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Human Metabolome Database Version 2.5

 

Showing metabocard for Hypotaurine (HMDB00965)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2009-05-05 20:58:24
Accession Number HMDB00965
Secondary Accession Numbers Not Available
Common Name Hypotaurine
Description Hypotaurine is a product of enzyme cysteamine dioxygenase [EC 1.13.11.19] in taurine and hypotaurine metabolism pathway (KEGG). It may function as an antioxidant and a protective agent under physiological conditions (PMID 14992269).
Synonyms
  1. 2-Aminoethylsulfinate
  2. 2-Aminoethylsulfinic acid
  3. 2-amino-Ethanesulfinate
  4. 2-amino-Ethanesulfinic acid
  5. 2-aminoethanesulfinate
  6. 2-aminoethanesulfinic acid
  7. Cystaminesulfinate
  8. Cystaminesulfinic acid
  9. Hypotaurine
Chemical IUPAC Name 2-aminoethanesulfinic acid
Chemical Formula C2H7NO2S
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)
  • sulfinic acid
Biofunction
  • Component of Taurine and hypotaurine metabolism
Application
—
Source
  • Endogenous
Average Molecular Weight 109.147
Monoisotopic Molecular Weight 109.019753
Isomeric SMILES NCCS(O)=O
Canonical SMILES NCCS(O)=O
KEGG Compound ID C00519 Link Image
BioCyc ID HYPOTAURINE Link Image
BiGG ID 35230 Link Image
Wikipedia Link Not Available
NuGOwiki Link HMDB00965 Link Image
Metagene Link HMDB00965 Link Image
METLIN ID 281 Link Image
PubChem Compound 107812 Link Image
PubChem Substance 10234448 Link Image
ChEBI ID 16668 Link Image
CAS Registry Number 300-84-5
InChI Identifier InChI=1/C2H7NO2S/c3-1-2-6(4)5/h1-3H2,(H,4,5)
Synthesis Reference Owen, Terence C.; Wilbraham, A. C. Convenient preparation and characterization of hypotaurine. Journal of the Chemical Society (1965), (Jan.), 826-7.
Melting Point (Experimental) Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 38.800003 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -1
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity -1.19 [Predicted by ALOGPS]; -2.6 [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 (Bruker)
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 LogP)
Biofluid Location
  • Urine
Tissue Location
Tissue References
Fibroblasts —
Sperm —
Concentrations (Normal)
Biofluid Urine
Value 0.65 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Guo K, Li L: Differential (12)C-/(13)C-Isotope Dansylation Labeling and Fast Liquid Chromatography/Mass Spectrometry for Absolute and Relative Quantification of the Metabolome. Anal Chem. 2009 Mar 23. [PubMed Link Image]
Concentrations (Abnormal) Not Available
Associated Disorders Not Available
OMIM ID Not Available
Pathways
Name SMPDB Link KEGG Link
Taurine and Hypotaurine Metabolism SMP00021 Link Image map00430 Link Image
General References
  1. Dominy J, Eller S, Dawson R Jr: Building biosynthetic schools: reviewing compartmentation of CNS taurine synthesis. Neurochem Res. 2004 Jan;29(1):97-103. [PubMed Link Image]
