Kinetic and stereochemical comparison of wild-type and active-site K145Q mutant enzyme of bacterial D-amino acid transaminase.

Article

Kinetic and stereochemical comparison of wild-type and active-site K145Q mutant enzyme of bacterial D-amino acid transaminase.

The Journal of biological chemistry - 5 Apr 1993

Bhatia M B, Futaki S, Ueno H, Manning J M, Ringe D, Yoshimura T, Soda K

Abstract excerpt

D-Amino acid transaminase (EC 2.6.1.21), from Bacillus sp. YM-1, a thermostable enzyme with pyridoxal 5'-phosphate as coenzyme and a target for the design of novel antimicrobial agents, catalyzes the reversible transfer of an amino group between D-alanine and alpha-ketoglutarate to form pyruvate...

Topics

Bacillus
Binding Sites
D-Alanine Transaminase
Kinetics
Lysine
Magnetic Resonance Spectroscopy
Molecular Structure
Mutation
Solvents
Transaminases

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