Article
Mutations affecting transition-state stabilization by residues coordinating zinc at the active site of cytidine deaminase.
Biochemistry - 31 May 1994
Smith A A, Carlow D C, Wolfenden R, Short S A
Abstract excerpt
Cytidine deaminase from Escherichia coli contains 1 mol of tightly bound zinc per enzyme subunit (Yang, C., Carlow, D., Wolfenden, R., & Short, S.A. (1992) Biochemistry 31, 4168-4174). When the metal liganding residues Cys-129 and Cys-132 were replaced by Ala, and His-102 was replaced by Ala, Asn, or Gln, deaminase activities of cell extracts containing these mutant enzymes were decreased by several orders of...
Topics
- Binding Sites
- Catalysis
- Cytidine Deaminase
- Electrophoresis, Polyacrylamide Gel
- Escherichia coli
- Mutation
- Zinc