Cold inactivation and dissociation into dimers of Escherichia coli tryptophanase and its W330F mutant form.

doi:10.1016/s0167-4838(98)00031-4

Back to search

Article

Cold inactivation and dissociation into dimers of Escherichia coli tryptophanase and its W330F mutant form.

Biochimica et biophysica acta - 19 May 1998

Erez T, Gdalevsky GYa, Torchinsky Y M, Phillips R S, Parola A H

Abstract excerpt

The kinetics and mechanism of reversible cold inactivation of the tetrameric enzyme tryptophanase have been studied. Cold inactivation is shown to occur slowly in the presence of K+ ions and much faster in their absence. The W330F mutant tryptophanase undergoes rapid cold inactivation even in the...

Topics

Bacterial Proteins
Chromatography, High Pressure Liquid
Cold Temperature
Dimerization
Enzyme Repression
Escherichia coli
Mutation
Potassium
Spectrum Analysis
Tryptophanase

Community interpretation

Discuss the evidence

Ask a question, add context or challenge an interpretation. Community activity is separate from scientific evidence strength.

discussions

replies

Citations encouraged

Claims remain attributable.

No discussion yet

Be the first to add a careful, cited interpretation.