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J Bacteriol. 1968 November; 96(5): 1512-1518
Copyright © 1968 American Society for Microbiology. All Rights Reserved.

L-Serine Deaminase of Escherichia coli

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 x 10^–3M. 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.

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• Adler, J. (1969). Chemoreceptors in Bacteria. Science 166: 1588-1597