1887

Abstract

B4 has a transport system for glucose and mannose, but β-glucanase expression is only catabolite-repressed by glucose. . B4 cell extracts had ATP-dependent gluco- and mannokinase activities, and significant phosphoenolpyruvate- or GTP-dependent hexose phosphorylation was not observed. Mannose inhibited glucose phosphorylation (and vice versa), and activity gels indicated that a single protein was responsible for both activities. Glucose was phosphorylated at a faster rate than was mannose [ 280 nmol hexose (mg protein) min versus 60 nmol hexose (mg protein) min, respectively] and glucose was a better substrate for the kinase ( 012 mM versus 12 mM, respectively). The purified glucomannokinase (1250-fold) had a molecular mass of 68 kDa, but SDS-PAGE gels indicated that it was a dimer (monomer 345 kDa). The N-terminus (25 residues) had an 8 amino acid segment that was homologous to other bacterial glucokinases. The glucomannokinase was competitively inhibited by the nonmetabolizable glucose analogue 2-deoxyglucose (2DG), and cells grown with glucose and 2DG had lower rates of glucose consumption than did cells given only glucose. When the ratio of 2DG to glucose was increased, the glucose consumption rate decreased and the β-glucanase activity increased. The glucose consumption rate and the glucomannokinase activity of cells treated with 2DG were highly correlated ( =098). This result suggested that glucomannokinase activity was either directly or indirectly regulating β-glucanase expression.

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2001-04-01
2020-12-02
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