| Version |
2.5 |
| Creation Date |
2005-11-16 15:48:42 |
| Update Date |
2009-05-05 20:58:37 |
| Accession Number |
HMDB01259 |
| Secondary Accession Numbers |
Not Available |
| Common Name |
Succinic acid semialdehyde |
| Description |
Succinic acid semialdehyde is an intermediate in the catabolism of gamma-aminobutyrate (PMID 16435183). Succinate semialdehyde dehydrogenase is an enzyme that catalyses the reaction of succinate semialdehyde and NAD+ to form succinate and NADH. Succinic semialdehyde dehydrogenase (SSADH) deficiency (gamma-hydroxybutyric aciduria) is a rare neurometabolic disorder of gamma-aminobutyric acid degradation. Symptoms include motor delay, hypotonia, speech delay, autistic features, seizures, and ataxia. Patients also exhibit behavioral problems, such as attention deficit, hyperactivity, anxiety, or aggression. (PMID: 18622364) |
| Synonyms |
- 2-formylpropionic acid ethyl ester
- 3-Formylpropanoate
- 3-Formylpropanoic acid
- 4-Oxobutanoate
- 4-Oxobutanoic acid
- Butryaldehydate
- Butryaldehydic acid
- Succinaldehydate
- Succinic acid semialdehyde
- Succinic semialdehyde
- beta-Formylpropionate
- beta-Formylpropionic acid
- gamma-Oxybutyrate
- gamma-Oxybutyric acid
- Succinate semialdehyde
|
| Chemical IUPAC Name |
4-oxobutanoic acid |
| Chemical Formula |
C4H6O3 |
| Chemical Structure |
 |
| Chemical Taxonomy |
| Kingdom |
|
| Super Class |
|
| Class |
|
| Sub Class |
|
| Family |
|
| Species |
|
| Biofunction |
- Component of Butanoate metabolism
- Component of Glutamate metabolism
|
| Application |
| — |
| Source |
|
|
| Average Molecular Weight |
102.089 |
| Monoisotopic Molecular Weight |
102.031693 |
| Isomeric SMILES |
OC(=O)CCC=O |
| Canonical SMILES |
OC(=O)CCC=O |
| KEGG Compound ID |
C00232  |
| BioCyc ID |
SUCC-S-ALD  |
| BiGG ID |
34331  |
| Wikipedia Link |
Succinic semialdehyde  |
| NuGOwiki Link |
HMDB01259  |
| Metagene Link |
HMDB01259  |
| METLIN ID |
6114  |
| PubChem Compound |
1112  |
| PubChem Substance |
3190  |
| ChEBI ID |
16265  |
| CAS Registry Number |
692-29-5 |
| InChI Identifier |
InChI=1/C4H6O3/c5-3-1-2-4(6)7/h3H,1-2H2,(H,6,7) |
| Synthesis Reference |
Bruce, R.; Sims, K.; Pitts, F. N., Jr. Synthesis and purification of succinic semialdehyde. Analytical Biochemistry (1971), 41(1), 271-3. |
| Melting Point (Experimental) |
Not Available |
| Experimental Water Solubility |
Not Available
Source: PhysProp
|
| Predicted Water Solubility |
654.0 mg/mL [MEYLAN,WM et al. (1996)]; 194.0 mg/mL [Predicted by ALOGPS]
Calculated using ALOGPS
|
| Physiological Charge |
-1 |
| State |
Solid |
| Experimental LogP/Hydrophobicity |
Not Available
Source: PhysProp
|
| Predicted LogP/Hydrophobicity |
-0.47 [Predicted by ALOGPS]; -0.3 [Predicted by PubChem via XLOGP]; -0.42 [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 |
Not Available |
| Experimental 1H NMR Spectrum |
Download Spectrum Download FID (Bruker) Show Experimental Conditions  |
| Experimental 13C NMR Spectrum |
Not Available |
| Experimental 13C HSQC Spectrum |
Download Spectrum Download FID (Bruker) Show Experimental Conditions  |
| Predicted 1H NMR Spectrum |
Show Image Show Peaklist
|
| Predicted 13C NMR Spectrum |
Show Image Show Peaklist
|
| Mass Spectrum |
|
| Simplified TOCSY Spectrum |
Not Available |
| BMRB Spectrum |
Not Available |
| Cellular Location |
|
| Biofluid Location |
- Cerebrospinal Fluid
- Urine
|
| Tissue Location |
| Tissue |
References |
| Testes |
— |
|
| Concentrations (Normal) |
| Biofluid |
CSF |
| Value |
28.5 (24.0-33.0) uM |
| Age |
Adult:>18 yrs old |
| Sex |
Both |
| Patient information |
Normal |
| Comments |
Not Available |
| References |
- Geigy Scientific Tables, 8th Rev edition, pp. 165-177. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp., Basel, Switzerland c1981-1992.
