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 Glyoxylic acid (HMDB00119)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2009-07-08 11:28:56
Accession Number HMDB00119
Secondary Accession Numbers Not Available
Common Name Glyoxylic acid
Description Glyoxylic acid or oxoacetic acid is an organic compound that is both an aldehyde and a carboxylic acid. Glyoxylic acid is a liquid with a melting Point of -93 degree centigrade and a boiling Point of 111 degree centigrade. It is an intermediate of the glyoxylate cycle, which enables certain organisms to convert fatty acids into carbohydrates. The conjugate base of gloxylic acid is known as glyoxylate. This compound is an intermediate of the glyoxylate cycle, which enables organisms, such as bacteria, fungi and plants to convert fatty acids into carbohydrates. Glyoxylate is the byproduct of the amidation process in biosynthesis of several amidated peptides. The glyoxylate cycle is a metabolic pathway occurring in plants, and several microorganisms, such as E. coli and yeast. Recent research shows that it is present in vertebrates (including humans) and insects. The glyoxylate cycle allows these organisms to use fats for the synthesis of carbohydrates. [PMID: 16396466]
Synonyms
  1. Formylformate
  2. Formylformic acid
  3. Glyoxalate
  4. Glyoxalic acid
  5. Glyoxylate
  6. Glyoxylic acid
  7. Oxalaldehydate
  8. Oxalaldehydic acid
  9. Oxoacetate
  10. Oxoacetic acid
  11. Oxoethanoate
  12. Oxoethanoic acid
  13. a-Ketoacetate
  14. a-Ketoacetic acid
  15. alpha-Ketoacetate
  16. alpha-Ketoacetic acid
Chemical IUPAC Name oxo-Acetic acid
Chemical Formula C2H2O3
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Organic acids
Class
  • Keto-Acids
Sub Class
  • Short chain fatty acids
Family
  • Mammalian Metabolite
Species
  • aldehyde
  • carboxylic acid
Biofunction
—
Application
—
Source
  • Endogenous
Average Molecular Weight 74.035
Monoisotopic Molecular Weight 74.000397
Isomeric SMILES OC(=O)C=O
Canonical SMILES OC(=O)C=O
KEGG Compound ID C00048 Link Image
BioCyc ID GLYOX Link Image
BiGG ID 33659 Link Image
Wikipedia Link Glyoxylic acid Link Image
NuGOwiki Link HMDB00119 Link Image
Metagene Link HMDB00119 Link Image
METLIN ID 3213 Link Image
PubChem Compound 760 Link Image
PubChem Substance 8027585 Link Image
ChEBI ID 16891 Link Image
CAS Registry Number 298-12-4
InChI Identifier InChI=1/C2H2O3/c3-1-2(4)5/h1H,(H,4,5)
Synthesis Reference Jie, Yuanping; Song, Zhen. Method for preparing glyoxylic acid. Faming Zhuanli Shenqing Gongkai Shuomingshu (2007), 5pp.
Melting Point (Experimental) -93 oC
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 1000.0 mg/mL [MEYLAN,WM et al. (1996)]; 224.0 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -1
State Liquid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity -0.59 [Predicted by ALOGPS]; -0.6 [Predicted by PubChem via XLOGP]; -1.40 [MEYLAN,WM & HOWARD,PH (1995)] Calculated using ALOGPS
Material Safety Data Sheet (MSDS)
MOL File Show
SDF File Show
PDB File Show
2D Structure
3D Structure
Experimental PDB ID 1D8C Link Image
Experimental PDB File Show
Experimental PDB Structure
Experimental 1H NMR Spectrum Download Spectrum
Download FID (Varian)
Show Experimental Conditions Link Image
Experimental 13C NMR Spectrum Not Available
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 Not Available
BMRB Spectrum Not Available
Cellular Location
  • Cytoplasm (Predicted from Solubility)
  • mitochondria
  • peroxisome
Biofluid Location
  • Blood
  • Cerebrospinal Fluid
  • Urine
Tissue Location
Tissue References
All Tissues —
Concentrations (Normal)
Biofluid Blood
Value 3.05 (0.25–12.78) uM
Age Adult:>18 yrs old
Sex Male
Patient information After overnight fast
Comments Not Available
References
  • Yan Z, Henderson GN, James MO, Stacpoole PW: Determination of dichloroacetate and its metabolites in human plasma by gas chromatography-mass spectrometry. J Chromatogr B Biomed Sci Appl. 1997 Dec 5;703(1-2):75-84. [PubMed Link Image]
Biofluid Urine
Value 1.27 (0.46-3.26) umol/mmol creatinine
Age Adult:>18 yrs old
Sex Male
Patient information Normal
Comments Not Available
References
  • Lee SH, Kim SO, Chung BC: Gas chromatographic-mass spectrometric determination of urinary oxoacids using O-(2,3,4,5,6-pentafluorobenzyl)oxime-trimethylsilyl ester derivatization and cation-exchange chromatography. J Chromatogr B Biomed Sci Appl. 1998 Nov 20;719(1-2):1-7. [PubMed Link Image]
Biofluid Urine
Value 1.88 (0.63-3.22) umol/mmol creatinine
Age Adult:>18 yrs old
Sex Female
Patient information Normal
Comments Not Available
References
  • Lee SH, Kim SO, Chung BC: Gas chromatographic-mass spectrometric determination of urinary oxoacids using O-(2,3,4,5,6-pentafluorobenzyl)oxime-trimethylsilyl ester derivatization and cation-exchange chromatography. J Chromatogr B Biomed Sci Appl. 1998 Nov 20;719(1-2):1-7. [PubMed Link Image]
Biofluid Urine
Value 3.28 (2.0-5.32) umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 130. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp. Basel, Switzerland c1981-1992.
