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Literature summary for 2.7.1.2 extracted from

  • Imriskova, I.; Arreguin-Espinosa, R.; Guzman, S.; Rodriguez-Sanoja, R.; Langley, E.; Sanchez, S.
    Biochemical characterization of the glucose kinase from Streptomyces coelicolor compared to Streptomyces peucetius var. caesius (2005), Res. Microbiol., 156, 361-366.
    View publication on PubMed
Search for more literature for 2.7.1.2

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information kinetic mechanism Streptomyces coelicolor
additional information
-
 additional information kinetic mechanism Streptomyces peucetius subsp. caesius

Localization

Localization Comment Organism GeneOntology No. Textmining
cytosol over 96% of the enzyme content in the cell Streptomyces coelicolor 5829
-
cytosol over 96% of the enzyme content in the cell Streptomyces peucetius subsp. caesius 5829
-

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ as MgATP2- Streptomyces coelicolor
Mg2+ as MgATP2- Streptomyces peucetius subsp. caesius

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + D-glucose Streptomyces coelicolor
-
 ADP + D-glucose 6-phosphate
-
 ?
ATP + D-glucose Streptomyces peucetius subsp. caesius
-
 ADP + D-glucose 6-phosphate
-
 ?

Organism

Organism UniProt Comment Textmining
Streptomyces coelicolor P0A4E1 no isozymes
-
Streptomyces peucetius subsp. caesius
-
 no isozymes
-

Purification (Commentary)

Purification (Comment) Organism
-
 Streptomyces coelicolor

Reaction

Reaction Comment Organism Reaction ID
ATP + D-glucose = ADP + D-glucose 6-phosphate rapid equilibrium-ordered bi bi sequential mechanism, formation of a ternary complex of enzyme-D-glucose-MgATP2- Streptomyces coelicolor
a
ATP + D-glucose = ADP + D-glucose 6-phosphate rapid equilibrium-ordered bi bi sequential mechanism, formation of a ternary complex of enzyme-D-glucose-MgATP2- Streptomyces peucetius subsp. caesius
a

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.09
-
 purified enzyme, Vmax Streptomyces peucetius subsp. caesius
1.67
-
 purified enzyme, Vmax Streptomyces coelicolor

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + D-glucose
-
 Streptomyces coelicolor ADP + D-glucose 6-phosphate
-
 ?
ATP + D-glucose
-
 Streptomyces peucetius subsp. caesius ADP + D-glucose 6-phosphate
-
 ?
additional information comparison of the biochemical properties to those of the enzyme from Streptomyces coelicolor Streptomyces peucetius subsp. caesius ?
-
 ?
additional information comparison of the biochemical properties to those of the enzyme from Streptomyces peucetius var. caesius Streptomyces coelicolor ?
-
 ?

Subunits

Subunits Comment Organism
dimer
-
 Streptomyces peucetius subsp. caesius
tetramer stable form Streptomyces coelicolor
tetramer unstable form, rapid dissociation to dimers Streptomyces peucetius subsp. caesius

Synonyms

Synonyms Comment Organism
glk
-
 Streptomyces coelicolor
glk
-
 Streptomyces peucetius subsp. caesius

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
33
-
-
 Streptomyces coelicolor
42
-
-
 Streptomyces peucetius subsp. caesius

Cofactor

Cofactor Comment Organism Structure
ATP as MgATP2- Streptomyces coelicolor
ATP as MgATP2- Streptomyces peucetius subsp. caesius