Abstract
Streptococcus faecalis sp. produces pyruvate and ammonia from L-serine via a specifie L-serine dehydratase. The apparent Michaelis. constant for L-serine is 50 mM and the Vmax is 142 nmol of pyruvate formed per minute and per mg of protein. Maximum enzymatic activity is observed at 40 C and pH 8 in 100 mM phosphate buffer. L-serine is the sole substrate. D-serine, L-threonine and glycine are competitive inhibitors, L-cysteine acts as a non-competitive inhibitor.
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