Cloning, functional expression and partial characterization of the glucose kinase from Renibacterium salmoninarum.
The complete glcK gene from the fish pathogen Renibacterium salmoninarum, encoding a glucose kinase, was analyzed and expressed. The partial characterization of the recombinant enzyme confirmed that it belongs to a group of glucose kinases involved in carbon catabolite repression. Multiple sequence alignments were used to deduce a new consensus sequence for this family of bacterial proteins, characterized by several conserved Cys residues. This sequence was more specific and allowed the detection of the first eukaryotic protein of this family. The recombinant enzyme was inhibited by N-ethylmaleimide and the substrates protected the enzyme from this inhibition, suggesting the presence of Cys residues in or close to the active site.
Concha
M I
MI
Instituto de Bioquímica, Facultad de Ciencias, Universidad Austral de Chile, Casilla 567, Valdivia, Chile. mconcha@uach.cl
León
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D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D004269:DNA, Bacterial / Q000032:analysis; D005941:Glucokinase / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism*; D005947:Glucose / Q000378:metabolism; D008835:Micrococcaceae / Q000201:enzymology* / Q000235:genetics; D008969:Molecular Sequence Data; D011994:Recombinant Proteins / Q000235:genetics / Q000378:metabolism; D012487:Salmonidae / Q000382:microbiology; D017422:Sequence Analysis, DNA
D004269:DNA, Bacterial; D011994:Recombinant Proteins; D005941:Glucokinase; D005947:Glucose