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 SAICAR (HMDB00797)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2009-08-06 13:27:11
Accession Number HMDB00797
Secondary Accession Numbers HMDB06274
Common Name SAICAR
Description SAICAR (or (S)-2-[5-Amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate) is a substrate for the multifunctional protein ADE2. SAICAR is an intermediate in purine metabolism. (S)-2-[5-Amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate is converted from 5-Amino-1-(5-phospho-D-ribosyl) imidazole-4-carboxylate via phosphoribosylaminoimidazole-succinocarboxamide synthase [EC: 6.3.2.6] or SAICAR synthase. This enzyme catalyses the seventh step out of ten in the biosynthesis of purine nucleotides. The appearance of succinylaminoimidazolecarboxamide riboside (SAICAriboside) and succinyladenosine (S-Ado) in cerebrospinal fluid, urine, and to a lesser extent in plasma is characteristic of a heritable deficiency Adenylosuccinate lyase deficiency. (Wikipedia)
Synonyms
  1. 5-Amino-4-imidazole-N-succinocarboxamide ribonucleotide
  2. 5'-Phosphoribosyl-4-(N-succinocarbozamide)-5-aminoimidazole
  3. L-N-[(5-amino-1-b-D-ribofuranosylimidazol-4-yl)carbonyl]-5'-(dihydrogen phosphate)
  4. N-(5-Amino-1-ribofuranosylimidazol-4-ylcarbonyl)aspartic acid 5'-phosphate
  5. N-[5-Amino-1-(5'-phosphoribofuranosyl)-4-imidazolecarbonyl]aspartate
  6. N-[5-Amino-1-(5'-phosphoribofuranosyl)-4-imidazolecarbonyl]aspartic acid
  7. SAICAR
  8. SAICAriboside
  9. Succinylaminoimidazole carboxamide riboside
  10. Succino-AICAR
  11. L-N-[(5-amino-1-beta-delta-ribofuranosylimidazol-4-yl)carbonyl]-5'-(dihydrogen phosphate)
  12. 1-(5'-Phosphoribosyl)-5-amino-4-(N-succinocarboxamide)-imidazole
  13. 1-(5'-Phosphoribosyl)-4-(N-succinocarboxamide)-5-aminoimidazole
  14. 5'-Phosphoribosyl-4-(N-succinocarboxamide)-5-aminoimidazole
  15. (S)-2-[5-Amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate
  16. (S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido)succinate
  17. (S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido)succinic acid
  18. 1-(5'-Phosphoribosyl)-5-amino-4-(N-succinocarboxamide)-imidazole' 1-(5'-Phosphoribosyl)-4-(N-succinocarboxamide)-5-aminoimidazole
  19. Phosphoribosylaminoimidazolesuccinocarboxamide
  20. (S)-2-[5-Amino-1-(5-phospho-delta-ribosyl)imidazole-4-carboxamido]succinate
  21. (S)-2-(5-amino-1-(5-phospho-delta-ribosyl)imidazole-4-carboxamido)succinate
  22. (S)-2-(5-amino-1-(5-phospho-delta-ribosyl)imidazole-4-carboxamido)succinic acid
Chemical IUPAC Name (2S)-2-[[5-amino-1-[(2R,3R,4S,5R)-3,4-dihydroxy-5-(phosphonooxymethyl)oxolan-2-yl]imidazole-4-carbonyl]amino]butanedioic acid
Chemical Formula C13H19N4O12P
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
  • primary amine
  • primary aromatic amine
  • carboxylic acid
  • secondary carboxylic acid amide
  • phosphoric acid ester
  • aromatic compound
  • heterocyclic compound
Biofunction
