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CarBamate Kinase of Lactobacillus Buchneri Ncdo110. II. KInetic Studies and Reaction Mechanism
Author(s) -
Manca Nadra MC,
Pesce Ruiz Holgado AA,
Oliver G.
Publication year - 1987
Publication title -
biotechnology and applied biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.468
H-Index - 70
eISSN - 1470-8744
pISSN - 0885-4513
DOI - 10.1111/j.1470-8744.1987.tb00469.x
Subject(s) - lactobacillus buchneri , carbamate , enzyme , chemistry , substrate (aquarium) , biochemistry , product inhibition , nucleoside , pyruvate kinase , stereochemistry , hydrolysis , biology , non competitive inhibition , lactic acid , bacteria , lactobacillus plantarum , ecology , genetics , glycolysis
The participation of Mg2+ or Mn2+ nucleoside diphosphates in the reverse reaction catalyzed by purified carbamate kinase (ATP:carbamate phosphotransferase, EC 2.7.2.2) of Lactobacillus buchneri NCDO110 was studied. The results of initial velocity studies have indicated that Mn2+ ADP is as effective as a substrate as Mg2+ ADP is. Product inhibition studies have revealed that the enzyme has two distinct sites, one for nucleoside diphosphate and the other for carbamyl phosphate. The reaction of the enzyme with the substrates is of the random type.