAN Link Image
Enzyme 1 PDB ID 1OHY Link Image
Enzyme 1 PDB File Show
Enzyme 1 3D Structure
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >1503 bp 
ATGGCCTCCATGTTGCTCGCCCAGCGGCTGGCCTGCAGCTTCCAGCACACGTACCGCCTG
CTGGTGCCTGGATCCAGACACATTAGTCAAGCTGCAGCCAAAGTCGACGTTGAATTTGAT
TATGATGGGCCTCTGATGAAGACGGAAGTCCCAGGGCCTAGATCTCAGGAGTTAATGAAA
CAGCTGAATATAATTCAGAATGCAGAGGCTGTGCATTTTTTCTGCAATTACGAAGAGAGC
CGAGGCAATTACCTGGTTGATGTGGACGGCAACCGAATGCTGGATCTTTATTCCCAGATC
TCCTCTGTTCCCATAGGTTACAGCGACCCGGCCCTCGTGAAACTCATCCAACAGCCACAA
AATGCGAGCATGTTTGTCAACAGACCCGCCCTCGAAATCCTGCCTCCGGAGAACTTTGTG
GAGAAGCTCCGGCAGTCCTTGCTCTCGGTGGCTCCCAAAGGGATGTCCCAGCTCATCACC
ATGGCCTGCGGCTCCTGCTCCAATGAAAACGCCTTAAAGACCATCTTCATGTGGTACCGG
AGCAAGGAAAGAGGGCAGAGGGGATTCTCCAAAGAGGAGCTGGAGACGTGCATGATTAAC
CAGGCCCCCTGGTGCCCCGACTACAGCATCCTCTCCTTCATGGGTTCCTTCCATGGGAGG
ACCATGGGTTGCTTAGCGACCACGCACTCTAAAGCCATTCACAAGATCGATATCCCTTCC
TTTGACTGGCCCATCGCACCGTTCCCACGGCTGAAATACCCTCTGGAAGAGTTTGTGAAA
GAGAACCAACAGGAAGAGGCCGGCTGTCTGGAAGAGGTTGAGGATCTGATTGTGAAATAT
CGAAAAAAGAAGAAGACGGTGGCCGGGATCATCGTGGAGCCCATCCAGTCCGAGGGTGGA
GACAACCATGCATCCGATGACTTCTTTCGGAAGCTGAGAGACATCGCCAGGAAGCACTGC
TGCGCCTTCTTGGTGGACGAGGTCCAGACCGGAGGAGGCTGCACGGGCAAGTTCTGGGCC
CATGAGCACTGGGGCCTGGATGACCCAGCAGACGTGATGACCTTCAGCAAGAAGATGATG
ACTGGGGGCTTCTTCCTCAAGGAGGAGTTCAGGCCTAATGCTCCCTACCGGATCTTCAAC
ACGTGGCTGGGGGACCCGTCCAAGAACCTGTTGCTGGCTGAGGTCATCAACATCATCAAG
CGGGAGGACCTGCTAAATAATGCAGCCCATGCCGGGAAGGCCCTGCTCACAGGACTGCTG
GACCTCCAGGCCCGGTACCCCCAGTTCATCAGCAGGGTGAGAGGACGAGGCACCTTTTGC
TCCTTCGATACTCCCGATGATTCCATACGGAATAAGCTCATTTTAATTGCCAGAAACAAA
GGTGTGGTGTTGGGTGGCTGTGGTGACAAATCCATTCGTTTCCGTCCCACGCTGGTGTTC
AGGGATCACCACGCTCACCTGTTCCTCAATATTTTCAGTGACATCTTAGCAGACTTCAAG
TAA
Enzyme 1 GenBank Gene ID L32961 Link Image
Enzyme 1 GeneCard ID ABAT Link Image
Enzyme 1 GenAtlas ID ABAT Link Image
Enzyme 1 HGNC ID HGNC:23 Link Image
Enzyme 1 Chromosome Location 16
Enzyme 1 Locus 16p13.2
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Osei YD, Churchich JE: Screening and sequence determination of a cDNA encoding the human brain 4-aminobutyrate aminotransferase. Gene. 1995 Apr 3;155(2):185-7. [PubMed Link Image]
  2. De Biase D, Barra D, Simmaco M, John RA, Bossa F: Primary structure and tissue distribution of human 4-aminobutyrate aminotransferase. Eur J Biochem. 1995 Jan 15;227(1-2):476-80. [PubMed Link Image]
  3. Medina-Kauwe LK, Tobin AJ, De Meirleir L, Jaeken J, Jakobs C, Nyhan WL, Gibson KM: 4-Aminobutyrate aminotransferase (GABA-transaminase) deficiency. J Inherit Metab Dis. 1999 Jun;22(4):414-27. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5526
Enzyme 2 Name 4-trimethylaminobutyraldehyde dehydrogenase
Enzyme 2 Synonyms
  1. TMABADH
  2. Aldehyde dehydrogenase 9A1
  3. Aldehyde dehydrogenase E3 isozyme
  4. Gamma-aminobutyraldehyde dehydrogenase
  5. R- aminobutyraldehyde dehydrogenase
Enzyme 2 Gene Name ALDH9A1
Enzyme 2 Protein Sequence >4-trimethylaminobutyraldehyde dehydrogenase 
MSTGTFVVSQPLNYRGGARVEPADASGTEKAFEPATGRVIATFTCSGEKEVNLAVQNAKA
AFKIWSQKSGMERCRILLEAARIIREREDEIATMECINNGKSIFEARLDIDISWQCLEYY
AGLAASMAGEHIQLPGGSFGYTRREPLGVCVGIGAWNYPFQIASWKSAPALACGNAMVFK
PSPFTPVSALLLAEIYSEAGVPPGLFNVVQGGAATGQFLCQHPDVAKVSFTGSVPTGMKI
MEMSAKGIKPVTLELGGKSPLIIFSDCDMNNAVKGALMANFLTQGQVCCNGTRVFVQKEI
LDKFTEEVVKQTQRIKIGDPLLEDTRMGPLINRPHLERVLGFVKVAKEQGAKVLCGGDIY
VPEDPKLKDGYYMRPCVLTNCRDDMTCVKEEIFGPVMSILSFDTEAEVLERANDTTFGLA
AGVFTRDIQRAHRVVAELQAGTCFINNYNVSPVELPFGGYKKSGFGRENGRVTIEYYSQL
KTVCVEMGDVESAF
Enzyme 2 Number of Residues 494
Enzyme 2 Molecular Weight 53802
Enzyme 2 Theoretical pI 5.61
Enzyme 2 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
Process
  • metabolism
  • physiological process
Component
—
Enzyme 2 General Function Energy production and conversion
Enzyme 2 Specific Function Converts gamma-trimethylaminobutyraldehyde into gamma- butyrobetaine. Catalyzes the irreversible oxidation of a broad range of aldehydes to the corresponding acids in an NAD-dependent reaction
Enzyme 2 Pathways
Enzyme 2 Reactions
  • 4-trimethylammoniobutanal + NAD+ = 4-trimethylammoniobutanoate + NADH + H+
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 1049219 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID P49189 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name AL9A1_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >1482 bp 
ATGAGCACTGGCACCTTCGTCGTGTCGCAGCCGCTCAATTACCGCGGCGGGGCCGCTGGA
GCCGGCGGACGCTCCGGTACCGAGAAAGCTTTCGAGCCAGCAACCGGCCGAGTGATAGCT
ACTTTCACATGTTCAGGAGAAAAGGAAGTAAATTTGGCTGTTCAAAATGCAAAGGCTGCT
TTTAAAATATGGAGTCAAAAATCTGGCATGGAGCGTTGCCGAATCCTTTTGGAGGCTGCC
AGGATAATAAGGGAACGGGAGGATGAAATTGCTACTATGGAGTGCATCAACAATGGCAAG
TCCATCTTTGAGGCCCGCTTGGACATTGACATTTCCTGGCAGTGCCTGGAGTATTATGCG
GGCTTGGCTGCATCCATGGCTGGTGAACACATCCAGCTCCCAGGTGGATCGTTTGGTTAT
ACCAGAAGAGAACCACTTGGGGTATGTGTGGGAATAGGAGCATGGAACTACCCCTTTCAG
ATTGCCTCTTGGAAGTCGGCTCCAGCATTAGCCTGTGGTAATGCCATGGTCTTTAAACCT
TCTCCCTTTACACCTGTTTCTGCATTGCTACTGGCTGAAATCTACAGTGAGGCTGGTGTA
CCTCCTGGGCTCTTCAATGTGGTGCAGGGAGGGGCTGCCACAGGCCAGTTTCTGTGTCAG
CATCCCGATGTGGCCAAAGTCTCCTTCACTGGAAGTGTGCCCACTGGCATGAAGATCATG
GAGATGTCAGCTAAAGGAATCAAACCTGTTACCTTGGAACTTGGAGGCAAATCTCCACTC
ATCATCTTCTCAGACTGTGATATGAACAATGCTGTAAAGGGGGCGCTGATGGCCAACTTC
CTCACACAAGGCCAGGTTTGCTGTAATGGCACAAGAGTATTTGTGCAGAAAGAAATTCTT
GATAAATTTACAGAGGAAGTGGTGAAACAGACCCAAAGGATTAAAATTGGAGATCCCCTT
CTGGAAGATACAAGGATGGGTCCACTCATCAACCGACCACACCTGGAGCGAGTCCTTGGG
TTTGTCAAAGTGGCAAAGGAGCAGGGTGCTAAAGTGTTATGTGGTGGAGATATATATGTA
CCTGAAGATCCCAAATTAAAGGATGGATATTACATGAGACCTTGTGTATTAACTAATTGC
AGAGACGACATGACCTGTGTGAAGGAAGAGATCTTTGGGCCTGTTATGTCCATTTTATCA
TTTGACACTGAAGCTGAGGTTCTAGAAAGAGCCAATGATACCACTTTTGGACTAGCAGCT
GGCGTCTTTACCAGGGACATCCAACGGGCTCATAGAGTGGTAGCTGAGCTTCAGGCTGGG
ACGTGCTTCATTAACAACTATAACGTCAGCCCAGTGGAGTTGCCCTTTGGTGGATATAAG
AAGTCAGGATTTGGCAGAGAGAACGGCCGTGTGACAATCGAATATTATTCACAGCTGAAG
ACTGTGTGTGTGGAGATGGGTGATGTGGAATCTGCTTTTTGA
Enzyme 2 GenBank Gene ID U34252 Link Image
Enzyme 2 GeneCard ID ALDH9A1 Link Image
Enzyme 2 GenAtlas ID ALDH9A1 Link Image
Enzyme 2 HGNC ID HGNC:412 Link Image
Enzyme 2 Chromosome Location 1
Enzyme 2 Locus 1q23.1
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Lin SW, Chen JC, Hsu LC, Hsieh CL, Yoshida A: Human gamma-aminobutyraldehyde dehydrogenase (ALDH9): cDNA sequence, genomic organization, polymorphism, chromosomal localization, and tissue expression. Genomics. 1996 Jun 15;34(3):376-80. [PubMed Link Image]
  2. Vaz FM, Fouchier SW, Ofman R, Sommer M, Wanders RJ: Molecular and biochemical characterization of rat gamma-trimethylaminobutyraldehyde dehydrogenase and evidence for the involvement of human aldehyde dehydrogenase 9 in carnitine biosynthesis. J Biol Chem. 2000 Mar 10;275(10):7390-4. [PubMed Link Image]
  3. Kikonyogo A, Pietruszko R: Aldehyde dehydrogenase from adult human brain that dehydrogenates gamma-aminobutyraldehyde: purification, characterization, cloning and distribution. Biochem J. 1996 May 15;316 ( Pt 1):317-24. [PubMed Link Image]
  4. Kurys G, Shah PC, Kikonygo A, Reed D, Ambroziak W, Pietruszko R: Human aldehyde dehydrogenase. cDNA cloning and primary structure of the enzyme that catalyzes dehydrogenation of 4-aminobutyraldehyde. Eur J Biochem. 1993 Dec 1;218(2):311-20. [PubMed Link Image]
  5. Kurys G, Ambroziak W, Pietruszko R: Human aldehyde dehydrogenase. Purification and characterization of a third isozyme with low Km for gamma-aminobutyraldehyde. J Biol Chem. 1989 Mar 15;264(8):4715-21. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 5528