  2. Fontana M, Pecci L, Dupre S, Cavallini D: Antioxidant properties of sulfinates: protective effect of hypotaurine on peroxynitrite-dependent damage. Neurochem Res. 2004 Jan;29(1):111-6. [PubMed Link Image]
  3. Pitari G, Dupre S, Spirito A, Antonini G, Amicarelli F: Hypotaurine protection on cell damage by singlet oxygen. Adv Exp Med Biol. 2000;483:157-62. [PubMed Link Image]
  4. Grafe F, Wohlrab W, Neubert RH, Brandsch M: Functional characterization of sodium- and chloride-dependent taurine transport in human keratinocytes. Eur J Pharm Biopharm. 2004 Mar;57(2):337-41. [PubMed Link Image]
  5. Krieg RC, Uihlein D, Murthum T, Endlicher E, Hausmann F, Messmann H, Knuechel R: Improving the use of 5-aminolevulinic acid (ALA)-induced protoporphyrin IX (PPIX) for the gastrointestinal tract by esterification--an in vitro study. Cell Mol Biol (Noisy-le-grand). 2002 Dec;48(8):917-23. [PubMed Link Image]
  6. Guerin P, Menezo Y: Hypotaurine and taurine in gamete and embryo environments: de novo synthesis via the cysteine sulfinic acid pathway in oviduct cells. Zygote. 1995 Nov;3(4):333-43. [PubMed Link Image]
  7. Masuoka N, Yao K, Kinuta M, Ohta J, Wakimoto M, Ubuka T: High-performance liquid chromatographic determination of taurine and hypotaurine using 3,5-dinitrobenzoyl chloride as derivatizing reagent. J Chromatogr B Biomed Appl. 1994 Oct 3;660(1):31-5. [PubMed Link Image]
  8. Guerin P, Guillaud J, Menezo Y: Hypotaurine in spermatozoa and genital secretions and its production by oviduct epithelial cells in vitro. Hum Reprod. 1995 Apr;10(4):866-72. [PubMed Link Image]
  9. Holmes RP, Goodman HO, Shihabi ZK, Jarow JP: The taurine and hypotaurine content of human semen. J Androl. 1992 May-Jun;13(3):289-92. [PubMed Link Image]
  10. Mahadevan MM, Trounson AO: Removal of the cumulus oophorus from the human oocyte for in vitro fertilization. Fertil Steril. 1985 Feb;43(2):263-7. [PubMed Link Image]
Metabolic Enzymes
  1. Glutamate decarboxylase 2
  2. Cysteine sulfinic acid decarboxylase
  3. Hypothetical protein GAD1
  4. Chromosome 10 open reading frame 22
  5. 2-aminoethanethiol dioxygenase
Enzyme 1 [top]
Enzyme 1 ID 5975
Enzyme 1 Name Glutamate decarboxylase 2
Enzyme 1 Synonyms
  1. Glutamate decarboxylase 65 kDa isoform
  2. GAD-65
  3. 65 kDa glutamic acid decarboxylase
Enzyme 1 Gene Name GAD2
Enzyme 1 Protein Sequence >Glutamate decarboxylase 2 
MASPGSGFWSFGSEDGSGDSENPGTARAWCQVAQKFTGGIGNKLCALLYGDAEKPAESGG
SQPPRAAARKAACACDQKPCSCSKVDVNYAFLHATDLLPACDGERPTLAFLQDVMNILLQ
YVVKSFDRSTKVIDFHYPNELLQEYNWELADQPQNLEEILMHCQTTLKYAIKTGHPRYFN
QLSTGLDMVGLAADWLTSTANTNMFTYEIAPVFVLLEYVTLKKMREIIGWPGGSGDGIFS
PGGAISNMYAMMIARFKMFPEVKEKGMAALPRLIAFTSEHSHFSLKKGAAALGIGTDSVI
LIKCDERGKMIPSDLERRILEAKQKGFVPFLVSATAGTTVYGAFDPLLAVADICKKYKIW
MHVDAAWGGGLLMSRKHKWKLSGVERANSVTWNPHKMMGVPLQCSALLVREEGLMQNCNQ
MHASYLFQQDKHYDLSYDTGDKALQCGRHVDVFKLWLMWRAKGTTGFEAHVDKCLELAEY
LYNIIKNREGYEMVFDGKPQHTNVCFWYIPPSLRTLEDNEERMSRLSKVAPVIKARMMEY
GTTMVSYQPLGDKVNFFRMVISNPAATHQDIDFLIEEIERLGQDL
Enzyme 1 Number of Residues 585
Enzyme 1 Molecular Weight 65412
Enzyme 1 Theoretical pI 6.89