Biofluid Urine
Value 5.5 (0.00-11.00) umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
Concentrations (Abnormal)
Biofluid CSF
Value 76 uM
Age Adult:>18 yrs old
Sex N/A
Condition Transurethral resection of the prostate
Comments Not Available
References
  • Perier C, Mahul P, Molliex S, Auboyer C, Frey J: Progressive changes in glycine and glycine derivatives in plasma and cerebrospinal fluid after transurethral prostatic resection. Clin Chem. 1990 Dec;36(12):2152-3. [PubMed Link Image]
Biofluid Urine
Value 20.00 (10.00-30.00) umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Comments Not Available
References
Associated Disorders
Condition References
Transurethral resection of the prostate
  • Perier C, Mahul P, Molliex S, Auboyer C, Frey J: Progressive changes in glycine and glycine derivatives in plasma and cerebrospinal fluid after transurethral prostatic resection. Clin Chem. 1990 Dec;36(12):2152-3. [PubMed Link Image]
OMIM ID Not Available
Pathways
Name SMPDB Link KEGG Link
Alanine Metabolism SMP00055 Link Image map00250 Link Image
Glycine and Serine Metabolism SMP00004 Link Image map00260 Link Image
General References
  1. Naghizadeh F, Barlow D, King J: The reduction of oxo-acids by human tissue extracts. Clin Biochem. 1976 Apr;9(2):65-6. [PubMed Link Image]
  2. Borondy PE, Michniewicz BM: Metabolic disposition of isoxicam in man, monkey, dog, and rat. Drug Metab Dispos. 1984 Jul-Aug;12(4):444-51. [PubMed Link Image]
  3. Arvesen A, Maehlen J, Rosen L, Aas P: Myointimal hyperplasia and sympathetic reinnervation following local cold injury and rapid rewarming in the rabbit central ear artery. Vasa. 2001 Jul;30(3):176-83. [PubMed Link Image]
  4. Motomiya Y, Oyama N, Iwamoto H, Uchimura T, Maruyama I: N epsilon-(carboxymethyl)lysine in blood from maintenance hemodialysis patients may contribute to dialysis-related amyloidosis. Kidney Int. 1998 Oct;54(4):1357-66. [PubMed Link Image]
  5. Holmes E, Foxall PJ, Spraul M, Farrant RD, Nicholson JK, Lindon JC: 750 MHz 1H NMR spectroscopy characterisation of the complex metabolic pattern of urine from patients with inborn errors of metabolism: 2-hydroxyglutaric aciduria and maple syrup urine disease. J Pharm Biomed Anal. 1997 Jul;15(11):1647-59. [PubMed Link Image]
  6. Mentasti E, Savigliano M, Marangella M, Petrarulo M, Linari F: High-performance liquid chromatographic determination of glyoxylic acid and other carbonyl compounds in urine. J Chromatogr. 1987 Jul 3;417(2):253-60. [PubMed Link Image]
  7. Bruzzese FJ, Dix JA, Rava RP, Cerny LC: Resonance Raman spectroscopy of chemically modified hemoglobins. Biomater Artif Cells Artif Organs. 1990;18(2):143-56. [PubMed Link Image]
  8. Lee SH, Kim SO, Chung BC: Gas chromatographic-mass spectrometric determination of urinary oxoacids using O-(2,3,4,5,6-pentafluorobenzyl)oxime-trimethylsilyl ester derivatization and cation-exchange chromatography. J Chromatogr B Biomed Sci Appl. 1998 Nov 20;719(1-2):1-7. [PubMed Link Image]
  9. Schmitt A, Gasic-Milenkovic J, Schmitt J: Characterization of advanced glycation end products: mass changes in correlation to side chain modifications. Anal Biochem. 2005 Nov 1;346(1):101-6. Epub 2005 Aug 15. [PubMed Link Image]
  10. Booth ED, Dofferhoff O, Boogaard PJ, Watson WP: Comparison of the metabolism of ethylene glycol and glycolic acid in vitro by precision-cut tissue slices from female rat, rabbit and human liver. Xenobiotica. 2004 Jan;34(1):31-48. [PubMed Link Image]
  11. Tainio H, Vaalasti A, Rechardt L: The distribution of sympathetic adrenergic, tyrosine hydroxylase- and neuropeptide Y-immunoreactive nerves in human axillary sweat glands. Histochemistry. 1986;85(2):117-20. [PubMed Link Image]
  12. Davis WL, Goodman DB: Evidence for the glyoxylate cycle in human liver. Anat Rec. 1992 Dec;234(4):461-8. [PubMed Link Image]
  13. Arvesen A, Maehlen J, Rosen L, Aas P: Early and late functional and histopathological perturbations in the rabbit ear-artery following local cold injury. Vasa. 1999 May;28(2):85-94. [PubMed Link Image]
