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- W1969430061 endingPage "3724" @default.
- W1969430061 startingPage "3699" @default.
- W1969430061 abstract "Purine 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." @default.
- W1969430061 created "2016-06-24" @default.
- W1969430061 creator A5010734647 @default.
- W1969430061 creator A5019164857 @default.
- W1969430061 creator A5022802322 @default.
- W1969430061 date "2008-08-19" @default.
- W1969430061 modified "2023-10-09" @default.
- W1969430061 title "Structural biology of the purine biosynthetic pathway" @default.
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- W1969430061 doi "https://doi.org/10.1007/s00018-008-8295-8" @default.
- W1969430061 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2596281" @default.
- W1969430061 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/18712276" @default.
- W1969430061 hasPublicationYear "2008" @default.
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