InChI=1S/C8H14N3O7P/c9- 5- 1- 10- 3- 11(5) 8- 7(13) 6(12) 4(18- 8) 2- 17- 19(14,15) 16/h1,3- 4,6- 8,12- 13H,2,9H2,(H2,14,15,16) /p- 1/t4- ,6- ,7- ,8- /m1/s1 |
PDACUKOKVHBVHJ-XVFCMESISA-M |
O1[C@@H]([C@H]([C@H]([C@@H]1N2C(=C[NH+]=C2)N)O)O)COP(=O)([O-])[O-] |
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Outgoing
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5-amino-1-(5-phosphonato-β-D-ribosyl)imidazol-3-ium
(CHEBI:137981)
is a
organophosphate oxoanion
(CHEBI:58945)
5-amino-1-(5-phosphonato-β-D-ribosyl)imidazol-3-ium
(CHEBI:137981)
is conjugate base of
5-amino-1-(5-phospho-β-D-ribosyl)imidazole
(CHEBI:138560)
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Incoming
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5-amino-1-(5-phospho-β-D-ribosyl)imidazole
(CHEBI:138560)
is conjugate acid of
5-amino-1-(5-phosphonato-β-D-ribosyl)imidazol-3-ium
(CHEBI:137981)
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5-amino-1-(5-O-phosphonato-β-D-ribofuranosyl)-1H-imidazol-3-ium
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5-amino-1-(5-phospho-β-D-ribosyl)imidazole
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UniProt
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Ostanin KV, Alenin VV, Domkin VD, Smirnov MN (1989) [Isolation and properties of phosphoribosyl-aminoimidazole-succinocarboxyamide-synthestase from Saccharomyces cerevisiae yeasts]. Biokhimiia (Moscow, Russia) 54, 1265-1273 (Source: SUBMITTER) [PubMed:2684279] [show Abstract] An isolation procedure for phosphoribosyl succinocarboxamideaminoimidazole synthetase (SAICAR synthetase) (EC 6.3.2.6) has been developed. Pure SAICAR synthetase was found to be a monomeric protein with the apparent molecular weight of 36 kDa. The Michaelis constant for the three substrates of the reaction are 1.6 microM for CAIR, 14 microM for ATP and 960 microM for aspartic acid. The structural analogs of CAIR, 5-aminoimidazole ribotide and 5-aminoimidazole-4-carboxamide ribotide, act as competitive inhibitors of SAICAR synthetase. GTP and 2'-dATP can substitute for ATP in the reaction, while CTP and UTP inhibit the enzyme. No structural analogs of the aspartic acid were found to have affinity for SAICAR synthetase. The optimal reaction conditions for the enzyme were established to be at pH 8.0 and magnesium chloride concentration around 5 mM. | Schrimsher JL, Schendel FJ, Stubbe J, Smith JM (1986) Purification and characterization of aminoimidazole ribonucleotide synthetase from Escherichia coli. Biochemistry 25, 4366-4371 (Source: SUBMITTER) [PubMed:3530323] [show Abstract] Aminoimidazole ribonucleotide (AIR) synthetase has been purified 15-fold to apparent homogeneity from Escherichia coli which contains a multicopy plasmid containing the purM, AIR synthetase, gene. The protein is a dimer composed of two identical subunits of Mr 38,500. The N-terminal sequence, amino acid composition, and steady-state kinetics of the protein have been determined. AIR synthetase has been shown to catalyze the transfer of the formyl oxygen of [18O]formylglycinamide ribonucleotide to Pi. |
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