  14. Wikipedia Link Image
Metabolic Enzymes
  1. D-amino-acid oxidase
  2. Alanine--glyoxylate aminotransferase 2, mitochondrial precursor
  3. Serine--pyruvate aminotransferase
  4. Glyoxylate reductase/hydroxypyruvate reductase
  5. Growth-inhibiting protein 16
  6. cDNA FLJ78493, highly similar to Homo sapiens hydroxyacid oxidase (glycolate oxidase) 1 (HAO1), mRNA (Hydroxyacid oxidase (Glycolate oxidase) 1, isoform CRA_a)
  7. cDNA, FLJ93456, highly similar to Homo sapiens D-amino-acid oxidase (DAO), mRNA (D-amino-acid oxidase, isoform CRA_c)
Enzyme 1 [top]
Enzyme 1 ID 5438
Enzyme 1 Name D-amino-acid oxidase
Enzyme 1 Synonyms
  1. DAMOX
  2. DAO
  3. DAAO
Enzyme 1 Gene Name DAO
Enzyme 1 Protein Sequence >D-amino-acid oxidase 
MRVVVIGAGVIGLSTALCIHERYHSVLQPLDIKVYADRFTPLTTTDVAAGLWQPYLSDPN
NPQEADWSQQTFDYLLSHVHSPNAENLGLFLISGYNLFHEAIPDPSWKDTVLGFRKLTPR
ELDMFPDYGYGWFHTSLILEGKNYLQWLTERLTERGVKFFQRKVESFEEVAREGADVIVN
CTGVWAGALQRDPLLQPGRGQIMKVDAPWMKHFILTHDPERGIYNSPYIIPGTQTVTLGG
IFQLGNWSELNNIQDHNTIWEGCCRLEPTLKNARIIGERTGFRPVRPQIRLEREQLRTGP
SNTEVIHNYGHGGYGLTIHWGCALEAAKLFGRILEEKKLSRMPPSHL
Enzyme 1 Number of Residues 347
Enzyme 1 Molecular Weight 39475
Enzyme 1 Theoretical pI 6.84
Enzyme 1 GO Classification
Function
  • D-amino-acid oxidase activity
  • catalytic activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on the CH-NH2 group of donors
  • oxidoreductase activity, acting on the CH-NH2 group of donors, oxygen as acceptor
Process
  • cellular metabolism
  • electron transport
  • generation of precursor metabolites and energy
  • metabolism
  • physiological process
Component
—
Enzyme 1 General Function Amino acid transport and metabolism
Enzyme 1 Specific Function Could act as a detoxifying agent which removes D-amino acids accumulated during aging. Acts on a variety of D-amino acids with a preference for those having small hydrophobic side chains followed by those bearing polar, aromatic, and basic groups. Does not act on acidic amino acids
Enzyme 1 Pathways
  • Arginine and Proline Metabolism (map00330 Link Image)
  • D-Arginine and D-ornithine Metabolism (map00472 Link Image)
  • Glycine, Serine and Threonine Metabolism (map00260 Link Image)
Enzyme 1 Reactions
  • a D-amino acid + H2O + O2 = a 2-oxo acid + ammonia + H2O2
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • 1-16
Enzyme 1 Transmembrane Regions Not Available
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 30446 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID P14920 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name OXDA_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >1044 bp 
ATGCGTGTGGTGGTGATTGGAGCAGGAGTCATCGGGCTGTCCACCGCCCTCTGCATCCAT
GAGCGCTACCACTCAGTCCTGCAGCCACTGCACATAAAGGTCTACGCGGACCGCTTCACC
CCACTCACCACCACCGACGTGGCTGCCGGCCTCTGGCAGCCCTACCTTTCTGACCCCAAC
AACCCACAGGAGGCGGACTGGAGCCAACAGACCTTTGACTATCTCCTGAGCCATGTCCAT
TCTCCCAACGCTGAAAACCTGGGCCTGTTCCTAATCTCGGGCTACAACCTCTTCCATGAA
GCCATTCCGGACCCTTCCTGGAAGGACACAGTTCTGGGATTTCGGAAGCTGACCCCCAGA
GAGCTGGATATGTTCCCAGATTACGGCTATGGCTGGTTCCACACAAGCCTAATTCTGGAG
GGAAAGAACTATCTACAGTGGCTGACTGAAAGGTTAACTGAGAGGGGAGTGAAGTTCTTC
CAGCGGAAAGTGGAGTCTTTTGAGGAGGTGGCAAGAGAAGGCGCAGACGTGATTGTCAAC
TGCACTGGGGTATGGGCTGGGGCGCTACAACGAGACCCCCTGCTGCAGCCAGGCCGGGGG
CAGATCATGAAGGTGGACGCCCCTTGGATGAAGCACTTCATTCTCACCCATGACCCAGAG
AGAGGCATCTACAATTCCCCGTACATCATCCCAGGGACCCAGACAGTTACTCTTGGAGGC
ATCTTCCAGTTGGGAAACTGGAGTGAACTAAACAATATCCAGGACCACAACACCATTTGG
GAAGGCTGCTGCAGACTGGAGCCCACACTGAAGAATGCAAGAATTATTGGTGAAGCAACT
GGCTTCCGGCCAGTACGCCCCCAGATTCGGCTAGAAAGAGAACAGCTTCGCACTGGACCT
TCAAACACAGAGGTCATCCACAACTATGGCCATGGAGGCTACGGGCTCACCATCCACTGG
GGATGTGCCCTGGAGGCAGCCAAGCTCTTTGGGAGAATCCTGGAAGAAAAGAAATTGTCC
AGAATGCCACCATCCCACCTCTGA
Enzyme 1 GenBank Gene ID X13227 Link Image
Enzyme 1 GeneCard ID DAO Link Image
Enzyme 1 GenAtlas ID DAO Link Image
Enzyme 1 HGNC ID HGNC:2671 Link Image
Enzyme 1 Chromosome Location 12
