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Literature summary 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

KM Value [mM]

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

Localization

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

Metals/Ions

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

Natural Substrates/ Products (Substrates)

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

Organism

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

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.1.2
-
Streptomyces coelicolor

Reaction

EC Number Reaction Comment Organism Reaction ID
2.7.1.2 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
2.7.1.2 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

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.7.1.2 1.09
-
purified enzyme, Vmax Streptomyces peucetius subsp. caesius
2.7.1.2 1.67
-
purified enzyme, Vmax Streptomyces coelicolor

Substrates and Products (Substrate)

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

Subunits

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

Synonyms

EC Number Synonyms Comment Organism
2.7.1.2 glk
-
Streptomyces coelicolor
2.7.1.2 glk
-
Streptomyces peucetius subsp. caesius

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.7.1.2 33
-
-
Streptomyces coelicolor
2.7.1.2 42
-
-
Streptomyces peucetius subsp. caesius

Cofactor

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