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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...

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PMID: 10320359
DOI: 10.1021/bi990021+

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