Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:2.7.1.1 (hexokinase)
 5,274 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Polyphosphate glucokinase from Mycobacterium tuberculosis catalyzes the phosphorylation of glucose using polyphosphate or ATP as the phosphoryl donor. The M. tuberculosis H37Rv gene encoding this enzyme has been cloned, sequenced, and expressed in Escherichia coli. The gene contains an open reading frame for 265 amino acids with a calculated mass of 27,400 daltons. The recombinant polyphosphate glucokinase was purified 189-fold to homogeneity and shown to contain dual enzymatic activities, similar to the native enzyme from H37Ra strain. The high G+C content in the codon usage (64.5%) of the gene and the absence of an E. coli-like promoter consensus sequence are consistent with other mycobacterial genes. Two phosphate binding domains conserved in the eukaryotic hexokinase family were identified in the polyphosphate glucokinase sequence, however, "adenosine" and "glucose" binding motifs were not apparent. In addition, a putative polyphosphate binding region is also proposed for the polyphosphate glucokinase enzyme.
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PMID:Cloning, expression, and characterization of polyphosphate glucokinase from Mycobacterium tuberculosis. 861 63

An ATP: D-glucose and D-mannose 6-phosphotransferase activity was found in Mycobacterium tuberculosis HERa. The activity was separated from other ATP- and polyphosphate D-glucose phosphotransferases in a procedure involving precipitation with ammonium sulfate, treatment with calcium phosphate gel, DEAE-cellulose and DEAE-Sephadex A50 chromatography. The optimum pH of the phosphorylation reaction was from 9 to 10.5. The hexokinase phosphorylated D-glucose with a Km of 20 mM under conditions of MgATP saturation. The Km for MgATP was 0.2 mM. The enzyme showed a higher activity on D-mannose at a saturation level being about 100-fold lower than that of D-glucose; it did not utilize either D-fructose or D-glucosamine. Inorganic poly(P) could not replace ATP as the phosphate donor. M. tuberculosis H37Ra was unable to grow on D-mannose which may suggest that the enzyme studied is involved in endogenous metabolism of this sugar.
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PMID:A mannoglucokinese of Mycobacterium tuberculosis H37Ra. 1985 10