Enzyme 1 Locus 12q24
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Momoi K, Fukui K, Watanabe F, Miyake Y: Molecular cloning and sequence analysis of cDNA encoding human kidney D-amino acid oxidase. FEBS Lett. 1988 Sep 26;238(1):180-4. [PubMed Link Image]
  2. Fukui K, Miyake Y: Molecular cloning and chromosomal localization of a human gene encoding D-amino-acid oxidase. J Biol Chem. 1992 Sep 15;267(26):18631-8. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5633
Enzyme 2 Name Alanine--glyoxylate aminotransferase 2, mitochondrial precursor
Enzyme 2 Synonyms
  1. (R-3-amino-2-methylpropionate--pyruvate transaminase
  2. AGT 2
  3. Beta-alanine-pyruvate aminotransferase
  4. Beta- ALAAT II
  5. D-AIBAT
Enzyme 2 Gene Name AGXT2
Enzyme 2 Protein Sequence >Alanine--glyoxylate aminotransferase 2, mitochondrial precursor 
MTLIWRHLLRPLCLVTSAPRILEMHPFLSLGTSRTSVTKLSLHTKPRMPPCDFMPERYQS
LGYNRVLEIHKEHLSPVVTAYFQKPLLLHQGHMEWLFDAEGSRYLDFFSGIVTVSVGHCH
PKVNAVAQKQLGRLWHTSTVFFHPPMHEYAEKLAALLPEPLKVIFLVNSGSEANELAMLM
ARAHSNNIDIISFRGAYHGCSPYTLGLTNVGTYKMELPGGTGCQPTMCPDVFRGPWGGSH
CRDSPVQTIRKCSCAPDCCQAKDQYIEQFKDTLSTSVAKSIAGFFAEPIQGVNGVVQYPK
GFLKEAFELVRARGGVCIADEVQTGFGRLGSHFWGFQTHDVLPDIVTMAKGIGNGFPMAA
VITTPEIAKSLAKCLQHFNTFGGNPMACAIGSAVLEVIKEENLQENSQEVGTYMLLKFAK
LRDEFEIVGDVRGKGLMIGIEMVQDKISCRPLPREEVNQIHEDCKHMGLLVGRGSIFSQT
FRIAPSMCITKPEVDFAVEVFRSALTQHMERRAK
Enzyme 2 Number of Residues 514
Enzyme 2 Molecular Weight 57157
Enzyme 2 Theoretical pI 7.91
Enzyme 2 GO Classification
Function
  • binding
  • catalytic activity
  • pyridoxal phosphate binding
  • transaminase activity
  • transferase activity
  • transferase activity, transferring nitrogenous groups
  • vitamin binding
Process
—
Component
—
Enzyme 2 General Function Amino acid transport and metabolism
Enzyme 2 Specific Function L-alanine + glyoxylate = pyruvate + glycine
Enzyme 2 Pathways
  • Glycine, Serine and Threonine Metabolism (map00260 Link Image)
Enzyme 2 Reactions
  • L-alanine + glyoxylate = pyruvate + glycine
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • 1-24
Enzyme 2 Transmembrane Regions Not Available
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 12406973 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID Q9BYV1 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name AGT2_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >1545 bp 
ATGACTCTAATCTGGAGACATTTGCTGAGACCCTTGTGCCTGGTCACTTCCGCTCCCAGG
ATCCTTGAGATGCATCCTTTCCTGAGCCTAGGTACTTCCCGGACATCAGTAACCAAGCTC
AGTCTTCATACAAAGCCCAGAATGCCTCCATGTGACTTCATGCCTGAAAGATACCAGTCC
CTTGGCTACAACCGTGTCCTGGAAATCCACAAGGAACATCTTTCTCCTGTGGTGACGGCA
TATTTCCAGAAACCCCTGCTGCTCCACCAGGGGCACATGGAGTGGCTCTTTGATGCTGAA
GGAAGCAGATACCTGGATTTCTTTTCCGGGATTGTTACTGTCAGTGTTGGCCATTGCCAC
CCAAAGGTGAATGCAGTGGCACAAAAGCAGCTCGGCCGCCTGTGGCATACAAGCACCGTC
TTCTTCCACCCTCCAATGCATGAATATGCAGAGAAGCTTGCCGCACTTCTTCCTGAGCCT
CTTAAGGTCATTTTCTTGGTGAACAGTGGCTCAGAAGCCAATGAGCTGGCCATGCTGATG
GCCAGGGCGCACTCAAACAACATAGACATCATTTCTTTCAGAGGAGCCTACCATGGATGC
AGTCCTTACACACTTGGCTTGACAAACGTAGGGACCTACAAGATGGAACTCCCTGGTGGG
ACAGGTTGCCAACCAACAATGTGTCCAGATGTTTTTCGTGGCCCTTGGGGAGGAAGCCAC
TGTCGAGATTCTCCAGTGCAAACAATCAGGAAGTGCAGCTGTGCACCAGACTGCTGCCAA
GCTAAAGATCAGTATATTGAGCAATTCAAAGATACGCTGAGCACATCTGTGGCCAAGTCA
ATTGCTGGATTTTTCGCAGAACCTATTCAAGGTGTGAATGGAGTTGTCCAGTACCCAAAG
GGGTTTCTAAAGGAAGCCTTTGAGCTGGTGCGAGCAAGGGGAGGCGTGTGCATTGCAGAT
GAAGTGCAGACAGGATTTGGAAGGTTGGGCTCTCACTTCTGGGGCTTCCAAACCCACGAT
GTCCTGCCTGACATTGTCACCATGGCTAAAGGGATTGGGAATGGCTTTCCCATGGCAGCA
GTCATAACCACTCCAGAGATTGCCAAATCTTTGGCGAAATGCCTGCAGCACTTCAACACC
TTTGGAGGGAACCCCATGGCCTGTGCCATTGGATCTGCTGTGCTTGAGGTGATTAAAGAA
GAAAATCTACAGGAAAACAGTCAAGAAGTTGGGACCTACATGTTACTAAAGTTTGCTAAG
CTGCGGGATGAATTTGAAATTGTTGGAGACGTCCGAGGCAAAGGTCTCATGATAGGCATA
GAAATGGTGCAGGATAAGATAAGCTGTCGGCCTCTTCCCCGTGAAGAAGTAAATCAGATC
CATGAGGACTGCAAGCACATGGGACTCCTCGTTGGCAGAGGCAGCATTTTTTCTCAGACA
TTTCGCATTGCGCCCTCAATGTGCATCACTAAACCAGAAGTTGATTTTGCAGTAGAAGTA
TTTCGTTCTGCCTTAACCCAACACATGGAAAGAAGAGCTAAGTAA
Enzyme 2 GenBank Gene ID AJ292204 Link Image