|
| Biofluid |
Urine |
| Value |
0.35 (0.14-0.54) 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
]
|
| Biofluid |
Urine |
| Value |
0.39 (0.28-0.51) 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
]
|
|
| Concentrations (Abnormal) |
Not Available |
| Associated Disorders |
Not Available |
| OMIM ID |
Not Available |
| Pathways |
|
| General References |
- Du L, Musson DG, Wang AQ: Stability studies of vorinostat and its two metabolites in human plasma, serum and urine. J Pharm Biomed Anal. 2006 Nov 16;42(5):556-64. Epub 2006 Jul 5. [PubMed
]
- Du L, Musson DG, Wang AQ: High turbulence liquid chromatography online extraction and tandem mass spectrometry for the simultaneous determination of suberoylanilide hydroxamic acid and its two metabolites in human serum. Rapid Commun Mass Spectrom. 2005;19(13):1779-87. [PubMed
]
- Hinshelwood A, McGarvie G, Ellis EM: Substrate specificity of mouse aldo-keto reductase AKR7A5. Chem Biol Interact. 2003 Feb 1;143-144:263-9. [PubMed
]
- Lee BC, Choe YS, Chi DY, Paik JY, Lee KH, Choi Y, Kim BT: 8-cyclopentadienyltricarbonyl 99mtc 8-oxooctanoic acid: a novel radiotracer for evaluation of medium chain fatty acid metabolism in the liver. Bioconjug Chem. 2004 Jan-Feb;15(1):121-7. [PubMed
]
- Parise RA, Holleran JL, Beumer JH, Ramalingam S, Egorin MJ: A liquid chromatography-electrospray ionization tandem mass spectrometric assay for quantitation of the histone deacetylase inhibitor, vorinostat (suberoylanilide hydroxamicacid, SAHA), and its metabolites in human serum. J Chromatogr B Analyt Technol Biomed Life Sci. 2006 Aug 18;840(2):108-15. Epub 2006 May 24. [PubMed
]
- Wikipedia

|
| Metabolic Enzymes |
- 4-aminobutyrate aminotransferase, mitochondrial precursor
- Succinate semialdehyde dehydrogenase, mitochondrial precursor
- Alcohol dehydrogenase iron-containing 1
- cDNA FLJ75643, highly similar to Homo sapiens 4-aminobutyrate aminotransferase
|
|
Enzyme 1
[top]
|
| Enzyme 1 ID |
5480 |
| Enzyme 1 Name |
4-aminobutyrate aminotransferase, mitochondrial precursor |
| Enzyme 1 Synonyms |
- (S-3-amino-2-methylpropionate transaminase
- Gamma-amino-N-butyrate transaminase
- GABA transaminase
- GABA aminotransferase
- GABA-AT
- GABA-T
- 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
)
|
| Enzyme 1 Reactions |
- (S)-3-amino-2-methylpropanoate + 2-oxoglutarate = 2-methyl-3-oxopropanoate + L-glutamate
|
| Enzyme 1 Pfam Domain Function |
|
| Enzyme 1 Signals |
|
| Enzyme 1 Transmembrane Regions |
|
| Enzyme 1 Essentiality |