Application
Source
  • Endogenous
Average Molecular Weight 454.283
Monoisotopic Molecular Weight 454.073700
Isomeric SMILES NC1=C(N=CN1[C@@H]1O[C@H](COP(O)(O)=O)[C@@H](O)[C@H]1O)C(=O)N[C@@H](CC(O)=O)C(O)=O
Canonical SMILES NC1=C(N=CN1C1OC(COP(O)(O)=O)C(O)C1O)C(=O)NC(CC(O)=O)C(O)=O
KEGG Compound ID C04823 Link Image
BioCyc ID P-RIBOSYL-4-SUCCCARB-AMINOIMIDAZOLE Link Image
BiGG ID 44624 Link Image
Wikipedia Link Not Available
NuGOwiki Link HMDB00797 Link Image
Metagene Link HMDB00797 Link Image
METLIN ID 5762 Link Image
PubChem Compound 160666 Link Image
PubChem Substance 841721 Link Image
ChEBI ID 18319 Link Image
CAS Registry Number 3031-95-6
InChI Identifier InChI=1/C13H19N4O12P/c14-10-7(11(22)16-4(13(23)24)1-6(18)19)15-3-17(10)12-9(21)8(20)5(29-12)2-28-30(25,26)27/h3-5,8-9,12,20-21H,1-2,14H2,(H,16,22)(H,18,19)(H,23,24)(H2,25,26,27)/t4-,5+,8+,9+,12+/m0/s1
Synthesis Reference Shaw, Gordon; Thomas, Peter S.; Patey, Carole A. H.; Thomas, Susan E. Purines, pyrimidines and imidazoles. Part 50. Inhibition of adenylosuccinate AMP-lyase no. 4.3.2.2. by derivatives of N-(5-amino-1-b-D-ribofuranosylimidazole-4-carbonyl)-L-aspartic acid 5'-phosphate (SAICAR) and virazole 5'-phosphate. Journal of the Chemical Society, Perkin Transactions 1: Organic and Bio-Organic Chemistry (1972-1999) (1979), (6), 1415-24.
Melting Point (Experimental) Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 1.73 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -4
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity -1.82 [Predicted by ALOGPS]; -6.1 [Predicted by PubChem via XLOGP] Calculated using ALOGPS
Material Safety Data Sheet (MSDS) Not Available
MOL File Show
SDF File Show
PDB File Show
2D Structure
3D Structure
Experimental PDB ID Not Available
Experimental 1H NMR Spectrum Not Available
Experimental 13C NMR Spectrum Not Available
Experimental 13C HSQC Spectrum Not Available
Predicted 1H NMR Spectrum Show Image
Show Peaklist
Predicted 13C NMR Spectrum Show Image
Show Peaklist
Mass Spectrum Not Available
Simplified TOCSY Spectrum Not Available
BMRB Spectrum Not Available
Cellular Location Not Available
Biofluid Location
  • Cerebrospinal Fluid
Tissue Location
Tissue References
Fibroblasts
Intestine
Concentrations (Normal) Not Available
Concentrations (Abnormal)
Biofluid CSF
Value 921.0 (0.0-1842.0) uM
Age Adult:>18 yrs old
Sex N/A
Condition Adenylosuccinate lyase deficiency
Comments Not Available
References
  • Marinaki AM, Champion M, Kurian MA, Simmonds HA, Marie S, Vincent MF, van den Berghe G, Duley JA, Fairbanks LD: Adenylosuccinate lyase deficiency--first British case. Nucleosides Nucleotides Nucleic Acids. 2004 Oct;23(8-9):1231-3. [PubMed Link Image]
Associated Disorders
Condition References
Adenylosuccinate lyase deficiency
  • Marinaki AM, Champion M, Kurian MA, Simmonds HA, Marie S, Vincent MF, van den Berghe G, Duley JA, Fairbanks LD: Adenylosuccinate lyase deficiency--first British case. Nucleosides Nucleotides Nucleic Acids. 2004 Oct;23(8-9):1231-3. [PubMed Link Image]
