Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.7.1.30 extracted from

  • Thorner, J.W.; Paulus, H.
    Catalytic and allosteric properties of glycerol kinase from Escherichia coli (1973), J. Biol. Chem., 248, 3922-3932.
    View publication on PubMed

General Stability

General Stability Organism
normal and mutant enzyme stabilized against heat inactivation by glycerol, but not by fructose 1,6-bisphosphate Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
fructose 1,6-diphosphate normal enzyme is inhibited, genetically altered enzyme not, inhibition is reduced by high pH, high ionic strength or 0.2 M guanidine HCl Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information
-
Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
normal and genetically altered enzyme Escherichia coli

Reaction

Reaction Comment Organism Reaction ID
ATP + glycerol = ADP + sn-glycerol 3-phosphate ordered mechanism with glycerol as the first substrate to bind Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + glycerol
-
Escherichia coli ADP + sn-glycerol 3-phosphate
-
?

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
additional information
-
normal and mutant enzyme stabilized against heat inactivation by glycerol, but not by fructose 1,6-bisphosphate Escherichia coli