Structural insights into the prereaction state of pyruvate decarboxylase from Zymomonas mobilis .

Abstract:

:Pyruvate decarboxylase (PDC) uses thiamine diphosphate as an essential cofactor to catalyze the formation of acetaldehyde on the pathway of ethanol synthesis. Here we report the crystallographic image of a prereaction intermediate of a bacterial pyruvate decarboxylase prepared by cocrystallizing the enzyme with pyruvate and a stable analogue of the cofactor's activated ylid form. A second crystal structure of PDC in complex with fluoride shows that the ion organizes a water molecule that occludes the pyruvate binding site, accounting for the inhibitory effect of the halide. Also reported is a structure of the cofactor-free apo form, which when compared to the structure of the holo form indicates how thiamine diphosphate organizes the active site pocket of pyruvate decarboxylase to support catalysis. Guided by the structural and enzymatic data, we propose roles for several key residues in the catalytic mechanism.

journal_name

Biochemistry

journal_title

Biochemistry

authors

Pei XY,Erixon KM,Luisi BF,Leeper FJ

doi

10.1021/bi901864j

subject

Has Abstract

pub_date

2010-03-02 00:00:00

pages

1727-36

issue

8

eissn

0006-2960

issn

1520-4995

journal_volume

49

pub_type

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