Cloned (Comment) | Organism |
---|---|
gene gldA, recombinant expression in Escherichia coli strain BL21(DE3) | Klebsiella pneumoniae |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
dihydroxyacetone | noncompetitive product inhibition; noncompetitive product inhibition with respect to NAD+ | Klebsiella pneumoniae | |
EDTA | nearly complete inhibition | Klebsiella pneumoniae | |
additional information | enzyme inhibition simulations, overview | Klebsiella pneumoniae | |
NADH | competitive product inhibition; competitive product inhibition | Klebsiella pneumoniae |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | kinetic model based on an ordered bi-bi mechanism, thermodynamics, simulations, overview | Klebsiella pneumoniae | |
additional information | - |
additional information | kinetic modeling based on an ordered Bi-Bi mechanism, nonlinear regression-based kinetic parameter estimation. Thermodynamics, overview | Klebsiella pneumoniae |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mn2+ | improvement of activity by the substitution of a zinc ion with a manganese ion, accelerating the release of dioxyacetone | Klebsiella pneumoniae | |
Mn2+ | the enzyme demonstrates an improvement in activity by the substitution of a zinc ion with a manganese ion. Mn-GDH obeys a compulsory ordered-Bi-Bi mechanism | Klebsiella pneumoniae | |
additional information | comparison of the binding energy of enzyme ternary complex for Mn-GDH and Zn-GDH | Klebsiella pneumoniae | |
additional information | the equilibrium constants for each ligand-binding are calculated by using the forward and reverse rate constants. By profiling the binding rate and energy for substrate and product with enzyme, the rate accelerating step is determined | Klebsiella pneumoniae | |
Zn2+ | a zinc-dependent metalloenzyme, improvement of activity by the substitution of a zinc ion with a manganese ion | Klebsiella pneumoniae | |
Zn2+ | glycerol dehydrogenase from Klebsiella pneumoniae sp. is a zinc-dependent metalloenzyme. The enzyme demonstrates an improvement in activity by the substitution of a zinc ion with a manganese ion | Klebsiella pneumoniae |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
glycerol + NAD+ | Klebsiella pneumoniae | - |
glycerone + NADH + H+ | - |
? | |
glycerol + NAD+ | Klebsiella pneumoniae | - |
glycerone + NADH + H+ | - |
r |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Klebsiella pneumoniae | - |
- |
- |
Klebsiella pneumoniae | B2ZPN8 | - |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
glycerol + NAD+ = glycerone + NADH + H+ | catalytic bi-bi mechanism | Klebsiella pneumoniae | |
glycerol + NAD+ = glycerone + NADH + H+ | the enzyme follows an ordered Bi-Bi mechanism kinetic model and shows product inhibition | Klebsiella pneumoniae |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
glycerol + NAD+ | - |
Klebsiella pneumoniae | glycerone + NADH + H+ | - |
? | |
glycerol + NAD+ | - |
Klebsiella pneumoniae | glycerone + NADH + H+ | - |
r |
Synonyms | Comment | Organism |
---|---|---|
GDH | - |
Klebsiella pneumoniae |
GldA | - |
Klebsiella pneumoniae |
glycerol dehydrogenase | - |
Klebsiella pneumoniae |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
45 | - |
assay at | Klebsiella pneumoniae |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
12 | - |
assay at | Klebsiella pneumoniae |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NAD+ | - |
Klebsiella pneumoniae | |
NADH | - |
Klebsiella pneumoniae |
Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | preliminary kinetic parameters of substrate and product inhibition, overview | Klebsiella pneumoniae |
General Information | Comment | Organism |
---|---|---|
evolution | NAD+-linked GDHs are members of the medium-chain alcohol dehydrogenase family, most of which are metalloenzymes | Klebsiella pneumoniae |
evolution | the NAD+-linked GDHs are members of the medium-chain alcohol dehydrogenase family, most of which are metalloenzymes | Klebsiella pneumoniae |
additional information | mechanistic study of manganese-substituted glycerol dehydrogenase using a kinetic and thermodynamic analysis, overview. The binding energy of enzyme ternary complex for Mn-GDH and GDH derived from kinetic parameters indicates that metal ion substitution accelerates the release of dioxyacetone. The metal ion plays a role in catalysis enhancement | Klebsiella pneumoniae |