Enzyme 3 Name Alpha-aminoadipic semialdehyde dehydrogenase
Enzyme 3 Synonyms
  1. Alpha-AASA dehydrogenase
  2. Delta1-piperideine-6-carboxylate dehydrogenease
  3. P6c dehydrogenase
  4. Aldehyde dehydrogenase family 7 member A1
  5. Antiquitin-1
Enzyme 3 Gene Name ALDH7A1
Enzyme 3 Protein Sequence >Alpha-aminoadipic semialdehyde dehydrogenase 
MSTLLINQPQYAWLKELGLREENEGVYNGSWGGRGEVITTYCPANNEPIARVRQASVADY
EETVKKAREAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKILVEGVGEVQ
EYVDICDYAVGLSRMIGGPILPSERSGHALIEQWNPVGLVGIITAFNFPVAVYGWNNAIA
MICGNVCLWKGAPTTSLISVAVTKIIAKVLEDNKLPGAICSLTCGGADIGTAMAKDERVN
LLSFTGSTQVGKQVGLMVQERFGRSLLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQ
RCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDPNVLYGPLHTKQAVSMFLGAVEEA
KKEGGTVVYGGKVMDRPGNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWN
NEVKQGLSSSIFTKDLGRIFRWLGPKGSDCGIVNVNIPTSGAEIGGAFGGEKHTGGGRES
GSDAWKQYMRRSTCTINYSKDLPLAQGIKFQ
Enzyme 3 Number of Residues 511
Enzyme 3 Molecular Weight 55367
Enzyme 3 Theoretical pI 6.86
Enzyme 3 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
Process
  • metabolism
  • physiological process
Component
—
Enzyme 3 General Function Energy production and conversion
Enzyme 3 Specific Function L-2-aminoadipate 6-semialdehyde + NAD(P)(+) + H(2)O = L-2-aminoadipate + NAD(P)H
Enzyme 3 Pathways
Enzyme 3 Reactions
  • L-2-aminoadipate 6-semialdehyde + NAD(P)+ + H2O = L-2-aminoadipate + NAD(P)H + H+
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 797410 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID P49419 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name AL7A1_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >1536 bp 
ATGTCCACTCTCCTCATCAATCAGCCCCAGTATGCGTGGCTGAAAGAGCTGGGGCTCCGC
GAGGAAAACGAGGGCGTGTATAATGGAAGCTGGGGAGGCCGGGGAGAGGTTATTACGACC
TATTGCCCCGCTAACAACGAGCCAATAGCAAGAGTCCGACAGGCCAGTGTGGCAGACTAT
GAAGAAACTGTAAAGAAAGCAAGAGAAGCATGGAAAATCTGGGCAGATATTCCTGCTCCA
AAACGAGGAGAAATAGTAAGACAGATTGGCGATGCCTTGCGGGAGAAGATCCAAGTACTA
GGAAGCTTGGTGTCTTTGGAGATGGGGAAAATCTTAGTGGAAGGTGTGGGTGAAGTTCAG
GAGTATGTGGATATCTGTGACTATGCTGTTGGTTTATCAAGGATGATTGGAGGACCTATC
TTGCCTTCTGAAAGATCTGGCCATGCACTGATTGAGCAGTGGAATCCCGTAGGCCTGGTT
GGAATCATCACGGCATTCAATTTCCCTGTGGCAGTGTATGGTTGGAACAACGCCATCGCC
ATGATCTGTGGAAATGTCTGCCTCTGGAAAGGAGCTCCAACCACTTCCCTCATTAGTGTG
GCTGTCACAAAGATAATAGCCAAGGTTCTGGAGGACAACAAGCTGCCTGGTGCAATTTGT
TCCTTGACTTGTGGTGGAGCAGATATTGGCACAGCAATGGCCAAAGATGAACGAGTGAAC
CTGCTGTCCTTCACTGGGAGCACTCAGGTGGGAAAACAGGTGGGCCTGATGGTGCAGGAG
AGGTTTGGGAGAAGTCTGTTGGAACTTGGAGGAAACAATGCCATTATTGCCTTTGAAGAT
GCAGACCTCAGCTTAGTTGTTCCATCAGCTCTCTTCGCTGCTGTGGGAACAGCTGGCCAG
AGGTGTACCACTGCGAGGCGACTGTTTATACATGAAAGCATCCATGATGAGGTTGTAAAC
AGACTTAAAAAGGCCTATGCACAGATCCGAGTTGGGAACCCATGGGACCCTAATGTTCTC
TATGGGCCACTCCACACCAAGCAGGCAGTGAGCATGTTTCTTGGAGCAGTGGAAGAAGCA
AAGAAAGAAGGTGGCACAGTGGTCTATGGGGGCAAGGTTATGGATCGCCCTGGAAATTAT
GTAGAACCGACAATTGTGACAGGTCTTGGCCACGATGCGTCCATTGCACACACAGAGACT
TTCGCTCCGATTCTCTATGTCTTTAAATTCAAGAATGAAGAAGAGGTCTTTGCATGGAAT
AATGAAGTAAAACAGGGACTTTCAAGTAGCATCTTTACCAAAGATCTGGGCAGAATCTTT
CGCTGGCTTGGACCTAAAGGATCAGACTGTGGCATTGTAAATGTCAACATTCCAACAAGT
GGGGCTGAGATTGGAGGTGCCTTTGGAGGAGAAAAGCACACTGGTGGTGGCAGGGAGTCT
GGCAGTGATGCCTGGAAACAGTACATGAGAAGGTCTACTTGTACTATCAACTACAGTAAA
GACCTTCCTCTGGCCCAAGGAATCAAGTTTCAGTAA
Enzyme 3 GenBank Gene ID S74728 Link Image
Enzyme 3 GeneCard ID ALDH7A1 Link Image
Enzyme 3 GenAtlas ID ALDH7A1 Link Image
Enzyme 3 HGNC ID HGNC:877 Link Image
Enzyme 3 Chromosome Location 5
Enzyme 3 Locus 5q31
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Lee P, Kuhl W, Gelbart T, Kamimura T, West C, Beutler E: Homology between a human protein and a protein of the green garden pea. Genomics. 1994 May 15;21(2):371-8. [PubMed Link Image]
  2. Skvorak AB, Robertson NG, Yin Y, Weremowicz S, Her H, Bieber FR, Beisel KW, Lynch ED, Beier DR, Morton CC: An ancient conserved gene expressed in the human inner ear: identification, expression analysis, and chromosomal mapping of human and mouse antiquitin (ATQ1). Genomics. 1997 Dec 1;46(2):191-9. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 5529
Enzyme 4 Name Aldehyde dehydrogenase 1A3
Enzyme 4 Synonyms
  1. Aldehyde dehydrogenase 6
  2. Retinaldehyde dehydrogenase 3
  3. RALDH-3
Enzyme 4 Gene Name ALDH1A3
Enzyme 4 Protein Sequence >Aldehyde dehydrogenase 1A3 
MATANGAVENGQPDRKPPALPRPIRNLEVKFTKIFINNEWHESKSGKKFATCNPSTREQI
CEVEEGDKPDVDKAVEAAQVAFQRGSPWRRLDALSRGRLLHQLADLVERDRATLAALETM
DTGKPFLHAFFIDLEGCIRTLRYFAGWADKIQGKTIPTDDNVVCFTRHEPIGVCGAITPW
NFPLLMLVWKLAPALCCGNTMVLKPAEQTPLTALYLGSLIKEAGFPPGVVNIVPGFGPTV
GAAISSHPQINKIAFTGSTEVGKLVKEAASRSNLKRVTLELGGKNPCIVCADADLDLAVE
CAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFDVKTEQGPQIDQK
QFDKILELIESGKKEGAKLECGGSAMEDKGLFIKPTVFSEVTDNMRIAKEEIFGPVQPIL
KFKSIEEVIKRANSTDYGLTAAVFTKNLDKALKLASALESGTVWINCYNALYAQAPFGGF
KMSGNGRELGEYALAEYTEVKTVTIKLGDKNP
Enzyme 4 Number of Residues 512
Enzyme 4 Molecular Weight 56109
Enzyme 4 Theoretical pI 7.29
Enzyme 4 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
Process
  • metabolism
  • physiological process
Component
—
Enzyme 4 General Function Energy production and conversion
Enzyme 4 Specific Function Recognizes as substrates free retinal and cellular retinol-binding protein-bound retinal. Seems to be the key enzyme in the formation of an RA gradient along the dorso-ventral axis during the early eye development and also in the development of the olfactory system
Enzyme 4 Pathways
Enzyme 4 Reactions
  • an aldehyde + NAD(P)+ + H2O = an acid + NAD(P)H + H+
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • None
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 544482 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID P47895 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name AL1A3_HUMAN Link Image
Enzyme 4 PDB ID Not Available
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >1539 bp 
ATGGCCACCGCTAACGGGGCCGTGGAAAACGGGCAGCCGGACGGGAAGCCGCCGGCCCTG
CCGCGCCCCATCCGCAACCTGGAGGTCAAGTTCACCAAGATATTTATCAACAATGAATGG
CACGAATCCAAGAGTGGGAAAAAGTTTGCTACATGTAACCCTTCAACTCGGGAGCAAATA
TGTGAAGTGGAAGAAGGAGATAAGCCCGACGTGGACAAGGCTGTGGAGGCTGCACAGGTT
GCCTTCCAGAGGGGCTCGCCATGGCGCCGGCTGGATGCCCTGAGTCGTGGGCGGCTGCTG
CACCAGCTGGCTGACCTGGTGGAGAGGGACCGCGCCACCTTGGCCGCCCTGGAGACGATG
GATACAGGGAAGCCATTTCTTCATGCTTTTTTCATCGACCTGGAGGGCTGTATTAGAACC
CTCAGATACTTTGCAGGGTGGGCAGACAAAATCCAGGGCAAGACCATCCCCACAGATGAC
AACGTCGTATGCTTCACCAGGCATGAGCCCATTGGTGTCTGTGGGGCCATCACTCCATGG
AACTTCCCCCTGCTGATGCTGGTGTGGAAGCTGGCACCCGCCCTCTGCTGTGGGAACACC
ATGGTCCTGAAGCCTGCGGAGCAGACACCTCTCACCGCCCTTTATCTCGGCTCTCTGATC
AAAGAGGCCGGGTTCCCTCCAGGAGTGGTGAACATTGTGCCAGGATTCGGGCCCACAGTG
GGAGCAGCAATTTCTTCTCACCCTCAGATCAACAAGATCGCCTTCACCGGCTCCACAGAG
GTTGGAAAACTGGTTAAAGAAGCTGCGTCCCGGAGCAATCTGAAGCGGGTGACGCTGGAG
CTGGGGGGGAAGAACCCCTGCATCGTGTGTGCGGACGCTGACTTGGACTTGGCAGTGGAG
TGTGCCCATCAGGGAGTGTTCTTCAACCAAGGCCAGTGTTGCACGGCAGCCTCCAGGGTG
TTCGTGGAGGAGCAGGTCTACTCTGAGTTTGTCAGGCGGAGCGTGGAGTATGCCAAGAAA
CGGCCCGTGGGAGACCCCTTCGATGTCAAAACAGAACAGGGGCCTCAGATTGATCAAAAG
CAGTTCGACAAAATCTTAGAGCTGATCGAGAGTGGGAAGAAGGAAGGGGCCAAGCTGGAA
TGCGGGGGCTCAGCCATGGAAGACAAGGGGCTCTTCATCAAACCCACTGTCTTCTCAGAA
GTCACAGACAACATGCGGATTGCCAAAGAGGAGATTTTCGGGCCAGTGCAACCAATACTG
AAGTTCAAAAGTATCGAAGAAGTGATAAAAAGAGCGAATAGCACCGACTATGGACTCACA
GCAGCCGTGTTCACAAAAAATCTCGACAAAGCCCTGAAGTTGGCTTCTGCCTTAGAGTCT
GGAACGGTCTGGATCAACTGCTACAACGCCCTCTATGCACAGGCTCCATTTGGTGGCTTT
