Logo image
 Home Academic units
Sign in
Back
Studies on an Active Site residue, E177, That Affects Binding of the Coenzyme in D-Amino Acid Transaminase, and Mechanistic Studies on a Suicide Substrate
Book chapter

Studies on an Active Site residue, E177, That Affects Binding of the Coenzyme in D-Amino Acid Transaminase, and Mechanistic Studies on a Suicide Substrate

Peter W van Ophem, Bryan W Lepore, Kazuhisa Kishimoto, Dagmar Ringe and James M Manning
Biochemistry and Molecular Biology of Vitamin B6 and PQQ-dependent Proteins, pp.339-346
Birkhäuser Basel
2000
DOI: https://doi.org/10.1007/978-3-0348-8397-9_56

Abstract

Crystallization Solution Pyridinium Nitrogen Pyruvate Production Mutant Enzyme 177S Mutant
While the E177S mutation in D-amino acid transaminase has a reduced ability to transaminate D-alanine, the efficiency of β-elimination of β-chloro-D-alanine remains almost intact. Interestingly, the latter reaction showed the appearance of an intermediate absorbing around 460 nm with this attenuated enzyme. The protein CD spectrum of the apo-enzyme of E177S resembled that of wild-type enzyme, but that of E 177K showed a negative elipticity around 280 nm.

Metrics

75 Record Views

Details