Not Available |
| Enzyme 1 GenBank ID Protein |
602705  |
| Enzyme 1 UniProtKB/Swiss-Prot ID |
P80404  |
| Enzyme 1 UniProtKB/Swiss-Prot Entry Name |
GABT_HUMAN  |
| Enzyme 1 PDB ID |
1OHY  |
| 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  |
| Enzyme 1 GeneCard ID |
ABAT  |
| Enzyme 1 GenAtlas ID |
ABAT  |
| Enzyme 1 HGNC ID |
HGNC:23  |
| Enzyme 1 Chromosome Location |
16 |
| Enzyme 1 Locus |
16p13.2 |
| Enzyme 1 SNPs |
SNPJam Report  |
| Enzyme 1 General References |
- 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
]
- 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
]
- 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
]
|
| Enzyme 1 Metabolite References |
Not Available |
|
Enzyme 2
[top]
|
| Enzyme 2 ID |
5481 |
| Enzyme 2 Name |
Succinate semialdehyde dehydrogenase, mitochondrial precursor |
| Enzyme 2 Synonyms |
- NAD(+-dependent succinic semialdehyde dehydrogenase
|
| Enzyme 2 Gene Name |
ALDH5A1 |
| Enzyme 2 Protein Sequence |
>Succinate semialdehyde dehydrogenase, mitochondrial precursor
MATCIWLRSCGARRLGSTFPGCRLRPRAGGLVPASGPAPGPAQLRCYAGRLAGLSAALLR
TDSFVGGRWLPAAATFPVQDPASGAALGMVADCGVREARAAVRAAYEAFCRWREVSAKER
SSLLRKWYNLMIQNKDDLARIITAESGKPLKEAHGEILYSAFFLEWFSEEARRVYGDIIH
TPAKDRRALVLKQPIGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPFSALAL
AELASQAGIPSGVYNVIPCSRKNAKEVGEAICTDPLVSKISFTGSTTTGKILLHHAANSV
KRVSMELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHDAFVKAF
AEAMKKNLRVGNGFEEGTTQGPLINEKAVEKVEKQVNDAVSKGATVVTGGKRHQLGKNFF
EPTLLCNVTQDMLCTHEETFGPLAPVIKFDTEEEAIAIANAADVGLAGYFYSQDPAQIWR
VAEQLEVGMVGVNEGLISSVECPFGGVKQSGLGREGSKYGIDEYLELKYVCYGGL
|
| Enzyme 2 Number of Residues |
535 |
| Enzyme 2 Molecular Weight |
57215 |
| Enzyme 2 Theoretical pI |
8.37 |
| Enzyme 2 GO Classification |
| Function |
- aldehyde dehydrogenase activity
- catalytic activity
- oxidoreductase activity
- oxidoreductase activity, acting on the aldehyde or oxo group of donors
- oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
|
| Process |
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 2 General Function |
Energy production and conversion |
| Enzyme 2 Specific Function |
Succinate semialdehyde + NAD(+) + H(2)O = succinate + NADH |
| Enzyme 2 Pathways |
|
| Enzyme 2 Reactions |
- succinate semialdehyde + NAD+ + H2O = succinate + NADH + H+
|
| Enzyme 2 Pfam Domain Function |
|
| Enzyme 2 Signals |
|
| Enzyme 2 Transmembrane Regions |
|
| Enzyme 2 Essentiality |
Not Available |
| Enzyme 2 GenBank ID Protein |
3766467  |
| Enzyme 2 UniProtKB/Swiss-Prot ID |