OMIM ID
  • 103050 Link Image (Adenylosuccinate lyase deficiency)
Pathways
Name SMPDB Link KEGG Link
Purine Metabolism SMP00050 Link Image map00230 Link Image
General References
  1. Marinaki AM, Champion M, Kurian MA, Simmonds HA, Marie S, Vincent MF, van den Berghe G, Duley JA, Fairbanks LD: Adenylosuccinate lyase deficiency--first British case. Nucleosides Nucleotides Nucleic Acids. 2004 Oct;23(8-9):1231-3. [PubMed Link Image]
  2. Laikind PK, Seegmiller JE, Gruber HE: Detection of 5'-phosphoribosyl-4-(N-succinylcarboxamide)-5-aminoimidazole in urine by use of the Bratton-Marshall reaction: identification of patients deficient in adenylosuccinate lyase activity. Anal Biochem. 1986 Jul;156(1):81-90. [PubMed Link Image]
  3. 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]
  4. Zikanova M, Krijt J, Hartmannova H, Kmoch S: Preparation of 5-amino-4-imidazole-N-succinocarboxamide ribotide, 5-amino-4-imidazole-N-succinocarboxamide riboside and succinyladenosine, compounds usable in diagnosis and research of adenylosuccinate lyase deficiency. J Inherit Metab Dis. 2005;28(4):493-9. [PubMed Link Image]
  5. 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]
  6. Wevers RA, Engelke UF, Moolenaar SH, Brautigam C, de Jong JG, Duran R, de Abreu RA, van Gennip AH: 1H-NMR spectroscopy of body fluids: inborn errors of purine and pyrimidine metabolism. Clin Chem. 1999 Apr;45(4):539-48. [PubMed Link Image]
Metabolic Enzymes
  1. Adenylosuccinate lyase
  2. Multifunctional protein ADE2 [Includes: Phosphoribosylaminoimidazole- succinocarboxamide synthase
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 6176
Enzyme 2 Name Multifunctional protein ADE2 [Includes: Phosphoribosylaminoimidazole- succinocarboxamide synthase
Enzyme 2 Synonyms
  1. SAICAR synthetase
  2. Phosphoribosylaminoimidazole carboxylase
  3. AIR carboxylase
  4. AIRC]
Enzyme 2 Gene Name PAICS
Enzyme 2 Protein Sequence >Multifunctional protein ADE2 [Includes: Phosphoribosylaminoimidazole- succinocarboxamide synthase
MATAEVLNIGKKLYEGKTKEVYELLDSPGKVLLQSKDQITAGNAARKNHLEGKAAISNKI
TSCIFQLLQEAGIKTAFTRKCGETAFIAPQCEMIPIEWVCRRIATGSFLKRNPGVKEGYK
FYPPKVELFFKDDANNDPQWSEEQLIAAKFCFAGLLIGQTEVDIMSHATQAIFEILEKSW
LPQNCTLVDMKIEFGVDVTTKEIVLADVIDNDSWRLWPSGDRSQQKDKQSYRDLKEVTPE
GLQMVKKNFEWVAERVELLLKSESQCRVVVLMGSTSDLGHCEKIKKACGNFGIPCELRVT
SAHKGPDETLRIKAEYEGDGIPTVFVAVAGRSNGLGPVMSGNTAYPVISCPPLTPDWGVQ
DVWSSLRLPSGLGCSTVLSPEGSAQFAAQIFGLSNHLVWSKLRASILNTWISLKQADKKI
RECNL
Enzyme 2 Number of Residues 425
Enzyme 2 Molecular Weight 47080
Enzyme 2 Theoretical pI 7.26
Enzyme 2 GO Classification
Function
  • acid-amino acid ligase activity
  • carbon-carbon lyase activity
  • carboxy-lyase activity
  • catalytic activity
  • ligase activity
  • ligase activity, forming carbon-nitrogen bonds
  • lyase activity
  • phosphoribosylaminoimidazole carboxylase activity
  • phosphoribosylaminoimidazolesuccinocarboxamide synthase activity
