Abstract
The reaction catalyzed by the enzyme GABA-transaminase has been studied by means of semi-empirical molecular orbital calculations. The results elucidate the role of the active site general base and the cofactor in reducing the barrier to a 1,3-prototropic shift, the rate-determining step in the transamination reaction. The mechanistic inferences drawn are consistent with previous studies of pyridoxal phosphate-dependent transaminases.
Original language | English |
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Pages (from-to) | 125-132 |
Number of pages | 8 |
Journal | European Journal of Medicinal Chemistry |
Volume | 23 |
Issue number | 2 |
DOIs | |
Publication status | Published - 1988 |
Externally published | Yes |
Keywords
- enzyme inhibitors
- GABA-transaminase
- molecular orbital study
- pyridoxal phosphate
- reaction mechanism
- transition state