P51649  |
| Enzyme 2 UniProtKB/Swiss-Prot Entry Name |
SSDH_HUMAN  |
| Enzyme 2 PDB ID |
Not Available |
| Enzyme 2 Cellular Location |
Not Available |
| Enzyme 2 Gene Sequence |
>1608 bp
ATGGCGACCTGCATTTGGCTGCGGAGCTGTGGGGCCCGGCGCCTCGGGTCGACGTTTCCA
GGCTGCCGCCTCCGCCCCCGCGCCGGCGGCCTGGTCCCTGCCTCCGGGCCTGCGCCCGGC
CCGGCCCAGCTCCGCTGCTACGCTGGGCGCCTGGCGGGCCTCTCTGCGGCGCTGCTGCGC
ACCGACAGCTTCGTGGGCGGCCGCTGGCTCCCGGCCGCCGCCACCTTCCCCGTGCAAGAC
CCGGCCAGCGGCGCCGCTCTGGGCATGGTAGCCGACTGCGGGGTGCGAGAGGCCCGCGCC
GCCGTGCGCGCTGCCTACGAGGCTTTCTGCCGCTGGAGGGAGGTCTCCGCCAAGGAGAGG
AGTTCATTACTTCGGAAGTGGTACAATTTAATGATACAAAATAAGGATGACCTTGCCAGA
ATAATCACAGCTGAAAGTGGAAAGCCACTGAAGGAGGCACATGGAGAAATTCTCTATTCC
GCCTTTTTCCTAGAGTGGTTCTCTGAGGAAGCCCGCCGTGTTTACGGAGACATTATCCAC
ACCCCGGCAAAGGACAGGCGGGCCCTGGTCCTCAAGCAGCCCATAGGCGTGGCTGCAGTC
ATCACCCCGTGGAATTTCCCCAGTGCCATGATCACCCGGAAGGTGGGGGCCGCCCTGGCA
GCCGGCTGTACTGTCGTGGTGAAGCCTGCCGAAGACACGCCCTTCTCCGCCCTGGCCCTG
GCTGAGCTTGCAAGCCAGGCTGGGATTCCTTCAGGTGTATACAATGTTATTCCCTGTTCT
CGAAAGAATGCCAAGGAAGTAGGGGAGGCAATTTGTACTGATCCTCTGGTGTCCAAAATT
TCCTTTACTGGTTCAACAACTACAGGAAAGATCCTGTTGCACCACGCAGCAAACTCTGTG
AAAAGGGTCTCTATGGAGCTGGGCGGCCTTGCTCCATTTATAGTATTTGACAGTGCCAAC
GTGGACCAGGCTGTAGCAGGGGCCATGGCATCTAAATTTAGGAACACTGGACAGACTTGT
GTTTGCTCAAACCAATTCTTGGTGCAAAGGGGCATCCATGATGCCTTTGTAAAAGCATTC
GCCGAGGCCATGAAGAAGAACCTGCGCGTAGGTAATGGATTTGAGGAAGGAACTACTCAG
GGCCCATTAATTAATGAAAAAGCGGTAGAAAAGGTGGAGAAACAGGTGAATGATGCCGTT
TCTAAAGGTGCCACCGTTGTGACAGGTGGAAAACGACACCAACTTGGAAAAAATTTCTTT
GAGCCTACCCTGCTGTGCAATGTCACCCAGGACATGCTGTGCACTCATGAAGAGACTTTC
GGGCCTCTGGCACCAGTTATCAAGTTCGATACAGAGGAGGAGGCTATAGCAATCGCTAAC
GCAGCTGATGTTGGGTTAGCAGGTTATTTTTACTCTCAAGACCCAGCCCAGATCTGGAGA
GTGGCAGAGCAGCTGGAAGTGGGCATGGTTGGCGTCAACGAAGGATTAATTTCCTCTGTG
GAGTGCCCTTTTGGTGGAGTGAAGCAGTCCGGCCTTGGGCGAGAGGGGTCCAAGTATGGC
ATTGATGAGTATCTGGAACTCAAGTATGTGTGTTACGGGGGCTTGTAG
|
| Enzyme 2 GenBank Gene ID |
Y11192  |
| Enzyme 2 GeneCard ID |
ALDH5A1  |
| Enzyme 2 GenAtlas ID |
ALDH5A1  |
| Enzyme 2 HGNC ID |
HGNC:408  |
| Enzyme 2 Chromosome Location |
6 |
| Enzyme 2 Locus |
6p22.2-p22.3 |
| Enzyme 2 SNPs |
SNPJam Report  |
| Enzyme 2 General References |
- Chambliss KL, Hinson DD, Trettel F, Malaspina P, Novelletto A, Jakobs C, Gibson KM: Two exon-skipping mutations as the molecular basis of succinic semialdehyde dehydrogenase deficiency (4-hydroxybutyric aciduria). Am J Hum Genet. 1998 Aug;63(2):399-408. [PubMed
]
- Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [PubMed
]
