| 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 |
- 5-Amino-4-imidazole-N-succinocarboxamide ribonucleotide
- 5'-Phosphoribosyl-4-(N-succinocarbozamide)-5-aminoimidazole
- L-N-[(5-amino-1-b-D-ribofuranosylimidazol-4-yl)carbonyl]-5'-(dihydrogen phosphate)
- N-(5-Amino-1-ribofuranosylimidazol-4-ylcarbonyl)aspartic acid 5'-phosphate
- N-[5-Amino-1-(5'-phosphoribofuranosyl)-4-imidazolecarbonyl]aspartate
- N-[5-Amino-1-(5'-phosphoribofuranosyl)-4-imidazolecarbonyl]aspartic acid
- SAICAR
- SAICAriboside
- Succinylaminoimidazole carboxamide riboside
- Succino-AICAR
- L-N-[(5-amino-1-beta-delta-ribofuranosylimidazol-4-yl)carbonyl]-5'-(dihydrogen phosphate)
- 1-(5'-Phosphoribosyl)-5-amino-4-(N-succinocarboxamide)-imidazole
- 1-(5'-Phosphoribosyl)-4-(N-succinocarboxamide)-5-aminoimidazole
- 5'-Phosphoribosyl-4-(N-succinocarboxamide)-5-aminoimidazole
- (S)-2-[5-Amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate
- (S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido)succinate
- (S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido)succinic acid
- 1-(5'-Phosphoribosyl)-5-amino-4-(N-succinocarboxamide)-imidazole' 1-(5'-Phosphoribosyl)-4-(N-succinocarboxamide)-5-aminoimidazole
- Phosphoribosylaminoimidazolesuccinocarboxamide
- (S)-2-[5-Amino-1-(5-phospho-delta-ribosyl)imidazole-4-carboxamido]succinate
- (S)-2-(5-amino-1-(5-phospho-delta-ribosyl)imidazole-4-carboxamido)succinate
- (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 |
 |
| Chemical Taxonomy |
| Kingdom |
|
| Super Class |
- Nucleosides and Nucleoside conjugates
|
| Class |
|
| Sub Class |
- Nucleotide monophosphates
|
| Family |
|
| 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 |
|
|
| 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  |
| BioCyc ID |
P-RIBOSYL-4-SUCCCARB-AMINOIMIDAZOLE  |
| BiGG ID |
44624  |
| Wikipedia Link |
Not Available |
| NuGOwiki Link |
HMDB00797  |
| Metagene Link |
HMDB00797  |
| METLIN ID |
5762  |
| PubChem Compound |
160666  |
| PubChem Substance |
841721  |
| ChEBI ID |
18319  |
| 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 |
|
| 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
]
|
|
| 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
]
|
|
| OMIM ID |
- 103050
(Adenylosuccinate lyase deficiency)
|
| Pathways |
|
| General 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
|
| Metabolic Enzymes |
- Adenylosuccinate lyase
- Multifunctional protein ADE2 [Includes: Phosphoribosylaminoimidazole- succinocarboxamide synthase
|
|
Enzyme 1
[top]
|
| Enzyme 1 ID |
5857 |
| Enzyme 1 Name |
Adenylosuccinate lyase |
| Enzyme 1 Synonyms |
- Adenylosuccinase
- ASL
- 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 |
|
| Enzyme 1 Transmembrane Regions |
|
| Enzyme 1 Essentiality |
Not Available |
| Enzyme 1 GenBank ID Protein |
28904  |
| Enzyme 1 UniProtKB/Swiss-Prot ID |
P30566  |
| Enzyme 1 UniProtKB/Swiss-Prot Entry Name |
PUR8_HUMAN  |
| 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  |
| Enzyme 1 GeneCard ID |
ADSL  |
| Enzyme 1 GenAtlas ID |
ADSL  |
| Enzyme 1 HGNC ID |
HGNC:291  |
| Enzyme 1 Chromosome Location |
22 |
| Enzyme 1 Locus |
22q13.1|22q13.2 |
| Enzyme 1 SNPs |
SNPJam Report  |
| Enzyme 1 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
|
| 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 |
- SAICAR synthetase
- Phosphoribosylaminoimidazole carboxylase
- AIR carboxylase
- 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 |
|
| Enzyme 2 Transmembrane Regions |
|
| Enzyme 2 Essentiality |
Not Available |
| Enzyme 2 GenBank ID Protein |
28384  |
| Enzyme 2 UniProtKB/Swiss-Prot ID |
P22234  |
| Enzyme 2 UniProtKB/Swiss-Prot Entry Name |
PUR6_HUMAN  |
| 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  |
| Enzyme 2 GeneCard ID |
PAICS  |
| Enzyme 2 GenAtlas ID |
PAICS  |
| Enzyme 2 HGNC ID |
HGNC:8587  |
| Enzyme 2 Chromosome Location |
4 |
| Enzyme 2 Locus |
4q12 |
| Enzyme 2 SNPs |
SNPJam Report  |
| Enzyme 2 General References |
- 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
]
|
| Enzyme 2 Metabolite References |
Not Available |