Molecular orbital studies of reaction mechanism and transition state structures for GABA-transaminase

Peter R. Andrews; Magdy Iskander; Graham Jones; David A. Winkler

doi:10.1016/0223-5234(88)90184-5

Molecular orbital studies of reaction mechanism and transition state structures for GABA-transaminase

Peter R. Andrews, Magdy Iskander, Graham Jones, David A. Winkler

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7 Citations (Scopus)

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	https://doi.org/10.1016/0223-5234(88)90184-5
Publication status	Published - 1988
Externally published	Yes

Keywords

enzyme inhibitors
GABA-transaminase
molecular orbital study
pyridoxal phosphate
reaction mechanism
transition state

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10.1016/0223-5234(88)90184-5

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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. ",

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doi = "10.1016/0223-5234(88)90184-5",

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journal = "European Journal of Medicinal Chemistry",

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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

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U2 - 10.1016/0223-5234(88)90184-5

DO - 10.1016/0223-5234(88)90184-5

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VL - 23

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EP - 132

JO - European Journal of Medicinal Chemistry

JF - European Journal of Medicinal Chemistry

SN - 0223-5234

IS - 2

ER -

Molecular orbital studies of reaction mechanism and transition state structures for GABA-transaminase

Abstract

Keywords

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