- Chambliss KL, Caudle DL, Hinson DD, Moomaw CR, Slaughter CA, Jakobs C, Gibson KM: Molecular cloning of the mature NAD(+)-dependent succinic semialdehyde dehydrogenase from rat and human. cDNA isolation, evolutionary homology, and tissue expression. J Biol Chem. 1995 Jan 6;270(1):461-7. [PubMed
]
- Trettel F, Malaspina P, Jodice C, Novelletto A, Slaughter CA, Caudle DL, Hinson DD, Chambliss KL, Gibson KM: Human succinic semialdehyde dehydrogenase. Molecular cloning and chromosomal localization. Adv Exp Med Biol. 1997;414:253-60. [PubMed
]
|
| Enzyme 2 Metabolite References |
Not Available |
|
Enzyme 3
[top]
|
| Enzyme 3 ID |
9419 |
| Enzyme 3 Name |
Alcohol dehydrogenase iron-containing 1 |
| Enzyme 3 Synonyms |
Not Available |
| Enzyme 3 Gene Name |
ADHFE1 |
| Enzyme 3 Protein Sequence |
>Alcohol dehydrogenase iron-containing 1
MAAAARARVAYLLRQLQRAACQCPTHSHTYSQAPGLSPSGKTTDYAFEMAVSNIRYGAAV
TKEVGMDLKNMGAKNVCLMTDKNLSKLPPVQVAMDSLVKNGIPFTVYDNVRVEPTDSSFM
EAIEFAQKGAFDAYVAVGGGSTMDTCKAANLYASSPHSDFLDYVSAPIGKGKPVSVPLKP
LIAVPTTSGTGSETTGVAIFDYEHLKVKIGITSRAIKPTLGLIDPLHTLHMPARVVANSG
FDVLCHALESYTTLPYHLRSPCPSNPITRPAYQGSNPISDIWAIHALRIVAKYLKRAVRN
PDDLEARSHMHLASAFAGIGFGNAGVHLCHGMSYPISGLVKMYKAKDYNVDHPLVPHGLS
VVLTSPAVFTFTAQMFPERHLEMAEILGADTRTARIQDAGLVLADTLRKFLFDLDVDDGL
AAVGYSKADIPALVKGTLPQERVTKLAPCPQSEEDLAALFEASMKLY
|
| Enzyme 3 Number of Residues |
467 |
| Enzyme 3 Molecular Weight |
50308 |
| Enzyme 3 Theoretical pI |
Not Available |
| Enzyme 3 GO Classification |
| Function |
- binding
- catalytic activity
- cation binding
- ion binding
- iron ion binding
- oxidoreductase activity
- transition metal ion binding
|
| Process |
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 3 General Function |
Energy production and conversion |
| Enzyme 3 Specific Function |
Not Available |
| Enzyme 3 Pathways |
Not Available |
| Enzyme 3 Reactions |
- 3,4-Dihydroxymandelaldehyde + H+ + Nicotinamide adenine dinucleotide - reduced <==> 3,4-Dihydroxyphenylethyleneglycol + Nicotinamide adenine dinucleotide
|
| Enzyme 3 Pfam Domain Function |
|
| Enzyme 3 Signals |
|
| Enzyme 3 Transmembrane Regions |
|
| Enzyme 3 Essentiality |
Not Available |
| Enzyme 3 GenBank ID Protein |
25989126  |
| Enzyme 3 UniProtKB/Swiss-Prot ID |
Q8IWW8  |
| Enzyme 3 UniProtKB/Swiss-Prot Entry Name |
Q8IWW8_HUMAN  |
| Enzyme 3 PDB ID |
Not Available |
| Enzyme 3 Cellular Location |
Not Available |
| Enzyme 3 Gene Sequence |
Not Available |
| Enzyme 3 GenBank Gene ID |
AY033237  |
| Enzyme 3 GeneCard ID |
Not Available |
| Enzyme 3 GenAtlas ID |
ADHFE1  |
| Enzyme 3 HGNC ID |