AAAATGTCAGGAAATGGCAGAGAACTAGGTGAATACGCTTTGGCCGAATACACAGAAGTG
AAAACTGTCACCATCAAACTTGGCGACAAGAACCCCTGA
Enzyme 4 GenBank Gene ID U07919 Link Image
Enzyme 4 GeneCard ID ALDH1A3 Link Image
Enzyme 4 GenAtlas ID ALDH1A3 Link Image
Enzyme 4 HGNC ID HGNC:409 Link Image
Enzyme 4 Chromosome Location 15
Enzyme 4 Locus 15q26.3
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. Hsu LC, Chang WC, Hiraoka L, Hsieh CL: Molecular cloning, genomic organization, and chromosomal localization of an additional human aldehyde dehydrogenase gene, ALDH6. Genomics. 1994 Nov 15;24(2):333-41. [PubMed Link Image]
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 5530
Enzyme 5 Name Aldehyde dehydrogenase, mitochondrial precursor
Enzyme 5 Synonyms
  1. ALDH class 2
  2. ALDHI
  3. ALDH-E2
Enzyme 5 Gene Name ALDH2
Enzyme 5 Protein Sequence >Aldehyde dehydrogenase, mitochondrial precursor 
MLRAAARFGPRLGRRLLSAAATQAVPAPNQQPEVFCNQIFINNEWHDAVSRKTFPTVNPS
TGEVICQVAEGDKEDVDKAVKAARAAFQLGSPWRRMDASHRGRLLNRLADLIERDRTYLA
ALETLDNGKPYVISYLVDLDMVLKCLRYYAGWADKYHGKTIPIDGDFFSYTRHEPVGVCG
QIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLTALYVANLIKEAGFPPGVVNIVPG
FGPTAGAAIASHEDVDKVAFTGSTEIGRVIQVAAGSSNLKRVTLELGGKSPNIIMSDADM
DWAVEQAHFALFFNQGQCCCAGSRTFVQEDIYDEFVERSVARAKSRVVGNPFDSKTEQGP
QVDETQFKKILGYINTGKQEGAKLLCGGGIAADRGYFIQPTVFGDVQDGMTIAKEEIFGP
VMQILKFKTIEEVVGRANNSTYGLAAAVFTKDLDKANYLSQALQAGTVWVNCYDVFGAQS
PFGGYKMSGSGRELGEYGLQAYTEVKTVTVKVPQKNS
Enzyme 5 Number of Residues 517
Enzyme 5 Molecular Weight 56382
Enzyme 5 Theoretical pI 7.05
Enzyme 5 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
Process
  • metabolism
  • physiological process
Component
—
Enzyme 5 General Function Energy production and conversion
Enzyme 5 Specific Function An aldehyde + NAD(+) + H(2)O = an acid + NADH
Enzyme 5 Pathways
Enzyme 5 Reactions
  • an aldehyde + NAD+ + H2O = an acid + NADH + H+
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • 1-24
Enzyme 5 Transmembrane Regions Not Available
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 28606 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID P05091 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name ALDH2_HUMAN Link Image
Enzyme 5 PDB ID 1OF7 Link Image
Enzyme 5 PDB File Show
Enzyme 5 3D Structure
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence >1551 bp 
ATGTTGCGCGCTGCCGCCGCTCGGGCCCCGCCTGGCCGCCGCCTCTTGTCAGCCGCCGCC
ACCCAGGCCGTGCCTGCCCCCAACCAGCAGCCCGAGGTCTTCTGCAACCAGATTTTCATA
AACAATGAATGGCACGATGCCGTCAGCAGGAAAACATTCCCCACCGTCAATCCGTCCACT
GGAGAGGTCATCTGTCAGGTAGCTGAAGGGGACAAGGAAGATGTGGACAAGGCACGTGAA
GGCCGCCCGGGCGCCTTCCAGCTGGGCTCACCTTGGCGCCGCATGGACGCATCACACAGC
GGCCGGCTGCTGAACCGCCTGGCCGATCTGATCGAGCGGGACCGGACCTACCTGGCGGCC
TTGGAGACCCTGGACAATGGCAAGCCCTATGTCATCTCCTACCTGGTGGATTTGGACATG
GTCCTCAAATGTCTCCGGTATTATGCCGGCTGGGCTGATAAGTACCACGGGAAAACCATC
CCCATTGACGGAGACTTCTTCAGCTACACACGCCATGAACCTGTGGGGGTGTGCGGGCAG
ATCATTCCGTGGAATTTCCCGCTCCTGATGCAAGCATGGAAGCTGGGCCCAGCCTTGGCA
ACTGGAAACGTGGTTGTGATGAAGGTAGCTGAGCAGACACCCCTCACCGCCCTCTATGTG
GCCAACCTGATCAAGGAGGCTGGCTTTCCCCCTGGTGTGGTCAACATTGTGCCTGGATTT
GGCCCCACGGCTGGGGCCGCCATTGCCTCCCATGAGGATGTGGACAAAGTGGCATTCACA
GGCTCCACTGAGATTGGCCGCGTAATCCAGGTTGCTGCTGGGAGCAGCAACCTCAAGAGA
GTGACCTTGGAGCTGGGGGGGAAGAGCCCCAACATCATCATGTCAGATGCCGATATGGAT
TGGGCCGTGGAACAGGCCCACTTCGCCCTGTTCTTCAACCAGGGCCAGTGCTGCTGTGCC
GGCTCCCGGACCTTCGTGCAGGAGGACATCTATGATGAGTTTGTGGTGCGGAGCGTTGCC
CGGGCCAAGTCTCGGGTGGTCGGGAACCCCTTTGATAGCAAGACCGAGCAGGGGCCGCAG
GTGGATGAAACTCAGTTTAAGAAGATCCTCGGCTACATCAACACGGGGAAGCAAGAGGGG
GCGAAGCTGCTGTGTGGTGGGGGCATTGCTGCTGACCGTGGTTACTTCATCCAGCCCACT
GTGTTTGGAGATGTGCAGGATGGCATGACCATCGCCAAGGAGGAGATCTTCGGGCCAGTG
ATGCAGATCCTGAAGTTCAAGACCATAGAGGAGGTTGTTGGGAGAGCCAACAATTCCACG
TACGGGCTGGCCGCAGCTGTCTTCACAAAGGATTTGGACAAGGCCAATTACCTGTCCCAG
GCCCTCCAGGCGGGCACTGTGTGGGTCAACTGCTATGATGTGTTTGGAGCCCAGTCACCC
TTTGGTGGCTACAAGATGTCGGGGAGTGGCCGGGAGTTGGGCGAGTACGGGCTGCAGGCA
TACACTGAAGTGAAAACTGTCACAGTCAAAGTGCCTCAGAAGAACTCATAA
Enzyme 5 GenBank Gene ID X05409 Link Image
Enzyme 5 GeneCard ID ALDH2 Link Image
Enzyme 5 GenAtlas ID ALDH2 Link Image
Enzyme 5 HGNC ID HGNC:404 Link Image
Enzyme 5 Chromosome Location 12
Enzyme 5 Locus 12q24.2
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References
  1. Braun T, Bober E, Singh S, Agarwal DP, Goedde HW: Evidence for a signal peptide at the amino-terminal end of human mitochondrial aldehyde dehydrogenase. FEBS Lett. 1987 May 11;215(2):233-6. [PubMed Link Image]
  2. Braun T, Bober E, Singh S, Agarwal DP, Goedde HW: Isolation and sequence analysis of a full length cDNA clone coding for human mitochondrial aldehyde dehydrogenase. Nucleic Acids Res. 1987 Apr 10;15(7):3179. [PubMed Link Image]
  3. Hsu LC, Bendel RE, Yoshida A: Genomic structure of the human mitochondrial aldehyde dehydrogenase gene. Genomics. 1988 Jan;2(1):57-65. [PubMed Link Image]
  4. Hempel J, Kaiser R, Jornvall H: Mitochondrial aldehyde dehydrogenase from human liver. Primary structure, differences in relation to the cytosolic enzyme, and functional correlations. Eur J Biochem. 1985 Nov 15;153(1):13-28. [PubMed Link Image]
  5. Hsu LC, Tani K, Fujiyoshi T, Kurachi K, Yoshida A: Cloning of cDNAs for human aldehyde dehydrogenases 1 and 2. Proc Natl Acad Sci U S A. 1985 Jun;82(11):3771-5. [PubMed Link Image]
  6. Yoshida A, Ikawa M, Hsu LC, Tani K: Molecular abnormality and cDNA cloning of human aldehyde dehydrogenases. Alcohol. 1985 Jan-Feb;2(1):103-6. [PubMed Link Image]
  7. Agarwal DP, Goedde HW: Human aldehyde dehydrogenase isozymes and alcohol sensitivity. Isozymes Curr Top Biol Med Res. 1987;16:21-48. [PubMed Link Image]
  8. Hempel J, Hoog JO, Jornvall H: Mitochondrial aldehyde dehydrogenase. Homology of putative targeting sequence to that of carbamyl phosphate synthetase I revealed by correlation of cDNA and protein data. FEBS Lett. 1987 Sep 28;222(1):95-8. [PubMed Link Image]
  9. Yoshida A, Huang IY, Ikawa M: Molecular abnormality of an inactive aldehyde dehydrogenase variant commonly found in Orientals. Proc Natl Acad Sci U S A. 1984 Jan;81(1):258-61. [PubMed Link Image]
  10. Novoradovsky A, Tsai SJ, Goldfarb L, Peterson R, Long JC, Goldman D: Mitochondrial aldehyde dehydrogenase polymorphism in Asian and American Indian populations: detection of new ALDH2 alleles. Alcohol Clin Exp Res. 1995 Oct;19(5):1105-10. [PubMed Link Image]
  11. Ni L, Zhou J, Hurley TD, Weiner H: Human liver mitochondrial aldehyde dehydrogenase: three-dimensional structure and the restoration of solubility and activity of chimeric forms. Protein Sci. 1999 Dec;8(12):2784-90. [PubMed Link Image]
Enzyme 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 5531
Enzyme 6 Name Fatty aldehyde dehydrogenase
Enzyme 6 Synonyms
  1. Aldehyde dehydrogenase, microsomal
  2. Aldehyde dehydrogenase family 3 member A2
  3. Aldehyde dehydrogenase 10
Enzyme 6 Gene Name ALDH3A2
Enzyme 6 Protein Sequence >Fatty aldehyde dehydrogenase 
MELEVRRVRQAFLSGRSRPLRFRLQQLEALRRMVQEREKDILTAIAADLCKSEFNVYSQE
VITVLGEIDFMLENLPEWVTAKPVKKNVLTMLDEAYIQPQPLGVVLIIGAWNYPFVLTIQ
PLIGAIAAGNAVIIKPSELSENTAKILAKLLPQYLDQDLYIVINGGVEETTELLKQRFDH
IFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQT
CIAPDYILCEASLQNQIVWKIKETVKEFYGENIKESPDYERIINLRHFKRILSLLEGQKI
AFGGETDEATRYIAPTVLTDVDPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLA
LYVFSHNHKLIKRMIDETSSGGVTGNDVIMHFTLNSFPFGGVGSSGMGAYHGKHSFDTFS
HQRPCLLKSLKREGANKLRYPPNSQSKVDWGKFFLLKRFNKEKLGLLLLTFLGIVAAVLV
KAEYY
Enzyme 6 Number of Residues 485
