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Class B nonspecific acid phosphatase from Salmonella typhimurium LT2: Phosphotransferase activity, stability and thiol group reactivity

Paper ID Volume ID Publish Year Pages File Format Full-Text
18625 42728 2006 6 PDF Available
Title
Class B nonspecific acid phosphatase from Salmonella typhimurium LT2: Phosphotransferase activity, stability and thiol group reactivity
Abstract

The class B acid phosphatase (AphA) from Salmonella typhimurium LT2 exhibits phosphotransferase activity in addition to its intrinsic phosphohydrolase activity. It was shown that the enzyme transfers phosphate groups from an organic phosphoric acid ester (donor) to the hydroxyl groups of various alcohols (acceptors). With aliphatic, primary alcohols phosphotransferase activity increased at the expense of phosphohydrolase activity with increasing number of carbon atoms of the acceptor. Secondary, tertiary and branched alcohols and those containing additional hydrophilic, polar, or charged groups were less efficient as acceptors. The ratio of phosphotransferase to phosphohydrolase activity is independent of donor concentration whereas it rises with increasing acceptor concentration. Detergents or polyethylene glycol were indispensible for enzyme stability. Nonionic detergents are able to reactivate surface inactivated enzyme. A single cystein group present in the polypeptide chain of the native, homotetrameric enzyme is able to form disulfid bridges between subunits without affecting enzyme activity.

Keywords
PNPP, p-nitrophenyl phosphate; PNP, p-nitrophenylate ion; NOG, n-octyl glucoside; PEG, polyethylene glycolSalmonella thyphimurium; Class B nonspecific acid phosphatase; Phosphotransferase activity
First Page Preview
Class B nonspecific acid phosphatase from Salmonella typhimurium LT2: Phosphotransferase activity, stability and thiol group reactivity
Publisher
Database: Elsevier - ScienceDirect
Journal: Enzyme and Microbial Technology - Volume 38, Issue 5, 2 March 2006, Pages 683–688
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering