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Literature summary for 2.7.1.2 extracted from

  • Mesak, L.R.; Mesak, F.M.; Dahl, M.K.
    Bacillus subtilis GlcK activity requires cysteines within a motif that discriminates microbial glucokinases into two lineages (2004), BMC Microbiol., 4, 6-13.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.7.1.2

Cloned(Commentary)

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

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 [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/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + D-glucose Bacillus subtilis
-
 ADP + D-glucose 6-phosphate
-
 ?

Organism

Organism UniProt Comment Textmining
Bacillus subtilis P54495
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain RB791 by nickel affinity chromatography Bacillus subtilis

Reaction

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
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + D-glucose
-
 Bacillus subtilis ADP + D-glucose 6-phosphate
-
 ?

Subunits

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

Synonyms Comment Organism
GlcK
-
 Bacillus subtilis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
32
-
 assay at Bacillus subtilis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
 assay at Bacillus subtilis

Cofactor

Cofactor Comment Organism Structure
ATP dependent on Bacillus subtilis