Abstract
The three enzymes glucokinase (EC 2.7.1.2), fructokinase (EC 2.7.1.4) and glucose-6-phosphate dehydrogenase (EC 1.1.1.49) were isolated in high yield from extracts of Zymomonas mobilis. The principal steps in the isolation procedures involved the use of selected dye-ligand adsorbent columns, with affinity elution of two of the three enzymes. Glucokinase and fructokinase are dimeric proteins (2 X 33000 Da and 2 X 28000 Da respectively) and glucose-6-phosphate dehydrogenase is a tetramer (4 X 52000 Da). Some similarities in the structural and kinetic parameters of the two kinases were noted, but they have absolute specificity for their substrates. Fructokinase is strongly inhibited by glucose; otherwise non-substrate sugars had little effect on any of the three enzymes.
MeSH Terms
Adsorption
Bacteria/enzymology
Carbohydrate Metabolism
Chromatography, Affinity
Electrophoresis, Polyacrylamide Gel
Fructokinases/isolation & purification,metabolism
Glucokinase/isolation & purification,metabolism
Glucosephosphate Dehydrogenase/isolation & purification,metabolism
Kinetics
Macromolecular Substances
Phosphotransferases/metabolism
Substrate Specificity
Chemicals
Macromolecular Substances
Glucosephosphate Dehydrogenase
Phosphotransferases
Fructokinases
Glucokinase
fructokinase
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Scopes R K
Testolin V
Stoter A
Griffiths-Smith K
Algar E M
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24 references, click to expand
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