Enzyme 6 Molecular Weight 54849
Enzyme 6 Theoretical pI 7.99
Enzyme 6 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
Process
  • metabolism
  • physiological process
Component
—
Enzyme 6 General Function Energy production and conversion
Enzyme 6 Specific Function Catalyzes the oxidation of long-chain aliphatic aldehydes to fatty acids. Active on a variety of saturated and unsaturated aliphatic aldehydes between 6 and 24 carbons in length
Enzyme 6 Pathways
Enzyme 6 Reactions
  • an aldehyde + NAD+ + H2O = an acid + NADH + H+
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • None
Enzyme 6 Transmembrane Regions
  • 464-480
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 1082036 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID P51648 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name AL3A2_HUMAN Link Image
Enzyme 6 PDB ID Not Available
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence >1458 bp 
ATGGAGCTCGAAGTCCGGCGGGTCCGACAGGCGTTCCTGTCCGGCCGGTCGCGACCTCTG
CGGTTTCGGCTGCAGCAGCTGGAGGCCCTGCGGAGGATGGTGCAGGAGCGCGAGAAGGAT
ATCCTGACGGCCATCGCCGCCGACCTGTGCAAGAGTGAATTCAATGTGTACAGTCAGGAA
GTCATTACTGTCCTTGGGGAAATTGATTTTATGCTTGAGAATCTTCCTGAATGGGTTACT
GCTAAACCAGTTAAGAAGAACGTGCTCACCATGCTGGATGAGGCCTATATTCAGCCACAG
CCTCTGGGAGTGGTGCTGATAATCGGAGCTTGGAATTACCCCTTCGTTCTCACCATTCAG
CCACTGATAGGAGCCATCGCTGCAGGAAATGCTGTGATTATAAAGCCTTCTGAACTGAGT
GAAAATACAGCCAAGATCTTGGCAAAGCTTCTCCCTCAGTATTTAGACCAGGATCTCTAT
ATTGTTATTAATGGTGGTGTTGAGGAAACCACGGAGCTCCTGAAGCAGCGATTTGACCAC
ATTTTCTATACGGGAAACACTGCGGTTGGCAAAATTGTCATGGAAGCTGCTGCCAAGCAT
CTGACCCCTGTGACTCTTGAACTGGGAGGGAAAAGTCCATGTTATATTGATAAAGATTGT
GACCTGGACATTGTTTGCAGACGCATAACCTGGGGAAAATACATGAATTGTGGCCAAACC
TGCATTGCACCCGACTATATTCTCTGTGAAGCATCCCTCCAAAATCAAATTGTATGGAAG
ATTAAGGAAACAGTGAAGGAATTTTATGGAGAAAATATAAAAGAGTCTCCTGATTATGAA
AGGATCATCAATCTTCGTCATTTTAAGAGGATACTAAGTTTGCTTGAAGGACAAAAGATA
GCTTTTGGTGGGGAGACTGATGAGGCCACACGCTACATAGCCCCAACAGTACTTACCGAT
GTTGATCCTAAAACCAAGGTGATGCAAGAAGAAATTTTTGGACCAATTCTTCCAATAGTG
CCTGTGAAAAATGTAGATGAGGCCATAAATTTCATAAATGAACGTGAAAAGCCTCTGGCT
CTTTATGTATTTTCGCATAACCATAAGCTCATCAAACGGATGATTGATGAGACATCCAGT
GGAGGTGTCACAGGCAATGACGTCATTATGCACTTCACGCTCAACTCTTTCCCATTTGGA
GGAGTGGGTTCCAGTGGGATGGGAGCTTATCACGGAAAACATAGTTTTGATACTTTTTCT
CATCAGCGTCCCTGTTTATTAAAAAGTTTAAAGAGAGAAGGTGCTAACAAACTCAGATAT
CCTCCCAACAGCCAGTCAAAGGTGGATTGGGGGAAATTTTTTCTCTTGAAACGGTTCAAC
AAAGAAAAACTCGGTCTCCTGTTGCTCACTTTCCTGGGTATTGTAGCCGCTGTGCTTGTC
AAGGCAGAATATTACTGA
Enzyme 6 GenBank Gene ID L47162 Link Image
Enzyme 6 GeneCard ID ALDH3A2 Link Image
Enzyme 6 GenAtlas ID ALDH3A2 Link Image
Enzyme 6 HGNC ID HGNC:403 Link Image
Enzyme 6 Chromosome Location 17
Enzyme 6 Locus 17p11.2
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 General References
  1. De Laurenzi V, Rogers GR, Hamrock DJ, Marekov LN, Steinert PM, Compton JG, Markova N, Rizzo WB: Sjogren-Larsson syndrome is caused by mutations in the fatty aldehyde dehydrogenase gene. Nat Genet. 1996 Jan;12(1):52-7. [PubMed Link Image]
  2. Rogers GR, Markova NG, De Laurenzi V, Rizzo WB, Compton JG: Genomic organization and expression of the human fatty aldehyde dehydrogenase gene (FALDH). Genomics. 1997 Jan 15;39(2):127-35. [PubMed Link Image]
  3. Chang C, Yoshida A: Human fatty aldehyde dehydrogenase gene (ALDH10): organization and tissue-dependent expression. Genomics. 1997 Feb 15;40(1):80-5. [PubMed Link Image]
  4. Sillen A, Jagell S, Wadelius C: A missense mutation in the FALDH gene identified in Sjogren-Larsson syndrome patients originating from the northern part of Sweden. Hum Genet. 1997 Aug;100(2):201-3. [PubMed Link Image]
  5. Sillen A, Anton-Lamprecht I, Braun-Quentin C, Kraus CS, Sayli BS, Ayuso C, Jagell S, Kuster W, Wadelius C: Spectrum of mutations and sequence variants in the FALDH gene in patients with Sjogren-Larsson syndrome. Hum Mutat. 1998;12(6):377-84. [PubMed Link Image]
Enzyme 6 Metabolite References Not Available
Enzyme 7 [top]
Enzyme 7 ID 5532
Enzyme 7 Name Aldehyde dehydrogenase X, mitochondrial precursor
Enzyme 7 Synonyms
  1. Aldehyde dehydrogenase family 1 member B1
  2. ALDH class 2
Enzyme 7 Gene Name ALDH1B1
Enzyme 7 Protein Sequence >Aldehyde dehydrogenase X, mitochondrial precursor 
MLRFLAPRLLSLQGRTARYSSAAALPSPILNPDIPYNQLFINNEWQDAVSKKTFPTVNPT
TGEVIGHVAEGDRADVDRAVKAAREAFRLGSPWRRMDASERGRLLNLLADLVERDRVYLA
SLETLDNGKPFQESYALDLDEVIKVYRYFAGWADKWHGKTIPMDGQHFCFTRHEPVGVCG
QIIPWNFPLVMQGWKLAPALATGNTVVMKVAEQTPLSALYLASLIKEAGFPPGVVNIITG
YGPTAGAAIAQHMDVDKVAFTGSTEVGHLIQKAAGDSNLKRVTLELGGKSPSIVLADADM
EHAVEQCHEALFFNMGQCCCAGSRTFVEESIYNEFLERTVEKAKQRKVGNPFELDTQQGP
QVDKEQFERVLGYIQLGQKEGAKLLCGGERFGERGFFIKPTVFGGVQDDMRIAKEEIFGP
VQPLFKFKKIEEVVERANNTRYGLAAAVFTRDLDKAMYFTQALQAGTVWVNTYNIVTCHT
PFGGFKESGNGRELGEDGLKAYTEVKTVTIKVPQKNS
Enzyme 7 Number of Residues 517
Enzyme 7 Molecular Weight 57239
Enzyme 7 Theoretical pI 6.79
Enzyme 7 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
Process
  • metabolism
  • physiological process
Component
—
Enzyme 7 General Function Energy production and conversion
Enzyme 7 Specific Function ALDHs play a major role in the detoxification of alcohol-derived acetaldehyde. They are involved in the metabolism of corticosteroids, biogenic amines, neurotransmitters, and lipid peroxidation
Enzyme 7 Pathways
Enzyme 7 Reactions
  • an aldehyde + NAD+ + H2O = an acid + NADH + H+
Enzyme 7 Pfam Domain Function
Enzyme 7 Signals
  • 1-22
Enzyme 7 Transmembrane Regions Not Available
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein 1263008 Link Image
Enzyme 7 UniProtKB/Swiss-Prot ID P30837 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name AL1B1_HUMAN Link Image
Enzyme 7 PDB ID Not Available
Enzyme 7 Cellular Location Not Available
Enzyme 7 Gene Sequence >1554 bp 
ATGCTGCGCTTCCTGGCACCCCGGCTGCTTAGCCTCCAGGGCAGGACCGCCCTCTACTCC
TCGGCAGCAGCCCTCCCAAGCCCCATTCTGAACCCAGACATCCCCTACAACCAGCTGTTC
ATCAACAATGAATGGCAAGATGCAGTCAGCAAGAAGACCTTCCCGACGGTCAACCCTACC
ACCGGGGAGGTCATCGGGCACGTGGCTGAAGGTGACCGGGCTGATGTGGATCGGGCCGTG
AAAGCAGCCCGGGAAGCCTTCCGCCTGGGGTCCCCATGGCGCCGGATGGATGCCTCTGAG
CGGGGCCGGCTGCTGAACCTCCTGGCAGACCTAGTGGAGCGGGATCGAGTCTACTTGGCC
TCACTCGAGACCTTGGACAATGGGAAGCCTTTCCAAGAGTCTTACGCCTTGGACTTGGAT
GAGGTCATCAAGGTGTATCGGTACTTTGCTGGCTGGGCTGACAAGTGGCATGGCAAGACC
ATCCCCATGCATGGCCAGCATTTCTGCTTCACCCGGCATGAGCCCGTTGGTGTCTGTGGC
CAGATCATCCCGTGGAACTTCCCCTTGGTCATGCAGGGTTGGAAACTTGCCCCGGCACTC
GCCACAGGCAACACTGTGGTTATGAAGGTGGCAGAGCAGACCCCCCTCTCTGCCCTGTAT
TTGGCCTCCCTCATCAAGGAGGCAGGCTTTCCCCCTGGGGTGGTGAACATCATCACGGGG
TATGGCCCAACAGCAGGTGCGGCCATCGCCCAGCACATGGATGTTGACAAAGTTGCCTTC
ACCGGTTCCACCGAGGTGGGCCACCTGATCCAGAAAGCAGCTGGCGATTCCAACCTCAAG
AGAGTCACCCTGGAGCTGGGTGGTAAGAGCCCCAGCATCGTGCTGGCCGATGCTGACATG
GAGCATGCCGTGGAGCAGTGCCACGAAGCCCTGTTCTTCAACATGGGCCAGTGCTGCTGT
GCTGGCTCCCGGACCTTCGTGGAAGAATCCATCTACAATGAGTTTCTCGAGAGAACCGTG
GAGAAAGCAAAGCAGAGGAAAGTGGGGAACCCCTTTGAGCTGGACACCCAGCAGGGGCCT
CAGGTGGACAAGGAGCAGTTTGAACGAGTCCTAGGCTACATCCAGCTTGGCCAGAAGGAG
GGCGCAAAACTCCTCTGTGGCGGAGAGCGTTTCGGGGAGCGTGGTTTCTTCATCAAGCCT
ACTGTCTTTGGTGGCGTGCAGGATGACATGAGAATTGCCAAAGAGGAGATCTTTGGGCCT
GTGCAGCCCCTGTTCAAGTTCAAGAAGATTGAGGAGGTGGTTGAGAGGGCCAACAACACC
AGGTATGGCCTGGCTGCGGCTGTGTTCACCCGGGATCTGGACAAGGCCATGTACTTCACC
CAGGCACTCCAGGCCGGGACCGTGTGGGTAAACACCTACAACATCGTCACCTGCCACACG
CCATTTGGAGGGTTTAAGGAATCTGGAAACGGGAGGGAGCTGGGTGAGGATGGGCTTAAG
GCCTACACAGAGGTAAAGACGGTCACCATCAAGGTTCCTCAGAAGAACTCGTAA
Enzyme 7 GenBank Gene ID M63967 Link Image
Enzyme 7 GeneCard ID ALDH1B1 Link Image