Enzyme 2 GeneCard ID AGXT2 Link Image
Enzyme 2 GenAtlas ID AGXT2 Link Image
Enzyme 2 HGNC ID HGNC:14412 Link Image
Enzyme 2 Chromosome Location Not Available
Enzyme 2 Locus Not Available
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References Not Available
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 6069
Enzyme 3 Name Serine--pyruvate aminotransferase
Enzyme 3 Synonyms
  1. SPT
  2. Alanine-- glyoxylate aminotransferase
  3. AGT
Enzyme 3 Gene Name AGXT
Enzyme 3 Protein Sequence >Serine--pyruvate aminotransferase 
MASHKLLVTPPKALLKPLSIPNQLLLGPGPSNLPPRIMAAGGLQMIGSMSKDMYQIMDEI
KEGIQYVFQTRNPLTLVISGSGHCALEAALVNVLEPGDSFLVGANGIWGQRAVDIGERIG
ARVHPMTKDPGGHYTLQEVEEGLAQHKPVLLFLTHGESSTGVLQPLDGFGELCHRYKCLL
LVDSVASLGGTPLYMDRQGIDILYSGSQKALNAPPGTSLISFSDKAKKKMYSRKTKPFSF
YLDIKWLANFWGCDDQPRMYHHTIPVISLYSLRESLALIAEQGLENSWRQHREAAAYLHG
RLQALGLQLFVKDPALRLPTVTTVAVPAGYDWRDIVSYVIDHFDIEIMGGLGPSTGKVLR
IGLLGCNATRENVDRVTEALRAALQHCPKKKL
Enzyme 3 Number of Residues 392
Enzyme 3 Molecular Weight 43011
Enzyme 3 Theoretical pI 8.55
Enzyme 3 GO Classification
Function
  • catalytic activity
  • transaminase activity
  • transferase activity
  • transferase activity, transferring nitrogenous groups
Process
  • metabolism
  • physiological process
Component
—
Enzyme 3 General Function Amino acid transport and metabolism
Enzyme 3 Specific Function L-serine + pyruvate = 3-hydroxypyruvate + L- alanine
Enzyme 3 Pathways
  • Glycine, Serine and Threonine Metabolism (map00260 Link Image)
Enzyme 3 Reactions
  • L-serine + pyruvate = 3-hydroxypyruvate + L-alanine
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 36582 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID P21549 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name SPYA_HUMAN Link Image
Enzyme 3 PDB ID 1H0C Link Image
Enzyme 3 PDB File Show
Enzyme 3 3D Structure
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >1179 bp 
ATGGCCTCTCACAAGCTGCTGGTGACCCCCCCCAAGGCCCTGCTCAAGCCCCTCTCCATC
CCCAACCAGCTCCTGCTGGGGCCTGGTCCTTCCAACCTGCCTCCTCGCATCATGGCAGCC
GGGGGGCTGCAGATGATCGGGTCCATGAGCAAGGATATGTACCAGATCATGGACGAGATC
AAGGAAGGCATCCAGTACGTGTTCCAGACCAGGAACCCACTCACACTGGTCATCTCTGGC
TCGGGACACTGTGCCCTGGAGGCCGCCCTGGTCAATGTGCTGGAGCCTGGGGACTCCTTC
CTGGTTGGGGCCAATGGCATTTGGGGGCAGCGAGCCGTGGACATCGGGGAGCGCATAGGA
GCCCGAGTGCACCCGATGACCAAGGACCCTGGAGGCCACTACACACTGCAGGAGGTGGAG
GAGGGCCTGGCCCAGCACAAGCCAGTGCTGCTGTTCTTAACCCACGGGGAGTCGTCCACC
GGCGTGCTGCAGCCCCTTGATGGCTTCGGGGAACTCTGCCACAGGTACAAGTGCCTGCTC
CTGGTGGATTCGGTGGCATCCCTGGGCGGGACCCCCCTTTACATGGACCGGCAAGGCATC
GACATCCTGTACTCGGGCTCCCAGAAGGCCCTGAACGCCCCTCCAGGGACCTCGCTCATC
TCCTTCAGTGACAAGGCCAAAAAGAAGATGTACTCCCGCAAGACGAAGCCCTTCTCCTTC
TACCTGGACATCAAGTGGCTGGCCAACTTCTGGGGCTGTGACGACCAGCCCAGGATGTAC
CATCACACAATCCCCGTCATCAGCCTGTACAGCCTGAGAGAGAGCCTGGCCCTCATTGCG
GAACAGGGCCTGGAGAACAGCTGGCGCCAGCACCGCGAGGCCGCGGCGTATCTGCATGGG
CGCCTGCAGGCACTGGGGCTGCAGCTCTTCGTGAAGGACCCGGCGCTCCGGCTTCCCACA
GTCACCACTGTGGCTGTACCCGCTGGCTATGACTGGAGAGACATCGTCAGCTACGTCATA
GACCACTTCGACATTGAGATCATGGGTGGCCTTGGGCCCTCCACGGGGAAGGTGCTGCGG
ATCGGCCTGCTGGGCTGCAATGCCACCCGCGAGAATGTGGACCGCGTGACGGAGGCCCTG
AGGGCGGCCCTGCAGCACTGCCCCAAGAAGAAGCTGTGA
Enzyme 3 GenBank Gene ID X56092 Link Image
Enzyme 3 GeneCard ID AGXT Link Image
Enzyme 3 GenAtlas ID AGXT Link Image
Enzyme 3 HGNC ID HGNC:341 Link Image
Enzyme 3 Chromosome Location 2
Enzyme 3 Locus 2q36-q37
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Nishiyama K, Berstein G, Oda T, Ichiyama A: Cloning and nucleotide sequence of cDNA encoding human liver serine-pyruvate aminotransferase. Eur J Biochem. 1990 Nov 26;194(1):9-18. [PubMed Link Image]
  2. Purdue PE, Takada Y, Danpure CJ: Identification of mutations associated with peroxisome-to-mitochondrion mistargeting of alanine/glyoxylate aminotransferase in primary hyperoxaluria type 1. J Cell Biol. 1990 Dec;111(6 Pt 1):2341-51. [PubMed Link Image]
