| Autor: |
A, Humm, E, Fritsche, S, Steinbacher |
| Rok vydání: |
1997 |
| Předmět: |
|
| Zdroj: |
Biological chemistry. 378(3-4) |
| ISSN: |
1431-6730 |
| Popis: |
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. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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