Enzyme 7 GenAtlas ID ALDH1B1 Link Image
Enzyme 7 HGNC ID HGNC:407 Link Image
Enzyme 7 Chromosome Location 9
Enzyme 7 Locus 9p11.1
Enzyme 7 SNPs SNPJam Report Link Image
Enzyme 7 General References
  1. Hsu LC, Chang WC: Cloning and characterization of a new functional human aldehyde dehydrogenase gene. J Biol Chem. 1991 Jul 5;266(19):12257-65. [PubMed Link Image]
  2. Sherman D, Dave V, Hsu LC, Peters TJ, Yoshida A: Diverse polymorphism within a short coding region of the human aldehyde dehydrogenase-5 (ALDH5) gene. Hum Genet. 1993 Nov;92(5):477-80. [PubMed Link Image]
Enzyme 7 Metabolite References Not Available
Enzyme 8 [top]
Enzyme 8 ID 5713
Enzyme 8 Name Beta-Ala-His dipeptidase precursor
Enzyme 8 Synonyms
  1. Carnosine dipeptidase 1
  2. CNDP dipeptidase 1
  3. Serum carnosinase
  4. Glutamate carboxypeptidase-like protein 2
Enzyme 8 Gene Name CNDP1
Enzyme 8 Protein Sequence >Beta-Ala-His dipeptidase precursor 
MDPKLGRMAASLLAVLLLLLERGMFSSPSPPPALLEKVFQYIDLHQDEFVQTLKEWVAIE
SDSVQPVPRFRQELFRMMAVAADTLQRLGARVASVDMGPQQLPDGQSLPIPPVILAELGS
DPTKGTVCFYGHLDVQPADRGDGWLTDPYVLTEVDGKLYGRGATDNKGPVLAWINAVSAF
RALEQDLPVNIKFIIEGMEEAGSVALEELVEKEKDRFFSGVDYIVISDNLWISQRKPAIT
YGTRGNSYFMVEVKCRDQDFHSGTFGGILHEPMADLVALLGSLVDSSGHILVPGIYDEVV
PLTEEEINTYKAIHLDLEEYRNSSRVEKFLFDTKEEILMHLWRYPSLSIHGIEGAFDEPG
TKTVIPGRVIGKFSIRLVPHMNVSAVEKQVTRHLEDVFSKRNSSNKMVVSMTLGLHPWIA
NIDDTQYLAAKRAIRTVFGTEPDMIRDGSTIPIAKMFQEIVHKSVVLIPLGAVDDGEHSQ
NEKINRWNYIEGTKLFAAFFLEMAQLH
Enzyme 8 Number of Residues 507
Enzyme 8 Molecular Weight 56693
Enzyme 8 Theoretical pI 4.95
Enzyme 8 GO Classification
Function
  • binding
  • catalytic activity
  • hydrolase activity
  • metallopeptidase activity
  • peptidase activity
  • protein binding
  • protein dimerization activity
Process
  • cellular protein metabolism
  • macromolecule metabolism
  • metabolism
  • physiological process
  • protein metabolism
  • proteolysis
Component
—
Enzyme 8 General Function Amino acid transport and metabolism
Enzyme 8 Specific Function Preferential hydrolysis of the beta-Ala-|-His dipeptide (carnosine), and also anserine, Xaa-|-His dipeptides and other dipeptides including homocarnosine
Enzyme 8 Pathways
Enzyme 8 Reactions
  • Preferential hydrolysis of the beta-Ala-|-His dipeptide (carnosine), and also anserine, Xaa-|-His dipeptides and other dipeptides including homocarnosine
Enzyme 8 Pfam Domain Function
Enzyme 8 Signals
  • 1-26
Enzyme 8 Transmembrane Regions Not Available
Enzyme 8 Essentiality Not Available
Enzyme 8 GenBank ID Protein 16555792 Link Image
Enzyme 8 UniProtKB/Swiss-Prot ID Q96KN2 Link Image
Enzyme 8 UniProtKB/Swiss-Prot Entry Name CNDP1_HUMAN Link Image
Enzyme 8 PDB ID Not Available
Enzyme 8 Cellular Location Not Available
Enzyme 8 Gene Sequence >1527 bp 
ATGGATCCCAAACTCGGGAGAATGGCTGCGTCCCTGCTGGCTGTGCTGCTGCTGCTGCTG
CTGGAGCGCGGCATGTTCTCCTCACCCTCCCCGCCCCCGGCGCTGTTAGAGAAAGTCTTC
CAGTACATTGACCTCCATCAGGATGAATTTGTGCAGACGCTGAAGGAGTGGGTGGCCATC
GAGAGCGACTCTGTCCAGCCTGTGCCTCGCTTCAGACAAGAGCTCTTCAGAATGATGGCC
GTGGCTGCGGACACGCTGCAGCGCCTGGGGGCCCGTGTGGCCTCGGTGGACATGGGTCCT
CAGCAGCTGCCCGATGGTCAGAGTCTTCCAATACCTCCCGTCATCCTGGCCGAACTGGGG
AGCGATCCCACGAAAGGCACCGTGTGCTTCTACGGCCACTTGGACGTGCAGCCTGCTGAC
CGGGGCGATGGGTGGCTCACGGACCCCTATGTGCTGACGGAGGTAGGCGGGAAACTTTAT
GGACGAGGAGCGACCGACAACAAAGGCCCTGTCTTGGCTTGGATCAATGCTGTGAGCGCC
TTCAGAGCCCTGGAGCAAGATCTTCCTGTGAATATCAAATTCATCATTGAGGGGATGGAA
GAGGCTGGCTCTGTTGCCCTGGAGGAACTTGTGGAAAAAGAAAAGGACCGATTCTTCTCT
GGTGTGGACTACATTGTAATTTCAGATAACCTGTGGATCAGCCAAAGGAAGCTAGCAATC
ACTTACGGAACCCGGGGGAACAGCTACTTCATGGTGGAGGTGAAATGCAGAGACCAGGAT
TTTCACTCAGGAACCTTTGGTGGCATCCTTCATGAACTAATGGCTGATCTGGTTGCTCTT
CTCGGTAGCCTGGTAGACTCGTCTGGTCATATCCTGGTCCCTGGAATCTATGATGAAGTG
GTTCCTCTTACAGAAGAGGAAATAAATACATACAAAGCCATCCATCTAGACCTAGAAGAA
TACCGGAATAGCAGCCGGGTTGAGAAATTTCTGTTCGATACTAAGGAGGAGATTCTAATG
CACCTCTGGAGGTACCCATCTCTTTCTATTCATGGGATCGAGGGCGCGTTTGATGAGCCT
GGAACTAAAACAGTCATACCTGGCCGAGTTATAGGAAAATTTTCAATCCGTCTAGTCCCT
CACATGAATGTGTCTGCGGTGGAAAAACAGGTGACACGACATCTTGAAGATGTGTTCTCC
AAAAGAAATAGTTCCAACAAGATGGTTGTTTCCATGACTCTAGGACTACACCCGTGGATT
GCAAATATTGATGACACTCAGTATCTCGCAGCAAAAAGAGCGATCAGAACAGTGTTTGGA
ACAGAACCAGATATGATCCGGGATGGATCCACCATTCCAATTGCCAAAATGTTCCAGGAG
ATCGTCCACAAGAGCGTGGTGCTAATTCCGCTGGGAGCTGTTGATGATGGAGAACATTCG
CAGAATGAGAAAATCAACAGGTGGAACTACATAGAGGGAACCAAATTATTTGCTGCCTTT
TTCTTAGAGATGGCCCAGCTCCATTAA
Enzyme 8 GenBank Gene ID AJ417564 Link Image
Enzyme 8 GeneCard ID CNDP1 Link Image
Enzyme 8 GenAtlas ID CNDP1 Link Image
Enzyme 8 HGNC ID HGNC:20675 Link Image
Enzyme 8 Chromosome Location 18
Enzyme 8 Locus 18q22.3
Enzyme 8 SNPs SNPJam Report Link Image
Enzyme 8 General References
  1. Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed Link Image]
Enzyme 8 Metabolite References Not Available
Enzyme 9 [top]
Enzyme 9 ID 5815
Enzyme 9 Name Beta-ureidopropionase
Enzyme 9 Synonyms
  1. Beta-alanine synthase
  2. N- carbamoyl-beta-alanine amidohydrolase
  3. BUP-1
Enzyme 9 Gene Name UPB1
Enzyme 9 Protein Sequence >Beta-ureidopropionase 
MAGAEWKSLEECLEKHLPLPDLQEVKRVLYGKELRKLDLPREAFEAASREDFELQGYAFE
AAEEQLRRPRIVHVGLVQNRIPLPANAPVAEQVSALHRRIKAIVEVAAMCGVNIICFQEA
WTMPFAFCTREKLPWTEFAESAEDGPTTRFCQKLAKNHDMVVVSPILERDSEHGDVLWNT
AVVISNSGAVLGKTRKNHIPRVGDFNESTYYMEGNLGHPVFQTQFGRIAVNICYGRHHPL
NWLMYSINGAEIIFNPSATIGALSESLWPIEARNAAIANHCFTCAINRVGTEHFPNEFTS
GDGKKAHQDFGYFYGSSYVAAPDSSRTPGLSRSRDGLLVAKLDLNLCQQVNDVWNFKMTG
RYEMYARELAEAVKSNYSPTIVKE
Enzyme 9 Number of Residues 384
Enzyme 9 Molecular Weight 43166
Enzyme 9 Theoretical pI 6.51
Enzyme 9 GO Classification
Function
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
Process
  • metabolism
  • nitrogen compound metabolism
  • physiological process
Component
—
Enzyme 9 General Function Not Available
Enzyme 9 Specific Function Converts N-carbamyl-beta-aminoisobutyric acid and N- carbamyl-beta-alanine to, respectively, beta-aminoisobutyric acid and beta-alanine, ammonia and carbon dioxide
Enzyme 9 Pathways
Enzyme 9 Reactions
  • N-carbamoyl-beta-alanine + H2O = beta-alanine + CO2 + NH3
Enzyme 9 Pfam Domain Function
Enzyme 9 Signals
  • None
Enzyme 9 Transmembrane Regions
  • None
Enzyme 9 Essentiality Not Available
Enzyme 9 GenBank ID Protein 6288771 Link Image
Enzyme 9 UniProtKB/Swiss-Prot ID Q9UBR1 Link Image
Enzyme 9 UniProtKB/Swiss-Prot Entry Name BUP1_HUMAN Link Image
Enzyme 9 PDB ID Not Available
Enzyme 9 Cellular Location Not Available
Enzyme 9 Gene Sequence >1155 bp 
ATGGCGGGCGCTGAGTGGAAGTCGCTGGAGGAATGCTTGGAGAAGCACCTGCCGCTCCCC
GACTTGCAGGAAGTGAAGCGCGTTCTCTATGGCAAGGAACTCAGGAAGCTTGATCTGCCC
AGGGAAGCTTTCGAAGCTGCCTCCAGAGAAGACTTTGAACTGCAGGGATATGCCTTTGAA
GCAGCGGAGGAGCAGCTGAGACGACCCCGCATTGTGCACGTGGGGCTGGTTCAGAACAGA
ATCCCCCTCCCCGCAAATGCCCCTGTGGCAGAACAGGTCTCTGCCCTTCATAGACGCATA
AAGGCTATCGTAGAGGTGGCTGCAATGTGTGGAGTCAACATCATCTGTTTCCAGGAAGCA
TGGACTATGCCCTTTGCCTTCTGTACGAGAGAGAAGCTTCCTTGGACAGAATTTGCTGAG
TCAGCAGAGGATGGGCCCACCACCAGATTCTGTCAGAAGCTGGCGAAGAACCATGACATG
GTGGTGGTGTCTCCCATCCTGGAACGAGACAGCGAGCATGGGGATGTTTTGTGGAATACA
GCCGTGGTGATCTCCAATTCCGGAGCAGTCCTGGGAAAGACCAGGAAAAACCACATCCCC
AGAGTGGGTGATTTCAACGAGTCAACTTACTACATGGAGGGAAACCTGGGCCACCCCGTG
TTCCAGACGCAGTTCGGAAGGATCGCGGTGAACATTTGCTACGGGCGGCACCACCCCCTC
AACTGGCTTATGTACAGCATCAACGGGGCTGAGATCATCTTCAACCCCTCGGCCACGATA
GGAGCACTCAGCGAGTCCCTGTGGCCCATCGAGGCCAGAAACGCAGCCATTGCCAATCAC
TGCTTCACCTGCGCCATCAATCGAGTGGGCACCGAGCACTTCCCGAACGAGTTTACCTCG
GGAGATGGAAAGAAAGCTCACCAGGACTTTGGCTACTTTTATGGCTCGAGCTATGTGGCA
GCCCCTGACAGCAGCCGGACTCCTGGGCTGTCCCGTAGCCGGGATGGACTGCTAGTTGCT
