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Phosphorylation of 3‐ O ‐methyl‐D‐glucose by yeast and beef hexokinase
Author(s) -
Malaisse-Lagae Francine,
Giroix Marie-Hélène,
Sener Abdullah,
Malaisse Willy J.
Publication year - 1986
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(86)80423-9
Subject(s) - hexokinase , phosphorylation , yeast , chemistry , biochemistry , glycolysis , enzyme
Beef heart hexokinase and yeast hexokinase both catalyzed the phosphorylation of 3‐ O ‐[ 14 C]methyl‐D‐glucose. The maximal velocity was 3 orders of magnitude lower and the K m , for the glucose analogue 40–120 times higher than those observed with D‐[U‐ 14 C]glucose. Hence, 3‐ O ‐methyl‐D‐glucose should not be considered as a truly nonmetabolized analogue of D‐glucose.