PMID:10079286
| Citation |
Kanai, S and Toh, H (1999) Identification of new members of the GS ADP-forming family from the de novo purine biosynthesis pathway. J. Mol. Evol. 48:482-92 |
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| Abstract |
Most living organisms can synthesize isosinate from 5-phosphoribosyl 1-pyrophosphate in the de novo purine biosynthesis pathway, which is basically composed of 10 reaction steps. Phosphoribosylglycinamide synthetase (GARS) catalyzes the second step of the pathway. We found that the enzyme shows weak, but significant, sequence similarity to phosphoribosylglycinamide formyltransferase 2 (GART2) and the ATPase domain of phosphoribosylaminoimidazole carboxylase (AIRCA), which catalyze the third and sixth steps of the pathway, respectively. In addition, the three enzymes were similar in amino acid sequence to biotin carboxylase (BC) and carbamoylphosphate synthetase (CPS), which are the members of the GS ADP-forming family. This family has been identified through a tertiary structure comparison and includes glutathione synthetase, d-alanine:d-alanine ligase, BC, succinyl-CoA synthetase beta-chain, and phosphoribosylaminoimidazole-succinocarboxamide synthase. Molecular phylogenetic analysis based on a multiple alignment of GARS, GART2, AIRCA, BC, and CPS suggests that GART2 is more closely related to AIRCA than to GARS among the three enzymes from the pathway, though the three enzymes are relatively close to each other within the GS ADP-forming family. Moreover, the analysis showed that archaeal GARS had diverged before the speciation between bacteria and eucarya. |
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| Keywords |
Amino Acid Sequence; Archaea/genetics; Carbon-Nitrogen Ligases/chemistry; Carbon-Nitrogen Ligases/genetics; Carbon-Nitrogen Ligases/metabolism; Evolution, Molecular; Humans; Molecular Sequence Data; Phylogeny; Purines/biosynthesis; Sequence Homology, Amino Acid |
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