1uw8
From Proteopedia
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CRYSTAL STRUCTURE OF OXALATE DECARBOXYLASE
Overview
Oxalate decarboxylase (EC 4.1.1.2) catalyzes the conversion of oxalate to, formate and carbon dioxide and utilizes dioxygen as a cofactor. By, contrast, the evolutionarily related oxalate oxidase (EC 1.2.3.4) converts, oxalate and dioxygen to carbon dioxide and hydrogen peroxide. Divergent, free radical catalytic mechanisms have been proposed for these enzymes, that involve the requirement of an active site proton donor in the, decarboxylase but not the oxidase reaction. The oxidase possesses only one, domain and manganese binding site per subunit, while the decarboxylase has, two domains and two manganese sites per subunit. A structure of the, decarboxylase together with a limited mutagenesis study has recently been, interpreted as evidence that the C-terminal domain manganese binding ... [(full description)]
About this Structure
1UW8 is a [Single protein] structure of sequence from [Bacillus subtilis] with MN and TRS as [ligands]. Active as [[1]], with EC number [4.1.1.2]. Full crystallographic information is available from [OCA].
Reference
A closed conformation of Bacillus subtilis oxalate decarboxylase OxdC provides evidence for the true identity of the active site., Just VJ, Stevenson CE, Bowater L, Tanner A, Lawson DM, Bornemann S, J Biol Chem. 2004 May 7;279(19):19867-74. Epub 2004 Feb 10. PMID:14871895
Page seeded by OCA on Mon Oct 29 17:06:34 2007
Categories: Bacillus subtilis | Single protein | Bornemann, S. | Bowater, L. | Just, V.J. | Lawson, D.M. | Stevenson, C.E.M. | Tanner, A. | MN | TRS | Cupin | Decarboxylase | Formate | Lyase | Manganese | Metal binding protein | Oxalate