Enzyme 1 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 1 General Function Amino acid transport and metabolism
Enzyme 1 Specific Function Catalyzes the production of GABA
Enzyme 1 Pathways
Enzyme 1 Reactions
  • L-glutamate = 4-aminobutanoate + CO2
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 182934 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID Q05329 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name DCE2_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 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 1 GenBank Gene ID M81882 Link Image
Enzyme 1 GeneCard ID GAD2 Link Image
Enzyme 1 GenAtlas ID GAD2 Link Image
Enzyme 1 HGNC ID HGNC:4093 Link Image
Enzyme 1 Chromosome Location 10
Enzyme 1 Locus 10p11.23
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 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 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 6224
Enzyme 2 Name Cysteine sulfinic acid decarboxylase
Enzyme 2 Synonyms
  1. Sulfinoalanine decarboxylase
  2. Cysteine-sulfinate decarboxylase
Enzyme 2 Gene Name CSAD
Enzyme 2 Protein Sequence >Cysteine sulfinic acid decarboxylase 
MADSEALPSLAGDPVAVEALLRAVFGVVVDEAIQKGTSVSQKVCEWKEPEELKQLLDLEL
RSQGESQKQILERCRAVIRYSVKTGHPRFFNQLFSGLDPHALAGRIITESLNTSQYTYEI
APVFVLMEEEVLRKLRALVGWSSGDGIFCPGGSISNMYAVNLARYQRYPDCKQRGLRTLP
PLALFTSKECHYSIQKGAAFLGLGTDSVRVVKADERGKMVPEDLERQIGMAEAEGAVPFL
VSATSGTTVLGAFDPLEAIADVCQRHGLWLHVDAAWGGSVLLSQTHRHLLDGIQRADSVA
WNPHKLLAAGLQCSALLLQDTSNLLKRCHGSQASYLFQQDKFYDVALDTGDKVVQCGRRV
DCLKLWLMWKAQGDQGLERRIDQAFVLARYLVEEMKKREGFELVMEPEFVNVCFWFVPPS
LRGKQESPDYHERLSKVAPVLKERMVKEGSMMIGYQPHGTRGNFFRVVVANSALTCADMD
FLLNELERLGQDL
Enzyme 2 Number of Residues 493
Enzyme 2 Molecular Weight 55024
Enzyme 2 Theoretical pI 6.44
Enzyme 2 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 2 General Function Amino acid transport and metabolism
Enzyme 2 Specific Function 3-sulfino-L-alanine = hypotaurine + CO(2)
Enzyme 2 Pathways
  • Taurine and Hypotaurine Metabolism (map00430 Link Image)
Enzyme 2 Reactions
  • 3-sulfino-L-alanine = hypotaurine + CO2
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 4894558 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID Q9Y600 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name CSAD_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >1041 bp 
ATGGCTGACTCAGAAGCACTCCCCTCCCTTGCTGGGGACCCAGTGGCTGTGGAAGCCTTG
CTCCGGGCCGTGTTTGGGGTTGTTGTGGATGAGGCCATTCAGAAAGGAACCAGTGTCTCC
CAGAAGTGTCACTACTCCATCCAGAAGGGAGCTGCGTTTCTGGGACTTGGCACCGACAGT
GTCCGAGTGGTCAAGGCTGATGAGAGAGGGAAAATGGTCCCCGAGGATCTGGAGAGGCAG
ATTGGTATGGCCGAGGCTGAGGGTGCTGTGCCGTTCCTGGTCAGTGCCACCTCTGGCACC
ACTGTGCTAGGGGCCTTTGACCCCCTGGAGGCAATTGCTGATGTGTGCCAGCGTCATGGG
CTATGGCTGCATGTGGATGCTGCCTGGGGTGGGAGCGTCCTGCTGTCACAGACACACAGG
CATCTCCTGGATGGGATCCAGAGGGCTGACTCTGTGGCCTGGAATCCCCACAAGCTCCTC
GCAGCAGGCCTGCAATGCTCTGCACTTCTTCTCCAGGATACCTCGAACCTGCTCAAGCGC
TGCCATGGGTCCCAGGCCAGCTACCTTTTCCAGCAGGACAAGTTCTACGATGTGGCTCTG
GACACGGGAGACAAGGTGGTGCAGTGTGGCCGCCGTGTGGACTGTCTGAAGCTGTGGCTC
