Structure and reaction mechanism of L-arginine:glycine amidinotransferase.

Abstract:

:L-Arginine:glycine amidinotransferase (AT) catalyzes the committed step in creatine biosynthesis by formation of guanidinoacetic acid, the direct precursor of creatine. The X-ray structure of the human enzyme shows a novel fold with fivefold pseudosymmetry of beta beta alphabeta-modules. These modules enclose the active site compartment of the basket-like structure. The active site of AT lies at the bottom of a very narrow channel and contains a catalytic triad with the residues Cys-His-Asp. The transamidination reaction follows a ping-pong mechanism and is accompanied by large conformational changes. During catalysis the amidino group is covalently attached to the active site cysteine to give an amidino-cysteine intermediate.

journal_name

Biol Chem

journal_title

Biological chemistry

authors

Humm A,Fritsche E,Steinbacher S

subject

Has Abstract

pub_date

1997-03-01 00:00:00

pages

193-7

issue

3-4

eissn

1431-6730

issn

1437-4315

journal_volume

378

pub_type

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