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 Adenylsuccinic acid (HMDB00536)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2009-05-05 20:58:03
Accession Number HMDB00536
Secondary Accession Numbers HMDB01332; HMDB11633
Common Name Adenylsuccinic acid
Description Adenylsuccinic acid is a substrate of the enzyme adenylosuccinase [EC 4.3.2.2] in purine metabolism pathway. The accumulation of adenylsuccinic acid in body fluids occurs due to a deficiency of adenylosuccinase. (KEGG; PMID 8412002)
Synonyms
  1. 6-Succino-5'-adenylate
  2. 6-Succino-5'-adenylic acid
  3. Adenylsuccinate
  4. Adenylsuccinic acid
  5. Aspartyl adenylate
  6. D-ribofuranosyl)-9H-purin-6-yl]
  7. D-ribofuranosyl-9H-purin-6-yl) mono(dihydrogen phosphate) (ester)
  8. Succinyl AMP
  9. Succinyladenosine 5'-monophosphate
  10. Succinyladenosine monophosphorate
  11. Succinyladenosine monophosphoric acid
  12. adenyl-Succinic acid
  13. adenylosuccinate
  14. adenylosuccinic acid;N(6)-(1,2-dicarboxyethyl)-AMP
Chemical IUPAC Name 2-[[9-[(2R,3R,4S,5R)-3,4-dihydroxy-5-(phosphonooxymethyl)oxolan-2-yl]purin-6-yl]amino]butanedioic acid
Chemical Formula C14H18N5O11P
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Nucleosides and Nucleoside conjugates
Class
  • Nucleotides
Sub Class
  • Nucleotide monophosphates
Family
  • Mammalian Metabolite
Species
  • secondary alcohol
  • 1,2-diol
  • secondary amine
  • secondary aliphatic/aromatic amine (alkylarylamine)
  • carboxylic acid
  • phosphoric acid ester
  • aromatic compound
  • heterocyclic compound
  • alpha-aminoacid
Biofunction
—
Application
—
Source
  • Endogenous
Average Molecular Weight 463.293
Monoisotopic Molecular Weight 463.074036
Isomeric SMILES O[C@@H]1[C@@H](COP(O)(O)=O)O[C@H]([C@@H]1O)N1C=NC2=C1N=CN=C2NC(CC(O)=O)C(O)=O
Canonical SMILES OC1C(COP(O)(O)=O)OC(C1O)N1C=NC2=C1N=CN=C2NC(CC(O)=O)C(O)=O
KEGG Compound ID C03794 Link Image
BioCyc ID Not Available
BiGG ID Not Available
Wikipedia Link Adenylsuccinate Link Image
NuGOwiki Link HMDB00536 Link Image
Metagene Link HMDB00536 Link Image
METLIN ID 5521 Link Image
PubChem Compound 440122 Link Image
PubChem Substance 46509168 Link Image
ChEBI ID 15919 Link Image
CAS Registry Number 19046-78-7
InChI Identifier InChI=1/C14H18N5O11P/c20-7(21)1-5(14(24)25)18-11-8-12(16-3-15-11)19(4-17-8)13-10(23)9(22)6(30-13)2-29-31(26,27)28/h3-6,9-10,13,22-23H,1-2H2,(H,20,21)(H,24,25)(H,15,16,18)(H2,26,27,28)/t5?,6-,9-,10-,13-/m1/s1
Synthesis Reference Buck, Ildiko; Reese, Colin B. An unambiguous synthesis of adenylosuccinic acid and its constituent nucleoside. Journal of the Chemical Society, Perkin Transactions 1: Organic and Bio-Organic Chemistry (1972-1999) (1990), (11), 2937-42.
