Molecular properties of yeast glucokinase

Maitra, Pabitra K. ; Lobo, Zita (1977) Molecular properties of yeast glucokinase Molecular and Cellular Biochemistry, 18 (1). pp. 21-27. ISSN 0300-8177

Full text not available from this repository.

Official URL:

Related URL:


Glucokinase from baker's yeast has been purified to homogeneity. The molecular weight of the subunit is 51,000. The native enzyme sediments with s20,w values in the range of 19 to nearly 4 S. The presence of glucose and phosphate favors the heavier species while ATP causes depolymerization. Titration experiments with the Ellman reagent support this view. The enzyme subunit has four sulfhydryl residues of which one is more reactive than the other three. However, it does not seem to be directly responsible for the catalytic activity. The amino acid composition of the enzyme is similar to those of the hexokinases P1 and P2 but for aspartic acid and histidine.

Item Type:Article
Source:Copyright of this article belongs to Springer-Verlag.
ID Code:31414
Deposited On:25 Apr 2011 09:27
Last Modified:09 Jun 2011 09:12

Repository Staff Only: item control page