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Ligases;
Forming carbon-nitrogen bonds;
Acid-D-amino-acid ligases (peptide synthases)
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate:L-aspartate ligase (ADP-forming)
Forms part of the purine biosynthesis pathway.
EC 6.3.2.6 created 1961, modified 2000, modified 2006
Biosynthesis of secondary metabolites |
phosphoribosylaminoimidazole carboxylase / phosphoribosylaminoimidazole-succinocarboxamide synthase |
phosphoribosylaminoimidazole-succinocarboxamide synthase |
fusion protein PurCD |
LUKENS LN, BUCHANAN JM.
Biosynthesis of the purines. XXIV. The enzymatic synthesis of 5-amino-1-ribosyl-4-imidazolecarboxylic acid 5′-phosphate from 5-amino-1-ribosylimidazole 5′-phosphate and carbon dioxide.
J Biol Chem 234:1799-805 (1959)
Parker J.
Identification of the purC gene product of Escherichia coli.
Ebbole DJ, Zalkin H.
Cloning and characterization of a 12-gene cluster from Bacillus subtilis encoding nine enzymes for de novo purine nucleotide synthesis.
J Biol Chem 262:8274-87 (1987)
Chen ZD, Dixon JE, Zalkin H.
Cloning of a chicken liver cDNA encoding 5-aminoimidazole ribonucleotide carboxylase and 5-aminoimidazole-4-N-succinocarboxamide ribonucleotide synthetase by functional complementation of Escherichia coli pur mutants.
O’Donnell AF, Tiong S, Nash D, Clark DV
The Drosophila melanogaster ade5 gene encodes a bifunctional enzyme for two steps in the de novo purine synthesis pathway.
Genetics 154:1239-53 (2000)
Nelson SW, Binkowski DJ, Honzatko RB, Fromm HJ.
Mechanism of action of Escherichia coli phosphoribosylaminoimidazolesuccinocarboxamide synthetase.
6.3.2.6 |
6.3.2.6 |
6.3.2.6 |
6.3.2.6 |
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