Article
Mechanistic insights into p-hydroxybenzoate hydroxylase from studies of the mutant Ser212Ala.
Biochemistry - 11 May 1999
Moran G R, Entsch B, Palfey B A, Ballou D P
Abstract excerpt
In the crystal structure of native p-hydroxybenzoate hydroxylase, Ser212 is within hydrogen bonding distance (2.7 A) of one of the carboxylic oxygens of p-hydroxybenzoate. In this study, we have mutated residue 212 to alanine to study the importance of the serine hydrogen bond to enzyme function. Comparisons between mutant and wild type (WT) enzymes with the natural substrate p-hydroxybenzoate showed that this...
Topics
- 4-Hydroxybenzoate-3-Monooxygenase
- Alanine
- Catalysis
- Mutation
- Oxidation-Reduction
- Pseudomonas fluorescens
- Serine