Catalytic ability and stability of two recombinant mutants of D-amino acid transaminase involved in coenzyme binding

Author:

Van Ophem Peter W.,Pospischil Maria A.,Manning James M.,Ringe Dagmar,Peisach Daniel,Petsko Gregory,Soda Kenji

Publisher

Wiley

Subject

Molecular Biology,Biochemistry

Reference22 articles.

1. Kinetic and stereochemical comparison of wild-type and active site K145Q mutant enzyme of bacterial D-amino acid transaminase;Bhatia;J Biol Chem,1993

2. Role reversal for substrates and inhibitors;Bhatia;J Biol Chem,1993

3. A note on the molar absorptivity of reduced Ellman's reagent, 3-carboxylato-4-nitrothiophenolate;Collier;Anal Biochem,1973

4. DawsonMC, ElliottDC, ElliottWM, JonesKM, eds. 1986. In: Data for biochemical research. Chapter 6. Vitamins and coenzymes. Oxford: Clarendon Press. pp 122-123.

5. Substitution of glutamine for lysine at the pyridoxal phosphate binding site of bacterial D-amino acid transaminase;Futaki;J Biol Chem,1990

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