AAGCTCGACCTAAACCTCTGCCAGCAGGTGAATGATGTCTGGAACTTCAAGATGACGGGC
AGGTATGAGATGTACGCACGGGAGCTCGCCGAAGCTGTCAAGTCCAACTACAGCCCCACC
ATCGTGAAAGAGTAG
Enzyme 9 GenBank Gene ID AF163312 Link Image
Enzyme 9 GeneCard ID UPB1 Link Image
Enzyme 9 GenAtlas ID UPB1 Link Image
Enzyme 9 HGNC ID HGNC:16297 Link Image
Enzyme 9 Chromosome Location 22
Enzyme 9 Locus 22q11.2
Enzyme 9 SNPs SNPJam Report Link Image
Enzyme 9 General References
  1. Vreken P, van Kuilenburg AB, Hamajima N, Meinsma R, van Lenthe H, Gohlich-Ratmann G, Assmann BE, Wevers RA, van Gennip AH: cDNA cloning, genomic structure and chromosomal localization of the human BUP-1 gene encoding beta-ureidopropionase. Biochim Biophys Acta. 1999 Oct 28;1447(2-3):251-7. [PubMed Link Image]
  2. Sakamoto T, Sakata SF, Matsuda K, Horikawa Y, Tamaki N: Expression and properties of human liver beta-ureidopropionase. J Nutr Sci Vitaminol (Tokyo). 2001 Apr;47(2):132-8. [PubMed Link Image]
Enzyme 9 Metabolite References Not Available
Enzyme 10 [top]
Enzyme 10 ID 5975
Enzyme 10 Name Glutamate decarboxylase 2
Enzyme 10 Synonyms
  1. Glutamate decarboxylase 65 kDa isoform
  2. GAD-65
  3. 65 kDa glutamic acid decarboxylase
Enzyme 10 Gene Name GAD2
Enzyme 10 Protein Sequence >Glutamate decarboxylase 2 
MASPGSGFWSFGSEDGSGDSENPGTARAWCQVAQKFTGGIGNKLCALLYGDAEKPAESGG
SQPPRAAARKAACACDQKPCSCSKVDVNYAFLHATDLLPACDGERPTLAFLQDVMNILLQ
YVVKSFDRSTKVIDFHYPNELLQEYNWELADQPQNLEEILMHCQTTLKYAIKTGHPRYFN
QLSTGLDMVGLAADWLTSTANTNMFTYEIAPVFVLLEYVTLKKMREIIGWPGGSGDGIFS
PGGAISNMYAMMIARFKMFPEVKEKGMAALPRLIAFTSEHSHFSLKKGAAALGIGTDSVI
LIKCDERGKMIPSDLERRILEAKQKGFVPFLVSATAGTTVYGAFDPLLAVADICKKYKIW
MHVDAAWGGGLLMSRKHKWKLSGVERANSVTWNPHKMMGVPLQCSALLVREEGLMQNCNQ
MHASYLFQQDKHYDLSYDTGDKALQCGRHVDVFKLWLMWRAKGTTGFEAHVDKCLELAEY
LYNIIKNREGYEMVFDGKPQHTNVCFWYIPPSLRTLEDNEERMSRLSKVAPVIKARMMEY
GTTMVSYQPLGDKVNFFRMVISNPAATHQDIDFLIEEIERLGQDL
Enzyme 10 Number of Residues 585
Enzyme 10 Molecular Weight 65412
Enzyme 10 Theoretical pI 6.89
Enzyme 10 GO Classification
Function
  • carbon-carbon lyase activity
  • carboxy-lyase activity
  • catalytic activity
  • lyase activity
Process
  • amino acid and derivative metabolism
  • amino acid metabolism
  • cellular metabolism
  • metabolism
  • physiological process
Component
—
Enzyme 10 General Function Amino acid transport and metabolism
Enzyme 10 Specific Function Catalyzes the production of GABA
Enzyme 10 Pathways
Enzyme 10 Reactions
  • L-glutamate = 4-aminobutanoate + CO2
Enzyme 10 Pfam Domain Function
Enzyme 10 Signals
  • None
Enzyme 10 Transmembrane Regions
  • None
Enzyme 10 Essentiality Not Available
Enzyme 10 GenBank ID Protein 182934 Link Image
Enzyme 10 UniProtKB/Swiss-Prot ID Q05329 Link Image
Enzyme 10 UniProtKB/Swiss-Prot Entry Name DCE2_HUMAN Link Image
Enzyme 10 PDB ID Not Available
Enzyme 10 Cellular Location Not Available
Enzyme 10 Gene Sequence >1758 bp 
ATGGCATCTCCGGGCTCTGGCTTTTGGTCTTTCGGGTCGGAAGATGGCTCTGGGGATTCC
GAGAATCCCGGCACAGCGCGAGCCTGGTGCCAAGTGGCTCAGAAGTTCACGGGCGGCATC
GGAAACAAACTGTGCGCCCTGCTCTACGGAGACGCCGAGAAGCCGGCGGAGAGCGGCGGG
AGCCAACCCCCGCGGGCCGCCGCCCGGAAGGCCGCCTGCGCCTGCGACCAGAAGCCCTGC
AGCTGCTCCAAAGTGGATGTCAACTACGCGTTTCTCCATGCAACAGACCTGCTGCCGGCG
TGTGATGGAGAAAGGCCCACTTTGGCGTTTCTGCAAGATGTTATGAACATTTTACTTCAG
TATGTGGTGAAAAGTTTCGATAGATCAACCAAAGTGATTGATTTCCATTATCCTAATGAG
CTTCTCCAAGAATATAATTGGGAATTGGCAGACCAACCACAAAATTTGGAGGAAATTTTG
ATGCATTGCCAAACAACTCTAAAATATGCAATTAAAACAGGGCATCCTAGATACTTCAAT
CAACTTTCTACTGGTTTGGATATGGTTGGATTAGCAGCAGACTGGCTGACATCAACAGCA
AATACTAACATGTTCACCTATGAAATTGCTCCAGTATTTGTGCTTTTGGAATATGTCACA
CTAAAGAAAATGAGAGAAATCATTGGCTGGCCAGGGGGCTCTGGCGATGGGATATTTTCT
CCCGGTGGCGCCATATCTAACATGTATGCCATGATGATCGCACGCTTTAAGATGTTCCCA
GAAGTCAAGGAGAAAGGAATGGCTGCTCTTCCCAGGCTCATTGCCTTCACGTCTGAACAT
AGTCATTTTTCTCTCAAGAAGGGAGCTGCAGCCTTAGGGATTGGAACAGACAGCGTGATT
CTGATTAAATGTGATGAGAGAGGGAAAATGATTCCATCTGATCTTGAAAGAAGGATTCTT
GAAGCCAAACAGAAAGGGTTTGTTCCTTTCCTCGTGAGTGCCACAGCTGGAACCACCGTG
TACGGAGCATTTGACCCCCTCTTAGCTGTCGCTGACATTTGCAAAAAGTATAAGATCTGG
ATGCATGTGGATGCAGCTTGGGGTGGGGGATTACTGATGTCCCGAAAACACAAGTGGAAA
CTGAGTGGCGTGGAGAGGGCCAACTCTGTGACGTGGAATCCACACAAGATGATGGGAGTC
CCTTTGCAGTGCTCTGCTCTCCTGGTTAGAGAAGAGGGATTGATGCAGAATTGCAACCAA
ATGCATGCCTCCTACCTCTTTCAGCAAGATAAACATTATGACCTGTCCTATGACACTGGA
GACAAGGCCTTACAGTGCGGACGCCACGTTGATGTTTTTAAACTATGGCTGATGTGGAGG
GCAAAGGGGACTACCGGGTTTGAAGCGCATGTTGATAAATGTTTGGAGTTGGCAGAGTAT
TTATACAACATCATAAAAAACCGAGAAGGATATGAGATGGTGTTTGATGGGAAGCCTCAG
CACACAAATGTCTGCTTCTGGTACATTCCTCCAAGCTTGCGTACTCTGGAAGACAATGAA
GAGAGAATGAGTCGCCTCTCGAAGGTGGCTCCAGTGATTAAAGCCAGAATGATGGAGTAT
GGAACCACAATGGTCAGCTACCAACCCTTGGGAGACAAGGTCAATTTCTTCCGCATGGTC
ATCTCAAACCCAGCGGCAACTCACCAAGACATTGACTTCCTGATTGAAGAAATAGAACGC
CTTGGACAAGATTTATAA
Enzyme 10 GenBank Gene ID M81882 Link Image
Enzyme 10 GeneCard ID GAD2 Link Image
Enzyme 10 GenAtlas ID GAD2 Link Image
Enzyme 10 HGNC ID HGNC:4093 Link Image
Enzyme 10 Chromosome Location 10
Enzyme 10 Locus 10p11.23
Enzyme 10 SNPs SNPJam Report Link Image
Enzyme 10 General References
  1. Karlsen AE, Hagopian WA, Grubin CE, Dube S, Disteche CM, Adler DA, Barmeier H, Mathewes S, Grant FJ, Foster D, et al.: Cloning and primary structure of a human islet isoform of glutamic acid decarboxylase from chromosome 10. Proc Natl Acad Sci U S A. 1991 Oct 1;88(19):8337-41. [PubMed Link Image]
  2. Bu DF, Erlander MG, Hitz BC, Tillakaratne NJ, Kaufman DL, Wagner-McPherson CB, Evans GA, Tobin AJ: Two human glutamate decarboxylases, 65-kDa GAD and 67-kDa GAD, are each encoded by a single gene. Proc Natl Acad Sci U S A. 1992 Mar 15;89(6):2115-9. [PubMed Link Image]
  3. Bu DF, Tobin AJ: The exon-intron organization of the genes (GAD1 and GAD2) encoding two human glutamate decarboxylases (GAD67 and GAD65) suggests that they derive from a common ancestral GAD. Genomics. 1994 May 1;21(1):222-8. [PubMed Link Image]
  4. Mauch L, Abney CC, Berg H, Scherbaum WA, Liedvogel B, Northemann W: Characterization of a linear epitope within the human pancreatic 64-kDa glutamic acid decarboxylase and its autoimmune recognition by sera from insulin-dependent diabetes mellitus patients. Eur J Biochem. 1993 Mar 1;212(2):597-603. [PubMed Link Image]
  5. Kim J, Richter W, Aanstoot HJ, Shi Y, Fu Q, Rajotte R, Warnock G, Baekkeskov S: Differential expression of GAD65 and GAD67 in human, rat, and mouse pancreatic islets. Diabetes. 1993 Dec;42(12):1799-808. [PubMed Link Image]
  6. Namchuk M, Lindsay L, Turck CW, Kanaani J, Baekkeskov S: Phosphorylation of serine residues 3, 6, 10, and 13 distinguishes membrane anchored from soluble glutamic acid decarboxylase 65 and is restricted to glutamic acid decarboxylase 65alpha. J Biol Chem. 1997 Jan 17;272(3):1548-57. [PubMed Link Image]
  7. Kanaani J, el-Husseini Ael-D, Aguilera-Moreno A, Diacovo JM, Bredt DS, Baekkeskov S: A combination of three distinct trafficking signals mediates axonal targeting and presynaptic clustering of GAD65. J Cell Biol. 2002 Sep 30;158(7):1229-38. [PubMed Link Image]
Enzyme 10 Metabolite References Not Available
Enzyme 11 [top]
Enzyme 11 ID 7966
Enzyme 11 Name Hypothetical protein GAD1
Enzyme 11 Synonyms Not Available
Enzyme 11 Gene Name GAD1
Enzyme 11 Protein Sequence >Hypothetical protein GAD1 
MASSTPSSSATSSNAGADPNTTNLRPTTYDTWCGVAHGCTRKLGLKICGFLQRTNSLEEK
SRLVSAFKERQSSKNLLSCENSDRDARFRRTETDFSNLFARDLLPAKNGEEQTVQFLLEV
VDILLNYVRKTFDRSTKVLDFHHPHQLLEGMEGFNLELSDHPESLEQILVDCRDTLKYGV
RTGHPRFFNQLSTGLDIIGLAGEWLTSTANTNMFTYEIAPVFVLMEQITLKKMREIVGWS
