M. I. Kotlov

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The steady-state kinetic parameters of pyridoxal 5'-phosphate-dependent recombinant methionine γ -lyase from three pathogenic bacteria, Clostridium tetani, Clostridium sporogenes, and Porphyromonas gingivalis, were determined in β- and γ-elimination reactions. The enzyme from C. sporogenes is characterized by the highest catalytic efficiency in the(More)
187 Pyridoxal 5''phosphateedependent methionine γ lyase (EC 4.4.1.11) catalyzes the reaction of γelimii nation of methionine and its derivatives (scheme 1), the reaction of βelimination of cysteine and its anaa logues, as well as the reactions of γ and βsubstitution of sulfurrcontaining amino acids [1, 2].
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