1dxl

From Proteopedia

Revision as of 12:57, 30 October 2007

DIHYDROLIPOAMIDE DEHYDROGENASE OF GLYCINE DECARBOXYLASE FROM PISUM SATIVUM

Overview

The glycine decarboxylase complex consists of four different component, enzymes (P-, H-, T- and L-proteins). The 14-kDa lipoamide-containing, H-protein plays a pivotal role in the complete sequence of reactions as, its prosthetic group (lipoic acid) interacts successively with the three, other components of the complex and undergoes a cycle of reductive, methylamination, methylamine transfer and electron transfer. With the aim, to understand the interaction between the H-protein and its different, partners, we have previously determined the crystal structure of the, oxidized and methylaminated forms of the H-protein. In the present study, we have crystallized the H-protein in its reduced state and the L-protein, (lipoamide dehydrogenase or dihydrolipoamide dehydrogenase). The L-protein, ... [(full description)]

About this Structure

1DXL is a [Single protein] structure of sequence from [Pisum sativum] with FAD as [ligand]. Active as [Dihydrolipoyl dehydrogenase], with EC number [1.8.1.4]. Structure known Active Sites: FAA, FAB, FAC and FAD. Full crystallographic information is available from [OCA].

Reference

Interaction between the lipoamide-containing H-protein and the lipoamide dehydrogenase (L-protein) of the glycine decarboxylase multienzyme system 2. Crystal structures of H- and L-proteins., Faure M, Bourguignon J, Neuburger M, MacHerel D, Sieker L, Ober R, Kahn R, Cohen-Addad C, Douce R, Eur J Biochem. 2000 May;267(10):2890-8. PMID:10806386

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