Process
  • 'de novo' IMP biosynthesis
  • IMP biosynthesis
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleotide metabolism
  • physiological process
  • purine nucleoside monophosphate biosynthesis
  • purine nucleotide biosynthesis
  • purine nucleotide metabolism
  • purine ribonucleoside monophosphate biosynthesis
Component
  • phosphoribosylaminoimidazole carboxylase complex
  • protein complex
  • unlocalized protein complex
Enzyme 2 General Function Nucleotide transport and metabolism
Enzyme 2 Specific Function ATP + 5-amino-1-(5-phospho-D- ribosyl)imidazole-4-carboxylate + L-aspartate = ADP + phosphate + (S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4- carboxamido)succinate
Enzyme 2 Pathways
Enzyme 2 Reactions
  • ATP + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + L-aspartate = ADP + phosphate + (S)-2-[5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 28384 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID P22234 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name PUR6_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >1278 bp
ATGGCGACAGCTGAGGTACTGAACATTGGTAAAAAATTATATGAGGGTAAAACAAAAGAA
GTCTACGAATTGTTAGACAGTCCAGGAAAAGTCCTCCTGCAGTCCAAGGACCAGATTACA
GCAGGAAATGCAGCTAGAAAAAACCACCTGGAAGGAAAAGCTGCAATCTCAAATAAAATC
ACCAGTTGTATTTTTCAGTTATTACAGGAAGCAGGTATTAAAACTGCCTTCACCAGAAAA
TGTGGGGAGACAGCTTTCATTGCACCGCAGTGTGAAATGATTCCAATTGAATGGGTTTGC
AGAAGAATAGCAACTGGTTCTTTTCTCAAAAGAAATCCTGGTGTCAAGGAAGGATATAAG
TTTTACCCACCTAAAGTGGAGTTGTTTTTCAAGGATGATGCCAATAATGACCCACAGTGG
TCTGAGGAACAGCTGATTGCTGCAAAATTTTGCTTTGCTGGACTTCTTATAGGCCAGACT
GAAGTGGATATCATGAGTCATGCTACACAGGCTATATTTGAAATACTGGAGAAATCCTGG
TTGCCCCAGAATTGTACACTGGTTGATATGAAGATTGAATTTGGTGTTGATGTAACCACC
AAAGAAATTGTTCTTGCTGATGTTATTGACAATGATTCCTGGAGACTCTGGCCATCAGGA
GATCGAAGCCAACAGAAAGACAAACAGTCTTATCGGGACCTCAAAGAAGTAACTCCTGAA
GGGCTCCAAATGGTAAAGAAAAACTTTGAGTGGGTTGCAGAGAGAGTAGAGTTGCTTTTG
AAATCAGAAAGTCAGTGCAGGGTTGTAGTGTTGATGGGCTCTACTTCTGATCTTGGTCAC
TGTGAAAAAATCAAGAAGGCCTGTGGAAATTTTGGCATTCCATGTGAACTTCGAGTAACA
TCTGCGCATAAAGGACCAGATGAAACTCTGAGGATTAAAGCTGAGTATGAAGGGGATGGC
ATTCCTACTGTATTTGTGGCAGTGGCAGGCAGAAGTAATGGTTTGGGACCAGTGATGTCT
GGGAACACTGCATATCCAGTTATCAGCTGTCCTCCCCTCACACCAGACTGGGGAGTTCAG
GATGTGTGGTCTTCTCTTCGACTACCCAGTGGTCTTGGCTGTTCAACCGTACTTTCTCCA
GAAGGATCAGCTCAATTTGCTGCTCAGATATTTGGGTTAAGCAACCATTTGGTATGGAGC
AAACTGCGAGCAAGCATTTTGAACACATGGATTTCCTTGAAGCAGGCTGACAAGAAAATC
AGAGAATGTAATTTATAA
Enzyme 2 GenBank Gene ID X53793 Link Image
Enzyme 2 GeneCard ID PAICS Link Image
Enzyme 2 GenAtlas ID PAICS Link Image
Enzyme 2 HGNC ID HGNC:8587 Link Image
Enzyme 2 Chromosome Location 4
Enzyme 2 Locus 4q12
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Minet M, Lacroute F: Cloning and sequencing of a human cDNA coding for a multifunctional polypeptide of the purine pathway by complementation of the ade2-101 mutant in Saccharomyces cerevisiae. Curr Genet. 1990 Nov;18(4):287-91. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available