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lüll Structural biology of the purine biosynthetic pathway Zhang Y; Morar M; Ealick SECell Mol Life Sci 2008[Nov]; 65 (23): 3699-724Purine biosynthesis requires ten enzymatic transformations to generate inosine monophosphate. PurF, PurD, PurL, PurM, PurC, and PurB are common to all pathways, while PurN or PurT, PurK/PurE-I or PurE-II, PurH or PurP, and PurJ or PurO catalyze the same steps in different organisms. X-ray crystal structures are available for all 15 purine biosynthetic enzymes, including 7 ATP-dependent enzymes, 2 amidotransferases and 2 tetrahydrofolate-dependent enzymes. Here we summarize the structures of the purine biosynthetic enzymes, discuss similarities and differences, and present arguments for pathway evolution. Four of the ATP-dependent enzymes belong to the ATP-grasp superfamily and 2 to the PurM superfamily. The amidotransferases are unrelated, with one utilizing an N-terminal nucleophileglutaminase and the other utilizing a triad glutaminase. Likewise the tetrahydrofolate-dependent enzymes are unrelated. Ancestral proteins may have included a broad specificity enzyme instead of PurD, PurT, PurK, PurC, and PurP, and a separate enzyme instead of PurM and PurL.|*Evolution, Molecular[MESH]|*Models, Molecular[MESH]|Binding Sites/genetics[MESH]|Enzymes/*chemistry/genetics[MESH]|Gene Components[MESH]|Inosine Monophosphate/biosynthesis[MESH]|Molecular Structure[MESH]|Purines/*biosynthesis[MESH]|Ribonucleotides/biosynthesis[MESH] |