Melting Point (Experimental) Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 2.38 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -4
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity -5.1 [Predicted by PubChem via XLOGP]; -1.96 [Predicted by ALOGPS] 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 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
Biofluid Location Not Available
Tissue Location Not Available
Concentrations (Normal) Not Available
Concentrations (Abnormal) Not Available
Associated Disorders Not Available
OMIM ID Not Available
Pathways
Name SMPDB Link KEGG Link
Aspartate Metabolism SMP00067 Link Image map00250 Link Image
Purine Metabolism SMP00050 Link Image map00230 Link Image
General References
  1. Van den Bergh F, Vincent MF, Jaeken J, Van den Berghe G: Residual adenylosuccinase activities in fibroblasts of adenylosuccinase-deficient children: parallel deficiency with adenylosuccinate and succinyl-AICAR in profoundly retarded patients and non-parallel deficiency in a mildly retarded girl. J Inherit Metab Dis. 1993;16(2):415-24. [PubMed Link Image]
  2. Wikipedia Link Image
Metabolic Enzymes
  1. Adenylosuccinate lyase
  2. Adenylosuccinate synthetase isozyme 1
  3. Adenylosuccinate synthetase
Enzyme 1 [top]
Enzyme 1 ID 5857
Enzyme 1 Name Adenylosuccinate lyase
Enzyme 1 Synonyms
  1. Adenylosuccinase
  2. ASL
  3. ASASE
Enzyme 1 Gene Name ADSL
Enzyme 1 Protein Sequence >Adenylosuccinate lyase 
MAAGGDHGSPDSYRSPLASRYASPEMCFVFSDRYKFRTWRQLWLWLAEAEQTLGLPITDE
QIQEMKSNLENIDFKMAAEEEKRLRHDVMAHVHTFGHCCPKAAGIIHLGATSCYVGDNTD
LIILRNALDLLLPKLARVISRLADFAKERASLPTLGFTHFQPAQLTTVGKRCCLWIQDLC
MDLQNLKRVRDDLRFRGVKGTTGTQASFLQLFEGDDHKVEQLDKMVTEKAGFKRAFIITG
QTYTRKVDIEVLSVLASLGASVHKICTDIRLLANLKEMEEPFEKQQIGSSAMPYKRNPMR
SERCCSLARHLMTLVMDPLQTASVQWFERTLDDSANRRICLAEAFLTADTILNTLQNISE
GLVVYPKVIERRIRQELPFMATENIIMAMVKAGGSRQDCHEKIRVLSQQAASVVKQEGGD
NDLIERIQVDAYFSPIHSQLDHLLDPSSFTGRASQQVQRFLEEEVYPLLKPYESVMKVKA
ELCL
Enzyme 1 Number of Residues 484
Enzyme 1 Molecular Weight 54890
Enzyme 1 Theoretical pI 7.12
Enzyme 1 GO Classification
Function
  • adenylosuccinate lyase activity
  • amidine-lyase activity
  • carbon-nitrogen lyase activity
  • catalytic activity
  • lyase activity
Process
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleotide metabolism
  • physiological process
  • purine nucleotide biosynthesis
  • purine nucleotide metabolism
  • purine ribonucleotide biosynthesis
Component
—
Enzyme 1 General Function Nucleotide transport and metabolism
Enzyme 1 Specific Function 6-N-(1,2-dicarboxyethyl)AMP = fumarate + AMP
Enzyme 1 Pathways
Enzyme 1 Reactions
  • (1) N6-(1,2-dicarboxyethyl)AMP = fumarate + AMP
  • (2) (S)-2-[5-amino-1-(5-phospho-D-ribosyl)imidazole-4- carboxamido]succinate = fumarate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 28904 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID P30566 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name PUR8_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >1455 bp 
ATGGCGGCTGGAGGCGATCATGGTTCGCCCGACAGCTACCGCTCACCTCTTGCCTCCCGC