SKDGDGIFSPGGAISNMYSIMAARYKYFPEVKTKGMAAVPKLVLFTSEQSHYSIKKAGAA
LGFGTDNVILIKCNERGKIIPADFEAKILEAKQKGYVPFYVNATAGTTVYGAFDPIQEIA
DICEKYNLWLHVDAAWGGGLLMSRKHRHKLNGIERANSVTWNPHKMMGVLLQCSAILVKE
KGILQGCNQMCAGYLFQPDKQYDVSYDTGDKAIQCGRHVDIFKFWLMWKAKGTVGFENQI
NKCLELAEYLYAKIKNREEFEMVFNGEPEHTNVCFWYIPQSLRGVPDSPQRREKLHKVAP
KIKALMMESGTTMVGYQPQGDKANFFRMVISNPAATQSDIDFLIEEIERLGQDL
Enzyme 11 Number of Residues 594
Enzyme 11 Molecular Weight 66897
Enzyme 11 Theoretical pI 7.67
Enzyme 11 GO Classification
Function
  • carbon-carbon lyase activity
  • carboxy-lyase activity
  • catalytic activity
  • lyase activity
Process
  • amino acid and derivative metabolism
  • amino acid metabolism
  • cellular metabolism
  • metabolism
  • physiological process
Component
—
Enzyme 11 General Function Amino acid transport and metabolism
Enzyme 11 Specific Function Not Available
Enzyme 11 Pathways Not Available
Enzyme 11 Reactions Not Available
Enzyme 11 Pfam Domain Function
Enzyme 11 Signals
  • None
Enzyme 11 Transmembrane Regions
  • None
Enzyme 11 Essentiality Not Available
Enzyme 11 GenBank ID Protein 62988850 Link Image
Enzyme 11 UniProtKB/Swiss-Prot ID Q53TQ7 Link Image
Enzyme 11 UniProtKB/Swiss-Prot Entry Name Q53TQ7_HUMAN Link Image
Enzyme 11 PDB ID Not Available
Enzyme 11 Cellular Location Not Available
Enzyme 11 Gene Sequence >1785 bp 
ATGGCGTCTTCGACCCCATCTTCGTCCGCAACCTCCTCGAACGCGGGAGCGGACCCCAAT
ACCACTAACCTGCGCCCCACAACGTACGATACCTGGTGCGGCGTGGCCCATGGATGCACC
AGAAAACTGGGGCTCAAGATCTGCGGCTTCTTGCAAAGGACCAACAGCCTGGAAGAGAAG
AGTCGCCTTGTGAGTGCCTTCAAGGAGAGGCAATCCTCCAAGAACCTGCTTTCCTGTGAA
AACAGCGACCGGGATGCCCGCTTCCGGCGCACAGAGACTGACTTCTCTAATCTGTTTGCT
AGAGATCTGCTTCCGGCTAAGAACGGTGAGGAGCAAACCGTGCAATTCCTCCTGGAAGTG
GTGGACATACTCCTCAACTATGTCCGCAAGACATTTGATCGCTCCACCAAGGTGCTGGAC
TTTCATCACCCACACCAGTTGCTGGAAGGCATGGAGGGCTTCAACTTGGAGCTCTCTGAC
CACCCCGAGTCCCTGGAGCAGATCCTGGTTGACTGCAGAGACACCTTGAAGTATGGGGTT
CGCACAGGTCATCCTCGATTTTTCAACCAGCTCTCCACTGGATTGGATATTATTGGCCTA
GCTGGAGAATGGCTGACATCAACGGCCAATACCAACATGTTTACATATGAAATTGCACCA
GTGTTTGTCCTCATGGAACAAATAACACTTAAGAAGATGAGAGAGATAGTTGGATGGTCA
AGTAAAGATGGTGATGGGATATTTTCTCCTGGGGGCGCCATATCCAACATGTACAGCATC
ATGGCTGCTCGCTACAAGTACTTCCCGGAAGTTAAGACAAAGGGCATGGCGGCTGTGCCT
AAACTGGTCCTCTTCACCTCAGAACAGAGTCACTATTCCATAAAGAAAGCTGGGGCTGCA
CTTGGCTTTGGAACTGACAATGTGATTTTGATAAAGTGCAATGAAAGGGGGAAAATAATT
CCAGCTGATTTTGAGGCAAAAATTCTTGAAGCCAAACAGAAGGGATATGTTCCCTTTTAT
GTCAATGCAACTGCTGGCACGACTGTTTATGGAGCTTTTGATCCGATACAAGAGATTGCA
GATATATGTGAGAAATATAACCTTTGGTTGCATGTCGATGCTGCCTGGGGAGGTGGGCTG
CTCATGTCCAGGAAGCACCGCCATAAACTCAACGGCATAGAAAGGGCCAACTCAGTCACC
TGGAACCCTCACAAGATGATGGGCGTGCTGTTGCAGTGCTCTGCCATTCTCGTCAAGGAA
AAGGGTATACTCCAAGGATGCAACCAGATGTGTGCAGGATACCTCTTCCAGCCAGACAAG
CAGTATGATGTCTCCTACGACACCGGGGACAAGGCAATTCAGTGTGGCCGCCACGTGGAT
ATCTTCAAGTTCTGGCTGATGTGGAAAGCAAAGGGCACAGTGGGATTTGAAAACCAGATC
AACAAATGCCTGGAACTGGCTGAATACCTCTATGCCAAGATTAAAAACAGAGAAGAATTT
GAGATGGTTTTCAATGGCGAGCCTGAGCACACAAACGTCTGTTTTTGGTATATTCCACAA
AGCCTCAGGGGTGTGCCAGACAGCCCTCAACGACGGGAAAAGCTACACAAGGTGGCTCCA
AAAATCAAAGCCCTGATGATGGAGTCAGGTACGACCATGGTTGGCTACCAGCCCCAAGGG
GACAAGGCCAACTTCTTCCGGATGGTCATCTCCAACCCAGCCGCTACCCAGTCTGACATT
GACTTCCTCATTGAGGAGATAGAAAGACTGGGCCAGGATCTGTAA
Enzyme 11 GenBank Gene ID AC007405 Link Image
Enzyme 11 GeneCard ID GAD1 Link Image
Enzyme 11 GenAtlas ID GAD1 Link Image
Enzyme 11 HGNC ID HGNC:4092 Link Image
Enzyme 11 Chromosome Location 2
Enzyme 11 Locus 2q31
Enzyme 11 SNPs SNPJam Report Link Image
Enzyme 11 General References Not Available
Enzyme 11 Metabolite References Not Available
Enzyme 12 [top]
Enzyme 12 ID 12979
Enzyme 12 Name cDNA FLJ75643, highly similar to Homo sapiens 4-aminobutyrate aminotransferase
Enzyme 12 Synonyms
  1. ABAT, nuclear gene encoding mitochondrial protein, transcript variant 2, mRNA
Enzyme 12 Gene Name Not Available
Enzyme 12 Protein Sequence >cDNA FLJ75643, highly similar to Homo sapiens 4-aminobutyrate aminotransferase 
MASMLLAQRLACSFQHSYRLLVPGSRHISQAAAKVDVEFDYDGPLMKTEVPGPRSQELMK
QLNIIQNAEAVHFFCNYEESRGNYLVDVDGNRMLDLYSQISSVPIGYSHPALLKLIQQPQ
NASMFVNRPALGILPPENFVEKLRQSLLSVAPKGMSQLITMACGSCSNENALKTIFMWYR
SKERGQRGFSQEELETCMINQAPGCPDYSILSFMGAFHGRTMGCLATTHSKAIHKIDIPS
FDWPIAPFPRLKYPLEEFVKENQQEEARCLEEVEDLIVKYRKKKKTVAGIIVEPIQSEGG
DNHASDDFFRKLRDIARKHGCAFLVDEVQTGGGCTGKFWAHEHWGLDDPADVMTFSKKMM
TGGFFHKEEFRPNAPYRIFNTWLGDPSKNLLLAEVINIIKREDLLNNAAHAGKALLTGLL
DLQARYPQFISRVRGRGTFCSFDTPDDSIRNKLILIARNKGVVLGGCGDKSIRFRPTLVF
RDHHAHLFLNIFSDILADFK
Enzyme 12 Number of Residues 500
Enzyme 12 Molecular Weight 56440
Enzyme 12 Theoretical pI 8.04
Enzyme 12 GO Classification Not Available
Enzyme 12 General Function Amino acid transport and metabolism
Enzyme 12 Specific Function Not Available
Enzyme 12 Pathways Not Available
Enzyme 12 Reactions Not Available
Enzyme 12 Pfam Domain Function Not Available
Enzyme 12 Signals
  • None
Enzyme 12 Transmembrane Regions
  • None
Enzyme 12 Essentiality Not Available
Enzyme 12 GenBank ID Protein 158254434 Link Image
Enzyme 12 UniProtKB/Swiss-Prot ID A8K386 Link Image
Enzyme 12 UniProtKB/Swiss-Prot Entry Name A8K386_HUMAN Link Image
Enzyme 12 PDB ID 1OHY Link Image
Enzyme 12 PDB File Show
Enzyme 12 3D Structure
Enzyme 12 Cellular Location Not Available
Enzyme 12 Gene Sequence Not Available
Enzyme 12 GenBank Gene ID AK290501 Link Image
Enzyme 12 GeneCard ID A8K386 Link Image
Enzyme 12 GenAtlas ID Not Available
Enzyme 12 HGNC ID Not Available
Enzyme 12 Chromosome Location Not Available
Enzyme 12 Locus Not Available
Enzyme 12 SNPs Not Available
Enzyme 12 General References Not Available
Enzyme 12 Metabolite References Not Available
Enzyme 13 [top]
Enzyme 13 ID 12999
Enzyme 13 Name UPB1 protein
Enzyme 13 Synonyms
  1. Ureidopropionase, beta, isoform CRA_b
Enzyme 13 Gene Name UPB1
Enzyme 13 Protein Sequence >UPB1 protein 
MAGAEWKSLEECLEKHLPLPDLQEVKRVLYGKELRKLDLPREAFEAASREDFELQGYAFE
AAEEQLRRPRIVHVGLVQNRIPLPANAPVAEQVSALHRRIKAIVEVAAMCGVNIICFQEA
WTMPFAFCTREKLPWTEFAESAEDGPTTRFCQKLAKNHDMVVVSPILERDSEHGDVLWNT
AVVISNSGAVLGKTRKNHIPRVGDFNESTYYMEGNLGHPVFQTQFGRIAVNICYGRHHPL
NWLMYSINGAEIIFNPSATIGALSESLWPIEARNAAIANHCFTCAINRVGTEHFPNEFTS
GDGKKAHQDFGYFYGSSYVAAPDSSRTPGLSRSRDGLLVAKLDLNLCQQVNDVWNFKMTG
RYEMYARELAEAVKSNYSPTIVKE
Enzyme 13 Number of Residues 384
Enzyme 13 Molecular Weight 43166
Enzyme 13 Theoretical pI 6.51
Enzyme 13 GO Classification
Function
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
Process
  • metabolism
  • nitrogen compound metabolism
  • physiological process
Component
—
Enzyme 13 General Function Not Available
Enzyme 13 Specific Function Not Available
Enzyme 13 Pathways Not Available
Enzyme 13 Reactions Not Available
Enzyme 13 Pfam Domain Function
Enzyme 13 Signals
  • None
Enzyme 13 Transmembrane Regions
  • None
Enzyme 13 Essentiality Not Available
Enzyme 13 GenBank ID Protein 126153365 Link Image
Enzyme 13 UniProtKB/Swiss-Prot ID A3KMF8 Link Image
Enzyme 13 UniProtKB/Swiss-Prot Entry Name A3KMF8_HUMAN Link Image
Enzyme 13 PDB ID Not Available
Enzyme 13 Cellular Location Not Available
Enzyme 13 Gene Sequence Not Available
Enzyme 13 GenBank Gene ID BC131703 Link Image
Enzyme 13 GeneCard ID A3KMF8 Link Image
Enzyme 13 GenAtlas ID Not Available
Enzyme 13 HGNC ID Not Available
Enzyme 13 Chromosome Location Not Available
Enzyme 13 Locus Not Available
Enzyme 13 SNPs SNPJam Report Link Image
Enzyme 13 General References
