L-serine deaminase of Escherichia coli.
作者信息
Alföldi L, Raskó I, Kerekes E
出版信息
J Bacteriol. 1968 Nov;96(5):1512-8. doi: 10.1128/jb.96.5.1512-1518.1968.
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(-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.
摘要
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