TATGCCAGCCCGGAGATGTGCTTCGTGTTTAGCGACAGGTATAAATTCCGGACATGGCGG
CAGCTGTGGCTGTGGCTGGCGGAGGCCGAGCAGACATTGGGTTTGCCTATCACAGATGAA
CAAATCCAGGAGATGAAATCAAACCTGGAGAACATAGACTTCAAGATGGCAGCTGAGGAA
GAGAAACGTTTACGACATGATGTGATGGCTCACGTGCACACATTTGGCCACTGCTGTCCA
AAAGCTGCAGGCATTATTCACCTTGGTGCTACTTCTTGCTATGTTGGAGACAATACTGAC
TTGATTATTCTTAGAAATGCACTTGACCTGCTTTTGCCAAAGCTTGCCAGAGTGATCTCT
CGGCTTGCCGACTTTGCTAAGGAACGAGCCAGTCTACCCACATTAGGTTTCACACATTTC
CAGCCTGCACAGCTGACCACAGTTGGGAAACGTTGCTGTCTTTGGATTCAGGATCTTTGC
ATGGATCTCCAGAACTTGAAGCGTGTCCGAGATGACCTGCGCTTCCGGGGAGTAAAGGGT
ACCACTGGCACTCAGGCCAGTTTCCTGCAGCTCTTTGAGGGAGATGACCATAAGGTAGAG
CAGCTTGACAAGATGGTGACAGAAAAGGCAGGATTTAAGAGAGCTTTCATCATCACAGGG
CAGACATATACACGAAAAGTGGATATTGAAGTACTGTCTGTGCTGGCTAGCTTGGGGGCA
TCAGTGCACAAGATTTGCACCGACATACGCCTCCTGGCAAACCTCAAGGAGATGGAGGAA
CCCTTTGAAAAACAGCAGATTGGCTCAAGTGCGATGCCATATAAGCGGAATCCCATGCGT
TCAGAACGTTGCTGCAGTCTTGCCCGCCACCTGATGACCCTTGTCATGGACCCGCTACAG
ACAGCATCTGTCCAGTGGTTTGAACGCACACTGGATGATAGTGCCAACCGACGGATCTGT
TTGGCCGAGGCATTTCTTACCGCAGATACTATATTGAATACGCTGCAGAACATTTCTGAA
GGATTGGTCGTGTACCCCAAAGTAATTGAACGGCGCATTCGGCAAGAGCTGCCTTTCATG
GCCACAGAGAACATCATCATGGCCATGGTCAAAGCTGGAGGTAGCCGCCAGGATTGCCAT
GAGAAAATCAGAGTGCTTTCTCAGCAGGCAGCTTCTGTGGTTAAGCAGGAAGGGGGTGAC
AATGACCTCATAGAGCGTATCCAGGTTGATGCCTACTTCAGTCCCATTCACTCCCAGTTG
GATCATTTACTGGATCCTTCTTCTTTCACTGGTCGTGCCTCCCAGCAGGTGCAGAGATTC
TTAGAAGAGGAGGTGTATCCCCTGTTAAAACCATATGAAAGCGTGATGAAGGTGAAAGCA
GAATTATGTCTGTAG
Enzyme 1 GenBank Gene ID X65867 Link Image
Enzyme 1 GeneCard ID ADSL Link Image
Enzyme 1 GenAtlas ID ADSL Link Image
Enzyme 1 HGNC ID HGNC:291 Link Image
Enzyme 1 Chromosome Location 22
Enzyme 1 Locus 22q13.1|22q13.2
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Kmoch S, Hartmannova H, Stiburkova B, Krijt J, Zikanova M, Sebesta I: Human adenylosuccinate lyase (ADSL), cloning and characterization of full-length cDNA and its isoform, gene structure and molecular basis for ADSL deficiency in six patients. Hum Mol Genet. 2000 Jun 12;9(10):1501-13. [PubMed Link Image]
  2. Dunham I, Shimizu N, Roe BA, Chissoe S, Hunt AR, Collins JE, Bruskiewich R, Beare DM, Clamp M, Smink LJ, Ainscough R, Almeida JP, Babbage A, Bagguley C, Bailey J, Barlow K, Bates KN, Beasley O, Bird CP, Blakey S, Bridgeman AM, Buck D, Burgess J, Burrill WD, O'Brien KP, et al.: The DNA sequence of human chromosome 22. Nature. 1999 Dec 2;402(6761):489-95. [PubMed Link Image]
  3. Stone RL, Aimi J, Barshop BA, Jaeken J, Van den Berghe G, Zalkin H, Dixon JE: A mutation in adenylosuccinate lyase associated with mental retardation and autistic features. Nat Genet. 1992 Apr;1(1):59-63. [PubMed Link Image]
  4. Verginelli D, Luckow B, Crifo C, Salerno C, Gross M: Identification of new mutations in the adenylosuccinate lyase gene associated with impaired enzyme activity in lymphocytes and red blood cells. Biochim Biophys Acta. 1998 Feb 27;1406(1):81-4. [PubMed Link Image]
  5. Marie S, Cuppens H, Heuterspreute M, Jaspers M, Tola EZ, Gu XX, Legius E, Vincent MF, Jaeken J, Cassiman JJ, Van den Berghe G: Mutation analysis in adenylosuccinate lyase deficiency: eight novel mutations in the re-evaluated full ADSL coding sequence. Hum Mutat. 1999;13(3):197-202. [PubMed Link Image]
