Structure-function relations in oxaloacetate decarboxylase complex. Fluorescence and infrared approaches to monitor oxomalonate and Na(+) binding effect.

ABSTRACT:

Background

Oxaloacetate decarboxylase (OAD) is a member of the Na(+) transport decarboxylase enzyme family found exclusively in anaerobic bacteria. OAD of Vibrio cholerae catalyses a key step in citrate fermentation, converting the chemical energy of the decarboxylation reaction into an electrochemical gradient of Na(+) ions across the membrane, which drives endergonic membrane reactions such as ATP synthesis, transport and motility. OAD is a membrane-bound enzyme composed of alpha, beta and gamma subunits. The alpha subunit contains the carboxyltransferase catalytic site.

Methodology/principal findings

In this report, spectroscopic techniques were used to probe oxomalonate (a competitive inhibitor of OAD with respect to oxaloacetate) and Na(+) effects on the enzyme tryptoph

SUBMITTER: Granjon T 

PROVIDER: S-EPMC2881705 | biostudies-literature | 2010 Jun

REPOSITORIES: biostudies-literature