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 Chemjournal_title
Biological chemistryauthors
Humm A,Fritsche E,Steinbacher Ssubject
Has Abstractpub_date
1997-03-01 00:00:00pages
193-7issue
3-4eissn
1431-6730issn
1437-4315journal_volume
378pub_type
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