ATGTGGAAGGCACAGGGCGATCAAGGGCTGGAGCGGCGCATCGACCAGGCCTTTGTCCTT
GCCCGGTACCTGGTGGAGGAAATGAAGAAGCGGGAAGGGTTTGAGCTAGTCATGGAGCCT
GAGTTTGTCAATGTGTGTTTCTGGTTCGTACCCCCCAGCCTGCGAGGGAAGCAGGAGAGT
CCAGATTACCACGAAGGGCTGTCAAAGGTGGCCCCCGTGCTCAAGGAGCGCATGGTGAAG
GAGGGCTCCATGATGATTGGCTACCAGCCCCACGGGACCCGGGGCAACTTCTTCCGTGTG
GTTGTGGCCAACTCTGCACTGACCTGTGCTGATATGGACTTCCTCCTCAACGAGCTGGAG
CGGCTAGGCCAGGACCTGTGA
Enzyme 2 GenBank Gene ID AF116546 Link Image
Enzyme 2 GeneCard ID CSAD Link Image
Enzyme 2 GenAtlas ID CSAD Link Image
Enzyme 2 HGNC ID HGNC:18966 Link Image
Enzyme 2 Chromosome Location 12
Enzyme 2 Locus 12q13.11-q14.3
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 7966
Enzyme 3 Name Hypothetical protein GAD1
Enzyme 3 Synonyms Not Available
Enzyme 3 Gene Name GAD1
Enzyme 3 Protein Sequence >Hypothetical protein GAD1 
MASSTPSSSATSSNAGADPNTTNLRPTTYDTWCGVAHGCTRKLGLKICGFLQRTNSLEEK
SRLVSAFKERQSSKNLLSCENSDRDARFRRTETDFSNLFARDLLPAKNGEEQTVQFLLEV
VDILLNYVRKTFDRSTKVLDFHHPHQLLEGMEGFNLELSDHPESLEQILVDCRDTLKYGV
RTGHPRFFNQLSTGLDIIGLAGEWLTSTANTNMFTYEIAPVFVLMEQITLKKMREIVGWS
SKDGDGIFSPGGAISNMYSIMAARYKYFPEVKTKGMAAVPKLVLFTSEQSHYSIKKAGAA
LGFGTDNVILIKCNERGKIIPADFEAKILEAKQKGYVPFYVNATAGTTVYGAFDPIQEIA
DICEKYNLWLHVDAAWGGGLLMSRKHRHKLNGIERANSVTWNPHKMMGVLLQCSAILVKE
KGILQGCNQMCAGYLFQPDKQYDVSYDTGDKAIQCGRHVDIFKFWLMWKAKGTVGFENQI
NKCLELAEYLYAKIKNREEFEMVFNGEPEHTNVCFWYIPQSLRGVPDSPQRREKLHKVAP
KIKALMMESGTTMVGYQPQGDKANFFRMVISNPAATQSDIDFLIEEIERLGQDL
Enzyme 3 Number of Residues 594
Enzyme 3 Molecular Weight 66897
Enzyme 3 Theoretical pI 7.67
Enzyme 3 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 3 General Function Amino acid transport and metabolism
Enzyme 3 Specific Function Not Available
Enzyme 3 Pathways Not Available
Enzyme 3 Reactions Not Available
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 62988850 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID Q53TQ7 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name Q53TQ7_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 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 3 GenBank Gene ID AC007405 Link Image
Enzyme 3 GeneCard ID GAD1 Link Image
Enzyme 3 GenAtlas ID GAD1 Link Image
Enzyme 3 HGNC ID HGNC:4092 Link Image
Enzyme 3 Chromosome Location 2
Enzyme 3 Locus 2q31
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References Not Available
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 13113
Enzyme 4 Name Chromosome 10 open reading frame 22
Enzyme 4 Synonyms
  1. Chromosome 10 open reading frame 22, isoform CRA_a
Enzyme 4 Gene Name C10orf22
Enzyme 4 Protein Sequence >Chromosome 10 open reading frame 22 
MPRDNMASLIQRIARQACLTFRGSGGGRGASDRDAASGPEAPMQPGFPENLSKLKSLLTQ
LRAEDLNIAPRKATLQPLPPNLPPVTYMHIYETDGFSLGVFLLKSGTSIPLHDHPGMHGM
LKVLYGTVRISCMDKLDAGGGQRPRALPPEQQFEPPLQPREREAVRPGVLRSRAEYTEAS
GPCILTPHRDNLHQIDAVEGPAAFLDILAPPYDPDDGRDCHYYRVLEPVRPKEASSSACD
LPREVWLLETPQADDFWCEGEPYPGPKVFP
Enzyme 4 Number of Residues 270
Enzyme 4 Molecular Weight 29751
Enzyme 4 Theoretical pI Not Available
Enzyme 4 GO Classification Not Available
