1.1.1.6: glycerol dehydrogenase
This is an abbreviated version!
For detailed information about glycerol dehydrogenase, go to the full flat file.
Reaction
Synonyms
B4100_2156, CglD, dehydrogenase, glycerol, GDH, GDH2, GLD, Gld3, GldA, GLDH
ECTree
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Metals Ions
Metals Ions on EC 1.1.1.6 - glycerol dehydrogenase
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Co2+
-
presence of Mn2+ enhances the enzyme activity by 31.4%
Cu2+
-
presence of Mn2+ enhances the enzyme activity by 37.0%
K+
Li+
Mg2+
improvement of stability, activity, and substrate promiscuity of glycerol dehydrogenase substituted by divalent metal ions Mn2+ and Mg2+, overview. The activity of Mn-GDH and Mg-GDH improves several folds in comparison to the native GDH. The activity of substituted GDH towards non-natural substrates, 4-chloroacetoacetate, 3-chloroacetylpyridine, p-chloroacetophenone, and acetophenone is 30folds higher than native GDH. Manganese substitution increases the half-life of GDH by 6folds at 60°C and 70°C
Mn2+
NH4+
Rb+
Zn2+
additional information
Mn2+
activates, polyethyleneimines-immobilized enzyme PEI-Mn2+-GDH exhibits a 2.9fold increase in activity compared with free GDH
Mn2+
improvement of activity by the substitution of a zinc ion with a manganese ion, accelerating the release of dioxyacetone
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
Mn2+
improvement of stability, activity, and substrate promiscuity of glycerol dehydrogenase substituted by divalent metal ions Mn2+ and Mg2+, overview
Mn2+
-
presence of Mn2+ enhances the enzyme activity by 79.5%
NH4+
-
activates, 4fold increase in Vmax produced by NH4Cl in the direction of glycerol oxidation, and 70fold reduction in the Km for dihydroxyaceton and 2fold increase in the Vmax with 30 mM NH4Cl added to the dihydroxyaceton reduction reaction
Zn2+
computer modeling suggests that the glycerol molecule is sandwiched by the Zn2+ and NAD+ ions
Zn2+
a zinc-dependent metalloenzyme, improvement of activity by the substitution of a zinc ion with a manganese ion
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
Zn2+
glycerol dehydrogenase from Klebsiella pneumoniae is a zinc-dependent metalloenzyme
Zn2+
-
active-site zinc responsible for coordinating glycerol in the active site of the enzyme. The active site is highly conserved and contains a zinc ion coordinated by two histidines and an aspartate
-
comparison of the binding energy of enzyme ternary complex for Mn-GDH and Zn-GDH
additional information
comparison of the binding energy of enzyme ternary complex for Mn-GDH and Zn-GDH
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
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
additional information
the natural GDH-bound Zn2+ are substituted with several divalent metal ions and the enzyme activity is significantly altered. Cu2+, Ni2+, Zn2+, Mn2+, Mg2+ and Ca2+ are used to investigate the effects of metal ions on GDH activity. Only Mn2+ improves the GDH activity by 1.1fold, whereas the other five metal ions inhibit the enzyme to varying degrees at high concentrations
additional information
bifunctional role of metal ions in GDH in catalysis and structure stabilization
additional information
-
three highly conserved enzyme residues, Asp171, His254, and His271, are associated with metal ion binding