Affiliation:
1. Research Department, CIBA Pharmaceutical Company, Summit, New Jersey
Abstract
Zeleznick
, L. D. (CIBA Pharmaceutical Co., Summit, N.J.), H.
Hankin, J. J. Boltralik, H. Heymann, and S. S. Barkulis
. Purification and properties of
N
-acetyl-
d
-glucosamine kinase from
Streptococcus pyogenes
. J. Bacteriol.
88:
1288–1295. 1964.—A kinase from
Streptococcus pyogenes
which catalyzes adenosine triphosphate-dependent phosphorylation of
d
-glucose and
N
-acetyl-
d
-glucosamine has been purified 1,500-fold. The ratio of the enzymatic activity on both substrates remained constant throughout the fractionation. Similarity in heat stability,
p
-hydroxymercuribenzoate inhibition, protection by either carbohydrate, and lack of repression of enzymatic activity when the bacteria were grown exclusively on one of the two substrates supports the hypothesis that kinase activity is associated with one enzyme.
Publisher
American Society for Microbiology
Subject
Molecular Biology,Microbiology
Reference29 articles.
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5. The phosphorylation of D(+)-glucosamine by crystalline yeast hexokinase;BROWN D. H.;Biochim. Biophys. Acta,1951
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