Ontology highlight
ABSTRACT:
SUBMITTER: Pop C
PROVIDER: S-EPMC3110659 | biostudies-literature | 2003 Oct
REPOSITORIES: biostudies-literature
Pop Cristina C Feeney Brett B Tripathy Ashutosh A Clark A Clay AC
Biochemistry 20031001 42
The interface of the procaspase-3 dimer plays a critical role in zymogen maturation. We show that replacement of valine 266, the residue at the center of the procaspase-3 dimer interface, with glutamate resulted in an increase in enzyme activity of approximately 60-fold, representing a pseudoactivation of the procaspase. In contrast, substitution of V266 with histidine abolished the activity of the procaspase-3 as well as that of the mature caspase. While the mutations do not affect the dimeric ...[more]