Conformational changes and loose packing promote E. coli Tryptophanase cold lability期刊界 All Journals 搜尽天下杂志传播学术成果专业期刊搜索期刊信息化学术搜索

Conformational changes and loose packing promote E. coli Tryptophanase cold lability

Authors:	Anna Kogan Garik Y Gdalevsky Rivka Cohen-Luria Yehuda Goldgur Robert S Phillips Abraham H Parola Orna Almog

Affiliation:	(1) Department of Chemistry, Ben-Gurion University of the Negev, POB 653, Beer-Sheva, 84105, Israel;(2) Departments of Chemistry and Biochemistry and Molecular Biology, University of Georgia, Athens, GA 30602, USA;(3) Department of Clinical Biochemistry, Faculty of Health Sciences, Ben-Gurion University, Beer-Sheva, 84105, Israel

Abstract:	Background Oligomeric enzymes can undergo a reversible loss of activity at low temperatures. One such enzyme is tryptophanase (Trpase) from Escherichia coli. Trpase is a pyridoxal phosphate (PLP)-dependent tetrameric enzyme with a Mw of 210 kD. PLP is covalently bound through an enamine bond to Lys270 at the active site. The incubation of holo E. coli Trpases at 2°C for 20 h results in breaking this enamine bond and PLP release, as well as a reversible loss of activity and dissociation into dimers. This sequence of events is termed cold lability and its understanding bears relevance to protein stability and shelf life.

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