Characterization of pyruvate kinase enzyme from streptomyces sporocinereus

ABSTRACT

Pyruvate kinase of Streptorrlyccs sparocinereus had a maximum activity at 40 and pH 8.0. Km value was 1.0 uM. It was activated by the addition of Mg SO4, KC1, Mg SO4, Ni 504, CoSO4, Hg C12 to the reaction mixture and inhibited by citrate, succinate, L-alanine and glutamate. Complete desiattuation occurred within few minutes with the exposure to acidic pH, while the enzyme was inactivated at pH7.0 and pH9.0 after 45 and 30 min respectively. Exposure of the enzyme to 50§ caused complete inactivation within few minutes, and it was rapidly inactivated when incubated at 40§. Some nucleocides revealed an increase in the activity of the enzyme such as AMP, GMP and CMP while others like ATP caused inhibition to the enzyme activity