Cloned (Comment) | Organism |
---|---|
gene glcK, phylogenetic analysis and tree, functional complementation of enzyme-deficient Escherichia coli strain UE26, overexpression of His-tagged wild-type and mutant enzymes in Escherichia coli strain RB791 as soluble proteins | Bacillus subtilis |
Protein Variants | Comment | Organism |
---|---|---|
C166A | site-directed mutagenesis, mutant shows activity similar to the wild-type enzyme | Bacillus subtilis |
C175A | site-directed mutagenesis, inactive active site residue mutant | Bacillus subtilis |
C177A | site-directed mutagenesis, inactive active site residue mutant | Bacillus subtilis |
C182A | site-directed mutagenesis, inactive active site residue mutant | Bacillus subtilis |
C282A | site-directed mutagenesis, mutant shows slightly increased enzyme activity compared to the wild-type enzyme, conformational changes different from the wild-type enzyme, overview | Bacillus subtilis |
C321A | site-directed mutagenesis, mutant shows 5fold increased enzyme activity compared to the wild-type enzyme, conformational changes different from the wild-type enzyme, overview | Bacillus subtilis |
D10K | site-directed mutagenesis, ATP binding site mutant, inactive mutant | Bacillus subtilis |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
35000 | - |
recombinant enzyme, oxidative conditions, PAGE, the wild-type and mutant enzymes occur as both monomer and homodimer | Bacillus subtilis |
35200 | - |
recombinant enzyme, about, mass spectrometry, 2 peaks | Bacillus subtilis |
70000 | - |
recombinant enzyme, oxidative conditions, PAGE, the wild-type and mutant enzymes occur as both monomer and homodimer | Bacillus subtilis |
70400 | - |
recombinant enzyme, about, mass spectrometry, 2 peaks | Bacillus subtilis |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + D-glucose | Bacillus subtilis | - |
ADP + D-glucose 6-phosphate | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Bacillus subtilis | P54495 | - |
- |
Purification (Comment) | Organism |
---|---|
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain RB791 by nickel affinity chromatography | Bacillus subtilis |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
ATP + D-glucose = ADP + D-glucose 6-phosphate | the enzyme activity requires 3 cysteine residues C175, C177, and C182 within the motif CXCGX(2)GCXE that discriminates microbial glucokinases into two lineages | Bacillus subtilis |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + D-glucose | - |
Bacillus subtilis | ADP + D-glucose 6-phosphate | - |
? |
Subunits | Comment | Organism |
---|---|---|
dimer | 2 * 35200, about, mass spectrometry, 2 * 35000, recombinant enzyme, PAGE under oxidative conditions or SDS-PAGE in absence of reductants, the wild-type and mutant enzymes occur as both monomer and homodimer | Bacillus subtilis |
monomer | 1 * 35200, about, mass spectrometry, 1 * 35000, recombinant enzyme, PAGE under reducing conditions or SDS-PAGE in absence of reductants, the wild-type and mutant enzymes occur as both monomer and homodimer | Bacillus subtilis |
Synonyms | Comment | Organism |
---|---|---|
GlcK | - |
Bacillus subtilis |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
32 | - |
assay at | Bacillus subtilis |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.5 | - |
assay at | Bacillus subtilis |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
ATP | dependent on | Bacillus subtilis |