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B6db references: 95236204

type Journal Article
authors Cohen-Addad, C.; Pares, S.; Sieker, L.; Neuburger, M.; Douce, R.
title The lipoamide arm in the glycine decarboxylase complex is not freely swinging
journal Nat Struct Biol
ui 95236204
year (1995)
volume 2
number 1
pages 63-8.
keywords Amino Acid Oxidoreductases/*chemistry
abstract Glycine decarboxylase consists of four protein components. Its structural and mechanistic heart is provided by the lipoic acid- containing H-protein which undergoes a cycle of reductive methylamination, methylamine transfer and electron transfer. Lipoic acid attached to a specific lysine side chain is assumed to act as a 'swinging arm' conveying the reactive dithiolane ring from one catalytic centre to another. The X-ray crystal structures of two forms of the H-protein have been determined. The lipoate cofactor is located in the loop of a hairpin configuration but following methylamine transfer it is pivoted to bind into a cleft at the surface of the H- protein. The lipoamide-methylamine arm is, therefore, not free to move in aqueous solvent.
last changed 2002/11/04 17:41

B6db references