HGNC:16354  |
| Enzyme 3 Chromosome Location |
Not Available |
| Enzyme 3 Locus |
Not Available |
| Enzyme 3 SNPs |
SNPJam Report  |
| Enzyme 3 General References |
- Deng Y, Wang Z, Gu S, Ji C, Ying K, Xie Y, Mao Y: Cloning and characterization of a novel human alcohol dehydrogenase gene (ADHFe1). DNA Seq. 2002 Oct;13(5):301-6. [PubMed
]
|
| Enzyme 3 Metabolite References |
Not Available |
|
Enzyme 4
[top]
|
| Enzyme 4 ID |
12979 |
| Enzyme 4 Name |
cDNA FLJ75643, highly similar to Homo sapiens 4-aminobutyrate aminotransferase |
| Enzyme 4 Synonyms |
- ABAT, nuclear gene encoding mitochondrial protein, transcript variant 2, mRNA
|
| Enzyme 4 Gene Name |
Not Available |
| Enzyme 4 Protein Sequence |
>cDNA FLJ75643, highly similar to Homo sapiens 4-aminobutyrate aminotransferase
MASMLLAQRLACSFQHSYRLLVPGSRHISQAAAKVDVEFDYDGPLMKTEVPGPRSQELMK
QLNIIQNAEAVHFFCNYEESRGNYLVDVDGNRMLDLYSQISSVPIGYSHPALLKLIQQPQ
NASMFVNRPALGILPPENFVEKLRQSLLSVAPKGMSQLITMACGSCSNENALKTIFMWYR
SKERGQRGFSQEELETCMINQAPGCPDYSILSFMGAFHGRTMGCLATTHSKAIHKIDIPS
FDWPIAPFPRLKYPLEEFVKENQQEEARCLEEVEDLIVKYRKKKKTVAGIIVEPIQSEGG
DNHASDDFFRKLRDIARKHGCAFLVDEVQTGGGCTGKFWAHEHWGLDDPADVMTFSKKMM
TGGFFHKEEFRPNAPYRIFNTWLGDPSKNLLLAEVINIIKREDLLNNAAHAGKALLTGLL
DLQARYPQFISRVRGRGTFCSFDTPDDSIRNKLILIARNKGVVLGGCGDKSIRFRPTLVF
RDHHAHLFLNIFSDILADFK
|
| Enzyme 4 Number of Residues |
500 |
| Enzyme 4 Molecular Weight |
56440 |
| Enzyme 4 Theoretical pI |
8.04 |
| Enzyme 4 GO Classification |
Not Available |
| Enzyme 4 General Function |
Amino acid transport and metabolism |
| Enzyme 4 Specific Function |
Not Available |
| Enzyme 4 Pathways |
Not Available |
| Enzyme 4 Reactions |
Not Available |
| Enzyme 4 Pfam Domain Function |
Not Available |
| Enzyme 4 Signals |
|
| Enzyme 4 Transmembrane Regions |
|
| Enzyme 4 Essentiality |
Not Available |
| Enzyme 4 GenBank ID Protein |
158254434  |
| Enzyme 4 UniProtKB/Swiss-Prot ID |
A8K386  |
| Enzyme 4 UniProtKB/Swiss-Prot Entry Name |
A8K386_HUMAN  |
| Enzyme 4 PDB ID |
1OHY  |
| Enzyme 4 PDB File |
Show |
| Enzyme 4 3D Structure |
|
| Enzyme 4 Cellular Location |
Not Available |
| Enzyme 4 Gene Sequence |
Not Available |
| Enzyme 4 GenBank Gene ID |
AK290501  |
| Enzyme 4 GeneCard ID |
A8K386  |
| Enzyme 4 GenAtlas ID |
Not Available |
| Enzyme 4 HGNC ID |
Not Available |
| Enzyme 4 Chromosome Location |
Not Available |
| Enzyme 4 Locus |
Not Available |
| Enzyme 4 SNPs |
Not Available |
| Enzyme 4 General References |
Not Available |
| Enzyme 4 Metabolite References |
Not Available |