  1. Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD, Collins FS, Wagner L, Shenmen CM, Schuler GD, Altschul SF, Zeeberg B, Buetow KH, Schaefer CF, Bhat NK, Hopkins RF, Jordan H, Moore T, Max SI, Wang J, Hsieh F, Diatchenko L, Marusina K, Farmer AA, Rubin GM, Hong L, Stapleton M, Soares MB, Bonaldo MF, Casavant TL, Scheetz TE, Brownstein MJ, Usdin TB, Toshiyuki S, Carninci P, Prange C, Raha SS, Loquellano NA, Peters GJ, Abramson RD, Mullahy SJ, Bosak SA, McEwan PJ, McKernan KJ, Malek JA, Gunaratne PH, Richards S, Worley KC, Hale S, Garcia AM, Gay LJ, Hulyk SW, Villalon DK, Muzny DM, Sodergren EJ, Lu X, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madan A, Young AC, Shevchenko Y, Bouffard GG, Blakesley RW, Touchman JW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Krzywinski MI, Skalska U, Smailus DE, Schnerch A, Schein JE, Jones SJ, Marra MA: Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proc Natl Acad Sci U S A. 2002 Dec 24;99(26):16899-903. Epub 2002 Dec 11. [PubMed Link Image]
Enzyme 13 Metabolite References Not Available
Enzyme 14 [top]
Enzyme 14 ID 17008
Enzyme 14 Name Transporter
Enzyme 14 Synonyms Not Available
Enzyme 14 Gene Name SLC6A6
Enzyme 14 Protein Sequence >Transporter 
MATKEKLQCLKDFHKDILKPSPGKSPGTRPEDEAEGKPPQREKWSSKIDFVLSVAGGFVG
LGNVWRFPYLCYKNGGGAFLIPYFIFLFGSGLPVFFLEIIIGQYTSEGGITCWEKICPLF
SGIGYASVVIVSLLNVYYIVILAWATYYLFQSFQKELPWAHCNHSWNTPHCMEDTMRKNK
SVWITISSTNFTSPVIEFWE
Enzyme 14 Number of Residues 200
Enzyme 14 Molecular Weight 22744
Enzyme 14 Theoretical pI 7.80
Enzyme 14 GO Classification
Function
  • neurotransmitter transporter activity
  • neurotransmitter:sodium symporter activity
  • taurine:sodium symporter activity
  • transporter activity
Process
  • cellular physiological process
  • neurotransmitter transport
  • physiological process
  • transport
Component
  • cell
  • integral to membrane
  • integral to plasma membrane
  • intrinsic to membrane
  • membrane
Enzyme 14 General Function Not Available
Enzyme 14 Specific Function Not Available
Enzyme 14 Pathways Not Available
Enzyme 14 Reactions Not Available
Enzyme 14 Pfam Domain Function
Enzyme 14 Signals
  • None
Enzyme 14 Transmembrane Regions
  • None
Enzyme 14 Essentiality Not Available
Enzyme 14 GenBank ID Protein Not Available
Enzyme 14 UniProtKB/Swiss-Prot ID Q9BRI2 Link Image
Enzyme 14 UniProtKB/Swiss-Prot Entry Name Q9BRI2_HUMAN Link Image
Enzyme 14 PDB ID Not Available
Enzyme 14 Cellular Location Not Available
Enzyme 14 Gene Sequence Not Available
Enzyme 14 GenBank Gene ID BC006252 Link Image
Enzyme 14 GeneCard ID Q9BRI2 Link Image
Enzyme 14 GenAtlas ID SLC6A6 Link Image
Enzyme 14 HGNC ID HGNC:11052 Link Image
Enzyme 14 Chromosome Location Not Available
Enzyme 14 Locus Not Available
Enzyme 14 SNPs SNPJam Report Link Image
Enzyme 14 General References Not Available
Enzyme 14 Metabolite References Not Available
Enzyme 15 [top]
Enzyme 15 ID 17009
Enzyme 15 Name Solute carrier family 6 (Neurotransmitter transporter, taurine), member 6 (Solute carrier family 6 (Neurotransmitter transporter, taurine), member 6, isoform CRA_a)
Enzyme 15 Synonyms Not Available
Enzyme 15 Gene Name SLC6A6
Enzyme 15 Protein Sequence >Solute carrier family 6 (Neurotransmitter transporter, taurine), member 6 (Solute carrier family 6 (Neurotransmitter transporter, taurine), member 6, isoform CRA_a) 
MATKEKLQCLKDFHKDILKPSPGKSPGTRPEDEAEGKPPQREKWSSKIDFVLSVAGGFVG
LGNVWRFPYLCYKNGGGAFLIPYFIFLFGSGLPVFFLEIIIGQYTSEGGITCWEKICPLF
SGIGYASVVIVSLLNVYYIVILAWATYYLFQSFQKELPWAHCNHSWNTPHCMEDTMRKNK
SVWITISSTNFTSPVIEFWERNVLSLSPGIDHPGSLKWDLALCLLLVWLVCFFCIWKGVR
STGKVVYFTATFPFAMLLVLLVRGLTLPGAGAGIKFYLYPDITRLEDPQVWIDAGTQIFF
SYAICLGAMTSLGSYNKYKYNSYRDCMLLGCLNSGTSFVSGFAIFSILGFMAQEQGVDIA
DVAESGPGLAFIAYPKAVTMMPLPTFWSILFFIMLLLLGLDSQFVEVEGQITSLVDLYPS
FLRKGYRREIFIAFVCSISYLLGLTMVTEGGMYVFQLFDYYAASGVCLLWVAFFECFVIA
WIYGGDNLYDGIEDMIGYRPGPWMKYSWAVITPVLCVGCFIFSLVKYVPLTYNKTYVYPN
WAIGLGWSLALSSMLCVPLVIVIRLCQTEGPFLVRVKYLLTPREPNRWAVEREGATPYNS
RTVMNGALVKPTHIIVETMM
Enzyme 15 Number of Residues 620
Enzyme 15 Molecular Weight 69831
Enzyme 15 Theoretical pI 7.43
Enzyme 15 GO Classification
Function
  • neurotransmitter transporter activity
  • neurotransmitter:sodium symporter activity
  • taurine:sodium symporter activity
  • transporter activity
Process
  • cellular physiological process
  • neurotransmitter transport
  • physiological process
  • transport
Component
  • cell
  • integral to membrane
  • integral to plasma membrane
  • intrinsic to membrane
  • membrane
Enzyme 15 General Function Not Available
Enzyme 15 Specific Function Not Available
Enzyme 15 Pathways Not Available
Enzyme 15 Reactions Not Available
Enzyme 15 Pfam Domain Function
Enzyme 15 Signals
  • None
Enzyme 15 Transmembrane Regions
  • None
Enzyme 15 Essentiality Not Available
Enzyme 15 GenBank ID Protein Not Available
Enzyme 15 UniProtKB/Swiss-Prot ID B2RNU7 Link Image
Enzyme 15 UniProtKB/Swiss-Prot Entry Name B2RNU7_HUMAN Link Image
Enzyme 15 PDB ID Not Available
Enzyme 15 Cellular Location Not Available
Enzyme 15 Gene Sequence Not Available
Enzyme 15 GenBank Gene ID BC137128 Link Image
Enzyme 15 GeneCard ID B2RNU7 Link Image
Enzyme 15 GenAtlas ID Not Available
Enzyme 15 HGNC ID Not Available
Enzyme 15 Chromosome Location Not Available
Enzyme 15 Locus Not Available
Enzyme 15 SNPs SNPJam Report Link Image
Enzyme 15 General References Not Available
Enzyme 15 Metabolite References Not Available
Enzyme 16 [top]
Enzyme 16 ID 17010
Enzyme 16 Name cDNA FLJ60211, highly similar to Sodium- and chloride-dependent taurine transporter
Enzyme 16 Synonyms Not Available
Enzyme 16 Gene Name Not Available
Enzyme 16 Protein Sequence >cDNA FLJ60211, highly similar to Sodium- and chloride-dependent taurine transporter 
MATKEKLQCLKDFHKDILKPSPGKSPGTRPEDEAEGKPPQREKWSSKIDFVLSVAGGFVG
LGNVWRFPYLCYKNGGGAFLIPYFIFLFGSGLPVFFLEIIIGQYTSEGGITCWEKICPLF
SGIGYASVVIVSLLNVYYIVILAWATYYLFQSFQKELPWAHCNHSWNTPHCMEDTMRKNK
SVWITISSTNFTSPVIEFWGRNVLSLSPVIDHPGSLKWDLALCLLLVWLVCFFCIWKGVR
STGKVVYFTATFPFAMLLVLLVRGLTLPGAGAGIKFYLYPDITRLEDPQVWIDAGTQIFF
SYAICLGAMTSLGSYNKYKYNSYRSWPGLHCLPKSCDNDAAAHILVHSFFYYASLAWTG
Enzyme 16 Number of Residues 359
Enzyme 16 Molecular Weight 40486
Enzyme 16 Theoretical pI 8.39
Enzyme 16 GO Classification
Function
  • neurotransmitter transporter activity
  • neurotransmitter:sodium symporter activity
  • taurine:sodium symporter activity
  • transporter activity
Process
  • cellular physiological process
  • neurotransmitter transport
  • physiological process
  • transport
Component
  • cell
  • integral to membrane
  • integral to plasma membrane
  • intrinsic to membrane
  • membrane
Enzyme 16 General Function Not Available
Enzyme 16 Specific Function Not Available
Enzyme 16 Pathways Not Available
Enzyme 16 Reactions Not Available
Enzyme 16 Pfam Domain Function
Enzyme 16 Signals
  • None
Enzyme 16 Transmembrane Regions
  • None
Enzyme 16 Essentiality Not Available
Enzyme 16 GenBank ID Protein Not Available
Enzyme 16 UniProtKB/Swiss-Prot ID B4E140 Link Image
Enzyme 16 UniProtKB/Swiss-Prot Entry Name B4E140_HUMAN Link Image
Enzyme 16 PDB ID Not Available
Enzyme 16 Cellular Location Not Available
Enzyme 16 Gene Sequence Not Available
Enzyme 16 GenBank Gene ID AK303649 Link Image
Enzyme 16 GeneCard ID B4E140 Link Image
Enzyme 16 GenAtlas ID Not Available
Enzyme 16 HGNC ID Not Available
Enzyme 16 Chromosome Location Not Available
Enzyme 16 Locus Not Available
Enzyme 16 SNPs Not Available
Enzyme 16 General References Not Available
Enzyme 16 Metabolite References Not Available