Article
The roles of Tyr70 and Tyr225 in aspartate aminotransferase assessed by analysing the effects of mutations on the multiple reactions of the substrate analogue serine o-sulphate.
European journal of biochemistry - 15 Sept 1995
Birolo L, Sandmeier E, Christen P, John R A
Abstract excerpt
Aspartate aminotransferase catalyses multiple reactions of the glutamate analogue, serine O-sulphate. The predominant reaction is beta-elimination of sulphate to give aminoacrylate (kcat = 13 s-1 for the Escherichia coli enzyme) which may either hydrolyse to pyruvate and ammonia, or react covalently with the enzyme and inactivate it (kinact = 1.1 x 10(-3) s-1). Serine O-sulphate also undergoes a transamination...
Topics
- Amination
- Aspartate Aminotransferases
- Methionine
- Mutation
- Phenylalanine
- Serine
- Structure-Activity Relationship
- Tyrosine