  3. Takada Y, Kaneko N, Esumi H, Purdue PE, Danpure CJ: Human peroxisomal L-alanine: glyoxylate aminotransferase. Evolutionary loss of a mitochondrial targeting signal by point mutation of the initiation codon. Biochem J. 1990 Jun 1;268(2):517-20. [PubMed Link Image]
  4. Purdue PE, Lumb MJ, Fox M, Griffo G, Hamon-Benais C, Povey S, Danpure CJ: Characterization and chromosomal mapping of a genomic clone encoding human alanine:glyoxylate aminotransferase. Genomics. 1991 May;10(1):34-42. [PubMed Link Image]
  5. Nishiyama K, Funai T, Katafuchi R, Hattori F, Onoyama K, Ichiyama A: Primary hyperoxaluria type I due to a point mutation of T to C in the coding region of the serine:pyruvate aminotransferase gene. Biochem Biophys Res Commun. 1991 May 15;176(3):1093-9. [PubMed Link Image]
  6. Purdue PE, Lumb MJ, Allsop J, Minatogawa Y, Danpure CJ: A glycine-to-glutamate substitution abolishes alanine:glyoxylate aminotransferase catalytic activity in a subset of patients with primary hyperoxaluria type 1. Genomics. 1992 May;13(1):215-8. [PubMed Link Image]
  7. Minatogawa Y, Tone S, Allsop J, Purdue PE, Takada Y, Danpur CJ, Kido R: A serine-to-phenylalanine substitution leads to loss of alanine:glyoxylate aminotransferase catalytic activity and immunoreactivity in a patient with primary hyperoxaluria type 1. Hum Mol Genet. 1992 Nov;1(8):643-4. [PubMed Link Image]
  8. Danpure CJ, Purdue PE, Fryer P, Griffiths S, Allsop J, Lumb MJ, Guttridge KM, Jennings PR, Scheinman JI, Mauer SM, et al.: Enzymological and mutational analysis of a complex primary hyperoxaluria type 1 phenotype involving alanine:glyoxylate aminotransferase peroxisome-to-mitochondrion mistargeting and intraperoxisomal aggregation. Am J Hum Genet. 1993 Aug;53(2):417-32. [PubMed Link Image]
  9. Danpure CJ: Primary hyperoxaluria type 1 and peroxisome-to-mitochondrion mistargeting of alanine:glyoxylate aminotransferase. Biochimie. 1993;75(3-4):309-15. [PubMed Link Image]
  10. von Schnakenburg C, Rumsby G: Primary hyperoxaluria type 1: a cluster of new mutations in exon 7 of the AGXT gene. J Med Genet. 1997 Jun;34(6):489-92. [PubMed Link Image]
  11. Amoroso A, Pirulli D, Puzzer D, Ferri L, Crovella S, Ferrettini C, Marangella M, Mazzola G, Florian F: Gene symbol: AGXT. Disease: primary hyperoxaluria type I. Hum Genet. 1999 May;104(5):441. [PubMed Link Image]
  12. Basmaison O, Rolland MO, Cochat P, Bozon D: Identification of 5 novel mutations in the AGXT gene. Hum Mutat. 2000 Jun;15(6):577. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 13057
Enzyme 4 Name Glyoxylate reductase/hydroxypyruvate reductase
Enzyme 4 Synonyms
  1. Glyoxylate reductase/hydroxypyruvate reductase, isoform CRA_b
Enzyme 4 Gene Name GRHPR
Enzyme 4 Protein Sequence >Glyoxylate reductase/hydroxypyruvate reductase 
MRPVRLMKVFVTRRIPAEGRVALARAADCEVEQWDSDEPIPAKELERGVAGAHGLLCLLS
DHVDKRILDAAGANLKVISTMSVGIDHLALDEIKKRGIRVGYTPDVLTDTTAELAVSLLL
TTCRRLPEAIEEVKNGGWTSWKPLWLCGYGLTQSTVGIIGLGRIGQAIARRLKPFGVQRF
LYTGRQPRPEEAAEFQAEFVSTPELAAQSDFIVVACSLTPATEGLCNKDFFQKMKETAVF
INISRGDVVNQDDLYQALASGKIAAAGLDVTSPEPLPTNHPLLTLKNCVILPHIGSATHR
TRNTMSLLAANNLLAGLRGEPMPSELKL
Enzyme 4 Number of Residues 328
Enzyme 4 Molecular Weight 35669
Enzyme 4 Theoretical pI 7.44
Enzyme 4 GO Classification
Function
  • NAD binding
  • binding
  • catalytic activity
  • coenzyme binding
  • cofactor binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on CH-OH group of donors
  • oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
Process
  • L-serine biosynthesis
  • L-serine metabolism
  • amino acid and derivative metabolism
  • amino acid metabolism
  • cellular metabolism
  • metabolism
  • physiological process
  • serine family amino acid metabolism
Component
—
Enzyme 4 General Function Energy production and conversion
Enzyme 4 Specific Function Not Available
Enzyme 4 Pathways Not Available
Enzyme 4 Reactions Not Available
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • None
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein Not Available
