2uy8

From Proteopedia

Revision as of 15:35, 30 October 2007

R92A MUTANT OF BACILLUS SUBTILIS OXALATE DECARBOXYLASE OXDC

Overview

Oxalate decarboxylase (EC 4.1.1.2) catalyses the conversion of oxalate to, carbon dioxide and formate. It requires manganese and, uniquely, dioxygen, for catalysis. It forms a homohexamer and each subunit contains two, similar, but distinct, manganese sites termed sites 1 and 2. There is, kinetic evidence that only site 1 is catalytically active and that site 2, is purely structural. However, the kinetics of enzymes with mutations in, site 2 are often ambiguous and all mutant kinetics have been interpreted, without structural information. Nine new site-directed mutants have been, generated and four mutant crystal structures have now been solved. Most, mutants targeted either the flexibility (T165P), favoured conformation, (S161A, S164A, D297A or H299A) or presence (Delta162-3 or ... [(full description)]

About this Structure

2UY8 is a [Single protein] structure of sequence from [Bacillus subtilis] with MN and TRS as [ligands]. Active as [Oxalate decarboxylase], with EC number [4.1.1.2]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].

Reference

The identity of the active site of oxalate decarboxylase and the importance of the stability of active site lid conformations., Just VJ, Burrell MR, Bowater L, McRobbie I, Stevenson CE, Lawson DM, Bornemann S, Biochem J. 2007 Aug 6;. PMID:17680775

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