|
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 |
Activity |
1.4.4.2 |
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 |
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