Enzyme 4 UniProtKB/Swiss-Prot ID Q5T945 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name Q5T945_HUMAN Link Image
Enzyme 4 PDB ID Not Available
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence Not Available
Enzyme 4 GenBank Gene ID AL158155 Link Image
Enzyme 4 GeneCard ID Q5T945 Link Image
Enzyme 4 GenAtlas ID GRHPR Link Image
Enzyme 4 HGNC ID HGNC:4570 Link Image
Enzyme 4 Chromosome Location Not Available
Enzyme 4 Locus Not Available
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References Not Available
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 13058
Enzyme 5 Name Growth-inhibiting protein 16
Enzyme 5 Synonyms
  1. Hydroxyacid oxidase 2
  2. Long chain, isoform CRA_b
Enzyme 5 Gene Name GIG16
Enzyme 5 Protein Sequence >Growth-inhibiting protein 16 
MSLVCLTDFQAHAREQLSKSTRDFIEGGADDSITRDDNIAAFKRIRLRPRYLRDVSEVDT
RTTIQGEEISAPICIAPTGFHCLVWPDGEMSTARAAQAAGICYITSTFASCSLEDIVIAA
PEGLRWFQLYVHPDLQLNKQLIQRVESLGFKALVITLDTPVCGNRRHDIRNQLRRNLTLT
DLQSPKKGNAIPYFQMTPISTSLCWNDLSWFQSITRLPIILKGILTKEDAELAVKHNVQG
IIVSNHGGRQLDEVLASIDALTEVVAAVKGKIEVYLDGGVRTGNDVLKALALGAKCIFLG
RPILWGLACKGEHGVKEVLNILTNEFHTSMALTGCRSVAEINRNLVQFSRL
Enzyme 5 Number of Residues 351
Enzyme 5 Molecular Weight 38839
Enzyme 5 Theoretical pI 7.69
Enzyme 5 GO Classification
Function
  • FMN binding
  • binding
  • catalytic activity
  • nucleotide binding
  • oxidoreductase activity
Process
  • cellular metabolism
  • electron transport
  • generation of precursor metabolites and energy
  • metabolism
  • physiological process
Component
—
Enzyme 5 General Function Energy production and conversion
Enzyme 5 Specific Function Not Available
Enzyme 5 Pathways Not Available
Enzyme 5 Reactions Not Available
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • None
Enzyme 5 Transmembrane Regions
  • None
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 46981963 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID Q2TU86 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name Q2TU86_HUMAN Link Image
Enzyme 5 PDB ID Not Available
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence Not Available
Enzyme 5 GenBank Gene ID AY513277 Link Image
Enzyme 5 GeneCard ID Q2TU86 Link Image
Enzyme 5 GenAtlas ID GIG16 Link Image
Enzyme 5 HGNC ID HGNC:4810 Link Image
Enzyme 5 Chromosome Location Not Available
Enzyme 5 Locus Not Available
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References Not Available
Enzyme 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 15208
Enzyme 6 Name cDNA FLJ78493, highly similar to Homo sapiens hydroxyacid oxidase (glycolate oxidase) 1 (HAO1), mRNA (Hydroxyacid oxidase (Glycolate oxidase) 1, isoform CRA_a)
Enzyme 6 Synonyms Not Available
Enzyme 6 Gene Name HAO1
Enzyme 6 Protein Sequence >cDNA FLJ78493, highly similar to Homo sapiens hydroxyacid oxidase (glycolate oxidase) 1 (HAO1), mRNA (Hydroxyacid oxidase (Glycolate oxidase) 1, isoform CRA_a) 
MLPRLICINDYEQHAKSVLPKSIYDYYRSGANDEETLADNIAAFSRWKLYPRMLRNVAET
DLSTSVLGQRVSMPICVGATAMQRMAHVDGELATVRACQSLGTGMMLSSWATSSIEEVAE
AGPEALRWLQLYIYKDREVTKKLVRQAEKMGYKAIFVTVDTPYLGNRLDDVRNRFKLPPQ
LRMKNFETSTLSFSPEENFGDDSGLAAYVAKAIDPSISWEDIKWLRRLTSLPIVAKGILR
GDDAREAVKHGLNGILVSNHGARQLDGVPATIDVLPEIVEAVEGKVEVFLDGGVRKGTDV
LKALALGAKAVFVGRPIVWGLAFQGEKGVQDVLEILKEEFRLAMALSGCQNVKVIDKTLV
RKNPLAVSKI
Enzyme 6 Number of Residues 370
Enzyme 6 Molecular Weight 40925
Enzyme 6 Theoretical pI 8.29
Enzyme 6 GO Classification Not Available
Enzyme 6 General Function Energy production and conversion
Enzyme 6 Specific Function Not Available
Enzyme 6 Pathways Not Available
Enzyme 6 Reactions Not Available
Enzyme 6 Pfam Domain Function Not Available
Enzyme 6 Signals
  • None
Enzyme 6 Transmembrane Regions
  • None
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 158259869 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID A8K058 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name A8K058_HUMAN Link Image
Enzyme 6 PDB ID Not Available
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence >1113 bp 
