Affiliation:
1. Institute of Microbiology, University Medical School, Szeged, Hungary
Abstract
The native
l
-serine deaminase (
l
-serine hydrolyase, deaminating, EC 4.2.1.13) of
Escherichia coli
K-12, which seems to be a very labile protein, is rather stable in concentrated solution. Dilution rapidly inactivates it, but in the presence of a saturating concentration of
l
-serine the molecule is protected from inactivation. It is a very specific enzyme;
l
-serine is the sole substrate with a
K
m
value of 6.60 × 10
−3
m. d
-Serine and
l
-cysteine are competitive inhibitors. Substrate saturation curves of the native enzyme show sigmoid shape, whereas the enzyme liberated from the bacteria in the presence of
l
-serine exhibits normal Michaelis-Menten kinetics.
Publisher
American Society for Microbiology
Subject
Molecular Biology,Microbiology
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