| 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
|
|
Enzyme 1
[top]
|
| Enzyme 1 ID |
5857 |
| Enzyme 1 Name |
Adenylosuccinate lyase |
| Enzyme 1 Synonyms |
- ASL
- Adenylosuccinase
- 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 |
54888.7 |
| Enzyme 1 Theoretical pI |
7.12 |
| Enzyme 1 GO Classification |
| Function |
- N6-(1,2-dicarboxyethyl)AMP AMP-lyase (fumarate-forming) activity
- amidine-lyase activity
- carbon-nitrogen lyase activity
- catalytic activity
- lyase activity
|
| Process |
- cellular nitrogen compound metabolic process
- metabolic process
- nitrogen compound metabolic process
- nucleobase, nucleoside and nucleotide metabolic process
- nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
- nucleoside phosphate metabolic process
- nucleotide metabolic process
- purine nucleotide biosynthetic process
- purine nucleotide metabolic process
- purine ribonucleotide biosynthetic process
|
| Component |
| — |
|
| Enzyme 1 General Function |
Involved in catalytic activity |
| Enzyme 1 Specific Function |
N(6)-(1,2-dicarboxyethyl)AMP = fumarate + AMP |
| Enzyme 1 Pathways |
|
| Enzyme 1 Reactions |
- (1) N6-(1,2-dicarboxyethyl)AMP = fumarate + AMP [RN:R01083]
- (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 [RN:R04559]
|
| 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 |
2 |
| Enzyme 1 Locus |
22q13.1|22q13.2 |
| Enzyme 1 SNPs |
SNPJam Report  |
| Enzyme 1 General References |
- Fon EA, Demczuk S, Delattre O, Thomas G, Rouleau GA: Mapping of the human adenylosuccinate lyase (ADSL) gene to chromosome 22q13.1-->q13.2. Cytogenet Cell Genet. 1993;64(3-4):201-3. [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
]
- Collins JE, Wright CL, Edwards CA, Davis MP, Grinham JA, Cole CG, Goward ME, Aguado B, Mallya M, Mokrab Y, Huckle EJ, Beare DM, Dunham I: A genome annotation-driven approach to cloning the human ORFeome. Genome Biol. 2004;5(10):R84. Epub 2004 Sep 30. [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
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [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
]
- Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed
]
- Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed
]
- Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed
]
- Maaswinkel-Mooij PD, Laan LA, Onkenhout W, Brouwer OF, Jaeken J, Poorthuis BJ: Adenylosuccinase deficiency presenting with epilepsy in early infancy. J Inherit Metab Dis. 1997 Aug;20(4):606-7. [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
]
- Edery P, Chabrier S, Ceballos-Picot I, Marie S, Vincent MF, Tardieu M: Intrafamilial variability in the phenotypic expression of adenylosuccinate lyase deficiency: a report on three patients. Am J Med Genet A. 2003 Jul 15;120A(2):185-90. [PubMed
]
|
| Enzyme 1 Metabolite References |
Not Available |
|
Enzyme 2
[top]
|
| Enzyme 2 ID |
6176 |
| Enzyme 2 Name |
Multifunctional protein ADE2 |
| Enzyme 2 Synonyms |
- Phosphoribosylaminoimidazole-succinocarboxamide synthase
- SAICAR synthetase
- Phosphoribosylaminoimidazole carboxylase
- AIR carboxylase
- AIRC
|
| Enzyme 2 Gene Name |
PAICS |
| Enzyme 2 Protein Sequence |
>Multifunctional protein ADE2
MATAEVLNIGKKLYEGKTKEVYELLDSPGKVLLQSKDQITAGNAARKNHLEGKAAISNKI
TSCIFQLLQEAGIKTAFTRKCGETAFIAPQCEMIPIEWVCRRIATGSFLKRNPGVKEGYK
FYPPKVELFFKDDANNDPQWSEEQLIAAKFCFAGLLIGQTEVDIMSHATQAIFEILEKSW
LPQNCTLVDMKIEFGVDVTTKEIVLADVIDNDSWRLWPSGDRSQQKDKQSYRDLKEVTPE
GLQMVKKNFEWVAERVELLLKSESQCRVVVLMGSTSDLGHCEKIKKACGNFGIPCELRVT
SAHKGPDETLRIKAEYEGDGIPTVFVAVAGRSNGLGPVMSGNTAYPVISCPPLTPDWGVQ
DVWSSLRLPSGLGCSTVLSPEGSAQFAAQIFGLSNHLVWSKLRASILNTWISLKQADKKI
RECNL
|
| Enzyme 2 Number of Residues |
425 |
| Enzyme 2 Molecular Weight |
47078.8 |
| Enzyme 2 Theoretical pI |
7.26 |
| Enzyme 2 GO Classification |
| Function |
- ATP binding
- acid-amino acid ligase activity
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- carbon-carbon lyase activity
- carboxy-lyase activity
- catalytic activity
- ligase activity
- ligase activity, forming carbon-nitrogen bonds
- lyase activity
- nucleoside binding
- phosphoribosylaminoimidazole carboxylase activity
- phosphoribosylaminoimidazolesuccinocarboxamide synthase activity
- purine nucleoside binding
|
| Process |
- 'de novo' IMP biosynthetic process
- IMP biosynthetic process
- cellular nitrogen compound metabolic process
- metabolic process
- nitrogen compound metabolic process
- nucleobase, nucleoside and nucleotide metabolic process
- nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
- nucleoside phosphate metabolic process
- nucleotide metabolic process
- purine nucleoside monophosphate biosynthetic process
- purine nucleotide biosynthetic process
- purine nucleotide metabolic process
- purine ribonucleoside monophosphate biosynthetic process
|
| Component |
| — |
|
| Enzyme 2 General Function |
Involved in phosphoribosylaminoimidazole carboxylase activity |
| 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 [RN:R04591]
|
| 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
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| 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
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Beausoleil SA, Villen J, Gerber SA, Rush J, Gygi SP: A probability-based approach for high-throughput protein phosphorylation analysis and site localization. Nat Biotechnol. 2006 Oct;24(10):1285-92. Epub 2006 Sep 10. [PubMed
]
- Yu LR, Zhu Z, Chan KC, Issaq HJ, Dimitrov DS, Veenstra TD: Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra. J Proteome Res. 2007 Nov;6(11):4150-62. Epub 2007 Oct 9. [PubMed
]
- Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed
]
- Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed
]
- Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed
]
- Oppermann FS, Gnad F, Olsen JV, Hornberger R, Greff Z, Keri G, Mann M, Daub H: Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics. 2009 Jul;8(7):1751-64. Epub 2009 Apr 15. [PubMed
]
- Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed
]
- Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed
]
- Li SX, Tong YP, Xie XC, Wang QH, Zhou HN, Han Y, Zhang ZY, Gao W, Li SG, Zhang XC, Bi RC: Octameric structure of the human bifunctional enzyme PAICS in purine biosynthesis. J Mol Biol. 2007 Mar 9;366(5):1603-14. Epub 2006 Dec 16. [PubMed
]
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| Enzyme 2 Metabolite References |
Not Available |