Disease relevance of glk

• The glk gene from Corynebacterium glutamicum was isolated by complementation using Escherichia coli ZSC113 (ptsG ptsM glk) [1].
• Among these were genes encoding additional ADP-ribosyltransferases, a homolog of SrfC (a candidate effector in Salmonella enterica), a catalase, and a glucokinase [2].
• The glucose kinase gene of Streptomyces coelicolor A3(2): its nucleotide sequence, transcriptional analysis and role in glucose repression [3].
• The glucose kinase of Bacillus subtilis [4].
• Characterization of glk, a gene coding for glucose kinase of Corynebacterium glutamicum [1].

High impact information on glk

• Here we show that Mlc(Tth) is not a glucokinase but is indeed able to bind glucose (K(D) = 20 microM), unlike Mlc(Eco) [5].
• The open reading frame yqgR (now termed glcK), which had been sequenced as part of the genome project, encodes a glucose kinase of Bacillus subtilis [4].
• A B. subtilis strain deficient for glucose kinase grew at the same rate on different carbon sources tested, including disaccharides such as maltose, trehalose, and sucrose [4].
• Insertional mutagenesis of glcK resulted in a complete inactivation of glucose kinase activity in crude protein extracts, indicating that B. subtilis contains one major glucose kinase [4].
• A novel plasmid vector that uses the glucose kinase gene (glkA) for the positive selection of stable gene disruptants in Streptomyces [6].

Chemical compound and disease context of glk

• The highest titers and yields of shikimic acid biosynthesized from glucose in 1 L fermentor runs were achieved using E. coli SP1.lpts/pSC6.090B, which expressed both Z. mobilis glf-encoded glucose facilitator protein and Z. mobilis glk-encoded glucose kinase in a host deficient in the phosphoenolpyruvate:carbohydrate phosphotransferase system [7].

Biological context of glk

• The glk gene has a deduced molecular mass of 34.2 kDa and contains a typical ATP binding site [1].
• The glk gene in C. glutamicum was inactivated on the chromosome via single crossover homologous recombination and the resulting glk mutant was characterized [1].
• Integration of pIJ2581 derivatives carrying chromosomal sequences is achieved by selecting for plasmid-encoded thiostrepton resistance, while plasmid excision is secured by counter-selection of the pIJ2581 glkA gene, which confers sensitivity to 2-deoxyglucose [6].
• Glucose kinase, which we tentatively use in this review, represents the enzymes catalyzing the phosphorylation of glucose and other hexoses by means of phosphoryl donors (ATP, ADP, and inorganic polyphosphate [poly(P)]) [8].

Associations of glk with chemical compounds

• The presence of plasmid-encoded MalX alone was sufficient for complementing growth on glucose in a ptsM ptsG glk mutant, and the plasmid-encoded MalY alone was sufficient to abolish the constitutivity of the mal genes in a malK mutant [9].
• Interestingly, the C. glutamicum glk mutant showed poor growth on rich medium such as LB medium or brain heart infusion medium in the presence or absence of glucose, fructose, maltose or sucrose as the sole carbon source [1].

References