  6. Race V, Marie S, Vincent MF, Van den Berghe G: Clinical, biochemical and molecular genetic correlations in adenylosuccinate lyase deficiency. Hum Mol Genet. 2000 Sep 1;9(14):2159-65. [PubMed Link Image]
  7. Castro M, Perez-Cerda C, Merinero B, Garcia MJ, Bernar J, Gil Nagel A, Torres J, Bermudez M, Garavito P, Marie S, Vincent F, Van den Berghe G, Ugarte M: Screening for adenylosuccinate lyase deficiency: clinical, biochemical and molecular findings in four patients. Neuropediatrics. 2002 Aug;33(4):186-9. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 6166
Enzyme 2 Name Adenylosuccinate synthetase isozyme 1
Enzyme 2 Synonyms
  1. IMP--aspartate ligase 1
  2. AdSS 1
  3. AMPSase 1
Enzyme 2 Gene Name ADSSL1
Enzyme 2 Protein Sequence >Adenylosuccinate synthetase isozyme 1 
MSGTRASNDRPPGAGGVKRGRLQQEAAATGSRVTVVLGAQWGDEGKGKVVDLLATDADII
SRCQGGNNAGHTVVVDGKEYDFHLLPSGIINTKAVSFIGNGVVIHLPGLFEEAEKNEKKG
LKDWEKRLIISDRAHLVFDFHQAVDGLQEVQRQAQEGKNIGTTKKGIGPTYSSKAARTGL
RICDLLSDFDEFSSRFKNLAHQHQSMFPTLEIDIEGQLKRLKGFAERIRPMVRDGVYFMY
EALHGPPKKILVEGANAALLDIDFGTYPFVTSSNCTVGGVCTGLGIPPQNIGDVYGVVKA
YTTRVGIGAFPTEQINEIGGLLQTRGHEWGVTTGRKRRCGWLDLMILRYAHMVNGFTALA
LTKLDILDVLGEVKVGVSYKLNGKRIPYFPANQEMLQKVEVEYETLPGWKADTTGARRWE
DLPPQAQNYIRFVENHVGVAVKWVGVGKSRESMIQLF
Enzyme 2 Number of Residues 457
Enzyme 2 Molecular Weight 50209
Enzyme 2 Theoretical pI 8.85
Enzyme 2 GO Classification
Function
  • GTP binding
  • adenylosuccinate synthase activity
  • binding
  • catalytic activity
  • guanyl nucleotide binding
  • ligase activity
  • ligase activity, forming carbon-nitrogen bonds
  • nucleotide binding
  • purine nucleotide binding
Process
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleotide metabolism
  • physiological process
  • purine nucleotide biosynthesis
  • purine nucleotide metabolism
Component
—
Enzyme 2 General Function Nucleotide transport and metabolism
Enzyme 2 Specific Function Plays an important role in the de novo pathway of purine nucleotide biosynthesis
Enzyme 2 Pathways
Enzyme 2 Reactions
  • GTP + IMP + L-aspartate = GDP + phosphate + N6-(1,2-dicarboxyethyl)-AMP
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 21303413 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID Q8N142 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name PURA1_HUMAN Link Image
Enzyme 2 PDB ID 1MF1 Link Image
Enzyme 2 PDB File Show
Enzyme 2 3D Structure
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >1374 bp 
ATGTCGGGGACCCGAGCCTCCAACGACCGGCCCCCCGGCGCAGGCGGCGTCAAGCGGGGG
CGGCTGCAGCAGGAGGCGGCGGCGACCGGCTCCCGCGTGACGGTGGTGCTGGGCGCGCAG
TGGGGGGACGAGGGCAAAGGCAAGGTGGTGGACCTGCTGGCCACGGACGCCGACATCATC
AGCCGCTGCCAGGGGGGCAACAACGCCGGCCACACGGTGGTGGTGGATGGGAAAGAGTAC
GACTTCCACCTGCTGCCCAGCGGCATCATCAACACCAAGGCCGTGTCCTTCATTGGCAAC
GGGGTGGTCATCCACTTGCCAGGCTTGTTTGAGGAAGCAGAGAAGAATGAAAAGAAAGGC
CTGAAGGACTGGGAGAAGAGGCTCATCATCTCTGACAGAGCCCACCTTGTGTTTGATTTT
CACCAGGCTGTCGACGGACTTCAGGAAGTGCAGCGCCAGGCACAAGAGGGGAAGAATATA
GGCACCACCAAGAAGGGAATCGGACCAACCTACTCTTCCAAAGCTGCCCGGACAGGCCTC