ATGCTCCCCCGGCTAATTTGTATCAATGATTATGAACAACATGCTAAATCAGTACTTCCA
AAGTCTATATATGACTATTACAGGTCTGGGGCAAATGATGAAGAAACTTTGGCTGATAAT
ATTGCAGCATTTTCCAGATGGAAGCTGTATCCAAGGATGCTCCGGAATGTTGCTGAAACA
GATCTGTCGACTTCTGTTTTAGGACAGAGGGTCAGCATGCCAATATGTGTGGGGGCTACG
GCCATGCAGCGCATGGCTCATGTGGACGGCGAGCTTGCCACTGTGAGAGCCTGTCAGTCC
CTGGGAACGGGCATGATGTTGAGTTCCTGGGCCACCTCCTCAATTGAAGAAGTGGCGGAA
GCTGGTCCTGAGGCACTTCGTTGGCTGCAACTGTATATCTACAAGGACCGAGAAGTCACC
AAGAAGCTAGTGCGGCAGGCAGAGAAGATGGGCTACAAGGCCATATTTGTGACAGTGGAC
ACACCTTACCTGGGCAACCGTCTGGATGATGTGCGTAACAGATTCAAACTGCCGCCACAA
CTCAGGATGAAAAATTTTGAAACCAGTACTTTATCATTTTCTCCTGAGGAAAATTTTGGA
GACGACAGTGGACTTGCTGCATATGTGGCTAAAGCAATAGACCCATCTATCAGCTGGGAA
GATATCAAATGGCTGAGAAGACTGACATCATTGCCAATTGTTGCAAAGGGCATTTTGAGA
GGTGATGATGCCAGGGAGGCTGTTAAACATGGCTTGAATGGGATCTTGGTGTCGAATCAT
GGGGCTCGACAACTCGATGGGGTGCCAGCCACTATTGATGTTCTGCCAGAAATTGTGGAG
GCTGTGGAAGGGAAGGTGGAAGTCTTCCTGGACGGGGGTGTGCGGAAAGGCACTGATGTT
CTGAAAGCTCTGGCTCTTGGCGCCAAGGCTGTGTTTGTGGGGAGACCAATCGTTTGGGGC
TTAGCTTTCCAGGGGGAGAAAGGTGTTCAAGATGTCCTCGAGATACTAAAGGAAGAATTC
CGGTTGGCCATGGCTCTGAGTGGGTGCCAGAATGTGAAAGTCATCGACAAGACATTGGTG
AGGAAAAATCCTTTGGCCGTTTCCAAGATCTGA
Enzyme 6 GenBank Gene ID AK289423 Link Image
Enzyme 6 GeneCard ID A8K058 Link Image
Enzyme 6 GenAtlas ID Not Available
Enzyme 6 HGNC ID Not Available
Enzyme 6 Chromosome Location 20
Enzyme 6 Locus 20p12
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 General References Not Available
Enzyme 6 Metabolite References Not Available
Enzyme 7 [top]
Enzyme 7 ID 16461
Enzyme 7 Name cDNA, FLJ93456, highly similar to Homo sapiens D-amino-acid oxidase (DAO), mRNA (D-amino-acid oxidase, isoform CRA_c)
Enzyme 7 Synonyms Not Available
Enzyme 7 Gene Name DAO
Enzyme 7 Protein Sequence >cDNA, FLJ93456, highly similar to Homo sapiens D-amino-acid oxidase (DAO), mRNA (D-amino-acid oxidase, isoform CRA_c) 
MRVVVIGAGVIGLSTALCIHERYHSVLQPLDIKVYADRFTPLTTTDVAAGLWQPYLSDPN
NPQEADWSQQTFDYLLSHVHSPNAENLGLFLISGYNLFHEAIPDPSWKDTVLGFRKLTPR
ELDMFPDYGYGWFHTSLILEGKNYLQWLTERLTERGVKFFQRKVESFEEVAREGADVIVN
CTGVWAGALQRDPLLQPGRGQIMKVDAPWMKHFILTHDPERGIYNSPYIIPGTQTVTLGG
IFQLGNWSELNNIQDHNTIWEGCCRLEPTLKNARIIGERTGFRPVRPQIRLEREQLRTGP
SNTEVIHNYGHGGYGLTIHWGCALEAAKLFGRILEEKKLSRMPPSHL
Enzyme 7 Number of Residues 347
Enzyme 7 Molecular Weight 39475
Enzyme 7 Theoretical pI 6.84
Enzyme 7 GO Classification
Function
  • ATP binding
  • D-amino-acid oxidase activity
  • RNA ligase activity
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • ligase activity
  • ligase activity, forming phosphoric ester bonds
  • nucleotide binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on the CH-NH2 group of donors
  • oxidoreductase activity, acting on the CH-NH2 group of donors, oxygen as acceptor
  • purine nucleotide binding
  • tRNA ligase activity
Process
  • RNA metabolism
  • cellular metabolism
  • electron transport
  • generation of precursor metabolites and energy
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • physiological process
  • tRNA aminoacylation
  • tRNA aminoacylation for protein translation
  • tRNA metabolism
Component
—
Enzyme 7 General Function Amino acid transport and metabolism
Enzyme 7 Specific Function Not Available
Enzyme 7 Pathways Not Available
Enzyme 7 Reactions Not Available
Enzyme 7 Pfam Domain Function
Enzyme 7 Signals
  • None
Enzyme 7 Transmembrane Regions
  • None
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein Not Available
Enzyme 7 UniProtKB/Swiss-Prot ID B2R7I5 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name B2R7I5_HUMAN Link Image
Enzyme 7 PDB ID Not Available
Enzyme 7 Cellular Location Not Available
Enzyme 7 Gene Sequence Not Available
Enzyme 7 GenBank Gene ID AK312995 Link Image
Enzyme 7 GeneCard ID B2R7I5 Link Image
Enzyme 7 GenAtlas ID Not Available
Enzyme 7 HGNC ID Not Available
Enzyme 7 Chromosome Location 12
Enzyme 7 Locus 12q24
Enzyme 7 SNPs SNPJam Report Link Image
Enzyme 7 General References Not Available
Enzyme 7 Metabolite References Not Available