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 |
|---|---|
| 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 |
Keywords
- enzyme inhibitors
- GABA-transaminase
- molecular orbital study
- pyridoxal phosphate
- reaction mechanism
- transition state
Cite this
}
Molecular orbital studies of reaction mechanism and transition state structures for GABA-transaminase. / Andrews, Peter R.; Iskander, Magdy; Jones, Graham; Winkler, David A.
In: European Journal of Medicinal Chemistry, Vol. 23, No. 2, 1988, p. 125-132.Research output: Contribution to journal › Article › Other
TY - JOUR
T1 - Molecular orbital studies of reaction mechanism and transition state structures for GABA-transaminase
AU - Andrews, Peter R.
AU - Iskander, Magdy
AU - Jones, Graham
AU - Winkler, David A.
PY - 1988
Y1 - 1988
N2 - 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.
AB - 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.
KW - enzyme inhibitors
KW - GABA-transaminase
KW - molecular orbital study
KW - pyridoxal phosphate
KW - reaction mechanism
KW - transition state
UR - http://www.scopus.com/inward/record.url?scp=0023926097&partnerID=8YFLogxK
U2 - 10.1016/0223-5234(88)90184-5
DO - 10.1016/0223-5234(88)90184-5
M3 - Article
VL - 23
SP - 125
EP - 132
JO - European Journal of Medicinal Chemistry
JF - European Journal of Medicinal Chemistry
SN - 0223-5234
IS - 2
ER -