Structural biology of the purine biosynthetic pathway

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 st...

Full description

Saved in:
Bibliographic Details
Published in:Cellular and molecular life sciences : CMLS 2008-11, Vol.65 (23), p.3699-3724
Main Authors: Zhang, Y, Morar, M, Ealick, S. E
Format: Article
Language:English
Subjects:
amidotransferases
ATP
ATP-grasp superfamily
Binding Sites - genetics
Biochemistry
Biomedical and Life Sciences
Biomedicine
Biosynthesis
Cell Biology
Enzymes
Enzymes - chemistry
Enzymes - genetics
Evolution, Molecular
Gene Components
Inosine Monophosphate - biosynthesis
Life Sciences
Models, Molecular
Molecular biology
Molecular Structure
protein evolution
Proteins
Purine biosynthesis
Purines - biosynthesis
PurM superfamily
Review
Ribonucleotides - biosynthesis
Citations: Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary: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.
ISSN:1420-682X
1420-9071
DOI:10.1007/s00018-008-8295-8