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Conformational changes in orotidine 5'-monophosphate decarboxylase: "remote" residues that stabilize the active conformation.

Abstract：

:The structural factors responsible for the extraordinary rate enhancement ( approximately 10(17)) of the reaction catalyzed by orotidine 5'-monophosphate decarboxylase (OMPDC) have not been defined. Catalysis requires a conformational change that closes an active site loop and "clamps" the orotate base proximal to hydrogen-bonded networks that destabilize the substrate and stabilize the intermediate. In the OMPDC from Methanobacter thermoautotrophicus, a "remote" structurally conserved cluster of hydrophobic residues that includes Val 182 in the active site loop is assembled in the closed, catalytically active conformation. Substitution of these residues with Ala decreases k(cat)/K(m) with a minimal effect on k(cat), providing evidence that the cluster stabilizes the closed conformation. The intrinsic binding energies of the 5'-phosphate group of orotidine 5'-monophosphate for the mutant enzymes are similar to that for the wild type, supporting this conclusion.

journal_name

Biochemistry

journal_title

Biochemistry

authors

Wood BM,Amyes TL,Fedorov AA,Fedorov EV,Shabila A,Almo SC,Richard JP,Gerlt JA

doi

10.1021/bi100443a

subject

Has Abstract

pub_date

2010-05-04 00:00:00

pages

3514-6

issue

17

eissn

0006-2960

issn

1520-4995

journal_volume

49

pub_type

杂志文章

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