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

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 Lys...

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Bibliographic Details
Main Authors: Kogan, Anna, Gdalevsky, Garik Y, Cohen-Luria, Rivka, Goldgur, Yehuda, Phillips, Robert S, Parola, Abraham H, Almog, Orna
Format: Artigo
Language:Inglês
Published: BioMed Central 2009
Subjects:
Research Article
Online Access:https://ncbi.nlm.nih.gov/pmc/articles/PMC2770544/
https://ncbi.nlm.nih.gov/pubmed/19814824
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1186/1472-6807-9-65
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