Unknown

Dataset Information

0

Structural biology of the purine biosynthetic pathway.


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.

SUBMITTER: Zhang Y 

PROVIDER: S-EPMC2596281 | biostudies-literature | 2008 Nov

REPOSITORIES: biostudies-literature

altmetric image

Publications

Structural biology of the purine biosynthetic pathway.

Zhang Y Y   Morar M M   Ealick S E SE  

Cellular and molecular life sciences : CMLS 20081101 23


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  ...[more]

Similar Datasets

| S-EPMC6499638 | biostudies-literature
| S-EPMC3220471 | biostudies-literature
| PRJEB24738 | ENA
| S-EPMC3566086 | biostudies-literature
| S-EPMC4618177 | biostudies-literature
| S-EPMC3557020 | biostudies-literature
| S-EPMC6486802 | biostudies-literature
| S-EPMC5942248 | biostudies-literature
| S-EPMC7247824 | biostudies-literature
| S-EPMC3046457 | biostudies-literature