Enzyme 4 General Function Not Available
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
  • None
Enzyme 4 Transmembrane Regions
  • None
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein Not Available
Enzyme 4 UniProtKB/Swiss-Prot ID B1AL29 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name B1AL29_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 Not Available
Enzyme 4 GeneCard ID B1AL29 Link Image
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 SNPJam Report Link Image
Enzyme 4 General References Not Available
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 14386
Enzyme 5 Name 2-aminoethanethiol dioxygenase
Enzyme 5 Synonyms
  1. Cysteamine dioxygenase
Enzyme 5 Gene Name ADO
Enzyme 5 Protein Sequence >2-aminoethanethiol dioxygenase 
MPRDNMASLIQRIARQACLTFRGSGGGRGASDRDAASGPEAPMQPGFPENLSKLKSLLTQ
LRAEDLNIAPRKATLQPLPPNLPPVTYMHIYETDGFSLGVFLLKSGTSIPLHDHPGMHGM
LKVLYGTVRISCMDKLDAGGGQRPRALPPEQQFEPPLQPREREAVRPGVLRSRAEYTEAS
GPCILTPHRDNLHQIDAVEGPAAFLDILAPPYDPDDGRDCHYYRVLEPVRPKEASSSACD
LPREVWLLETPQADDFWCEGEPYPGPKVFP
Enzyme 5 Number of Residues 270
Enzyme 5 Molecular Weight 29751
Enzyme 5 Theoretical pI 5.91
Enzyme 5 GO Classification Not Available
Enzyme 5 General Function Not Available
Enzyme 5 Specific Function 2-aminoethanethiol + O(2) = hypotaurine
Enzyme 5 Pathways
  • Taurine and Hypotaurine Metabolism (map00430 Link Image)
Enzyme 5 Reactions
  • 2-aminoethanethiol + O2 = hypotaurine [RN:R02467] ALL_REAC R02467
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • None
Enzyme 5 Transmembrane Regions
  • None
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 66840146 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID Q96SZ5 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name AEDO_HUMAN Link Image
Enzyme 5 PDB ID Not Available
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence >813 bp 
ATGCCCCGAGACAACATGGCCTCCTTGATCCAACGGATCGCCCGCCAGGCTTGCCTCACC
TTCCGGGGCAGCTGGGGCGGCCGCGGCGCTTCCGATCGCGACGCGGCTTCTGGCGCGGAG
GCGCCGATGCAGCCGGGCTTCCCCGAGAACCTGAGCAAGCTGAAGAGCCTCCTGACCCAG
CTCCGCGCCGAGGACTTGAACATCGCCCCGCGCAAGGCCACACTGCAGCCGCTGCCGCCC
AACCTGCCGCCAGTCACCTACATGCACATCTACGAGACGGACGGCTTCAGCCTGGGCGTG
TTCCTGCTCAAGAGCGGCACGTCCATCCCGCTGCACGACCACCCGGGCATGCACGGCATG
CTCAAGGTGCTGTACGGCACCGTGCGCATCAGCTGCATGGACAAGCTAGACGCGGGCGGC
GGGCAACGGCCGCGGGCCTTGCCGCCCGAGCAGCAGTTCGAGCCGCCGCTGCAGCCCCGG
GAGCGAGAAGCCGTGCGGCCGGGCGTGCTGCGTTCGCGGGCCGAGTACACCGAGGCCAGC
GGCCCCTGCATCCTCACACCGCACCGGGACAACCTGCACCAGATCGACGCCGTGGAAGGG
CCTGCCGCCTTCCTGGACATCCTGGCCCCGCCCTACGACCCGGACGATGGCCGGGACTGC
CACTATTACCGGGTGCTGGAGCCGGTCAGGCCCAAGGAGGCCTCCAGCTCGGCCTGTGAC
CTGCCTCGAGAGGTGTGGCTCCTGGAGACCCCACAGGCCGATGACTTCTGGTGCGAGGGA
GAACCCTATCCAGGTCCCAAGGTCTTCCCTTGA
Enzyme 5 GenBank Gene ID BC018660 Link Image
Enzyme 5 GeneCard ID Q96SZ5 Link Image
Enzyme 5 GenAtlas ID ADO Link Image
Enzyme 5 HGNC ID HGNC:23506 Link Image
Enzyme 5 Chromosome Location 10
Enzyme 5 Locus 10q21.2
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References Not Available
Enzyme 5 Metabolite References Not Available