| Literature DB >> 16349054 |
T C Cheng1, S P Harvey, A N Stroup.
Abstract
A highly active organophosphorus acid anhydrolase from Alteromonas undina was purified to homogeneity and found to be composed of a single polypeptide chain with a molecular weight of 53,000. With diisopropylfluorophosphate as a substrate, the purified enzyme has a specific activity of approximately 575 mumol/min/mg of protein. The enzyme has optimum activity at pH 8.0 and 55 degrees C and is stimulated by sulfhydryl reducing agents and manganese. It is capable of rapidly hydrolyzing a wide range of nerve agents and several chromogenic phosphinates.Entities:
Year: 1993 PMID: 16349054 PMCID: PMC182420 DOI: 10.1128/aem.59.9.3138-3140.1993
Source DB: PubMed Journal: Appl Environ Microbiol ISSN: 0099-2240 Impact factor: 4.792