Ontology highlight
ABSTRACT:
SUBMITTER: Kogan A
PROVIDER: S-EPMC2770544 | biostudies-literature | 2009 Oct
REPOSITORIES: biostudies-literature
BMC structural biology 20091008
<h4>Background</h4>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 degrees C for 20 h results in breaking this enamine bond and PLP release, as well as a reversible loss of activity and dissoc ...[more]