Abstract
Structural and biochemical analyses reveal how ornithine acetyl-transferases catalyse the reversible transfer of an acetyl-group from a basic (ornithine) to an acidic (glutamate) amino acid by employing a common mechanism involving an acetyl-enzyme intermediate but using different side chain binding modes.
Original language | English |
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Pages (from-to) | 6219-6225 |
Number of pages | 7 |
Journal | Organic & biomolecular chemistry |
Volume | 9 |
Issue number | 18 |
Early online date | 28 Jul 2011 |
DOIs | |
Publication status | Published - 21 Sept 2011 |
Keywords
- SERINE-PROTEASE CATALYSIS
- ACYL-ENZYME COMPLEX
- CRYSTAL-STRUCTURE
- GENE-CLUSTER
- ACETYLTRANSFERASE
- INTERMEDIATE
- MECHANISM