CGCATCTGCGACCTCCTGTCAGATTTTGATGAGTTTTCCTCCAGATTCAAGAACCTGGCC
CACCAGCACCAGTCGATGTTCCCCACCCTGGAAATAGACATTGAAGGCCAACTCAAAAGG
CTCAAGGGCTTTGCTGAGCGGATCAGACCCATGGTCCGAGATGGTGTTTACTTTATGTAT
GAGGCACTCCACGGCCCCCCCAAGAAGATCCTGGTGGAGGGTGCCAACGCCGCCCTCCTC
GACATTGACTTCGGGACCTACCCCTTTGTGACTTCATCCAACTGCACCGTGGGCGGTGTG
TGCACGGGCCTGGGCATCCCCCCGCAGAACATAGGTGACGTGTATGGCGTGGTGAAAGCC
TATACCACACGTGTGGGCATCGGGGCCTTCCCCACCGAGCAGATCAACGAGATTGGAGGC
CTGCTGCAGACCCGCGGCCACGAGTGGGGAGTGACCACAGGCAGGAAGAGGCGCTGCGGC
TGGCTCGACCTGATGATTCTAAGATATGCTCACATGGTCAACGGATTCACTGCGCTGGCC
CTGACGAAGCTGGACATCCTGGACGTACTGGGTGAGGTTAAAGTCGGTGTCTCATACAAG
CTGAACGGGAAAAGGATTCCCTATTTCCCAGCTAACCAGGAGATGCTTCAGAAGGTCGAA
GTTGAGTATGAAACGCTGCCTGGGTGGAAAGCAGACACCACAGGCGCCAGGAGGTGGGAG
GACCTGCCCCCACAGGCCCAGAACTACATCCGCTTTGTGGAGAATCACGTGGGAGTCGCA
GTCAAATGGGTTGGTGTTGGCAAGTCAAGAGAGTCGATGATCCAGCTGTTTTAG
Enzyme 2 GenBank Gene ID AY037159 Link Image
Enzyme 2 GeneCard ID ADSSL1 Link Image
Enzyme 2 GenAtlas ID ADSSL1 Link Image
Enzyme 2 HGNC ID HGNC:20093 Link Image
Enzyme 2 Chromosome Location 14
Enzyme 2 Locus 14q32.33
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 16506
Enzyme 3 Name Adenylosuccinate synthetase
Enzyme 3 Synonyms Not Available
Enzyme 3 Gene Name ADSS
Enzyme 3 Protein Sequence >Adenylosuccinate synthetase 
MAFAETYPAASSLPNGDCGRPRARPGGNRVTVVLGAQWGDEGKGKVVDLLAQDADIVCRC
QGGNNAGHTVVVDSVEYDFHLLPSGIINPNVTAFIGNGVVIHLPGLFEEAEKNVQKGKGL
EGWEKRLIISDRAHIVFDFHQAADGIQEQQRQEQAGKNLGTTKKGIGPVYSSKAARSGLR
MCDLVSDFDGFSERFKVLANQYKSIYPTLEIDIEGELQKLKGYMEKIKPMVRDGVYFLYE
ALHGPPKKILVEGANAALLDIDFGTYPFVTSSNCTVGGVCTGLGMPPQNVGEVYGVVKAY
TTRVGIGAFPTEQDNEIGELLQTRGREFGVTTGRKRRCGWLDLVLLKYAHMINGFTALAL
TKLDILDMFTEIKVGVAYKLDGEIIPHIPANQEVLNKVEVQYKTLPGWNTDISNARAFKE
LPVNAQNYVRFIEDELQIPVKWIGVGKSRESMIQLF
Enzyme 3 Number of Residues 456
Enzyme 3 Molecular Weight 50098
Enzyme 3 Theoretical pI 6.52
Enzyme 3 GO Classification
Function
  • GTP binding
  • adenylosuccinate synthase activity
  • binding
  • catalytic activity
  • guanyl nucleotide binding
  • ligase activity
  • ligase activity, forming carbon-nitrogen bonds
  • nucleotide binding
  • purine nucleotide binding
Process
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleotide metabolism
  • physiological process
  • purine nucleotide biosynthesis
  • purine nucleotide metabolism
Component
—
Enzyme 3 General Function Nucleotide transport and metabolism
Enzyme 3 Specific Function Plays an important role in the de novo pathway of purine nucleotide biosynthesis
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 Not Available
Enzyme 3 UniProtKB/Swiss-Prot ID B1AQM5 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name B1AQM5_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence Not Available
Enzyme 3 GenBank Gene ID AL591594 Link Image
Enzyme 3 GeneCard ID B1AQM5 Link Image
Enzyme 3 GenAtlas ID Not Available
Enzyme 3 HGNC ID Not Available
Enzyme 3 Chromosome Location Not Available
Enzyme 3 Locus Not Available
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References Not Available
Enzyme 3 Metabolite References Not Available