Ontology highlight
ABSTRACT:
SUBMITTER: Olucha J
PROVIDER: S-EPMC3156872 | biostudies-literature | 2011 Aug
REPOSITORIES: biostudies-literature
Olucha Jose J Ouellette Andrew N AN Luo Qianyi Q Lamb Audrey L AL
Biochemistry 20110722 33
An isochorismate-pyruvate lyase with adventitious chorismate mutase activity from Pseudomonas aerugionsa (PchB) achieves catalysis of both pericyclic reactions in part by the stabilization of reactive conformations and in part by electrostatic transition-state stabilization. When the active site loop Lys42 is mutated to histidine, the enzyme develops a pH dependence corresponding to a loss of catalytic power upon deprotonation of the histidine. Structural data indicate that the change is not due ...[more]