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Literature summary extracted from

  • Fang, B.; Niu, J.; Ren, H.; Guo, Y.; Wang, S.
    Mechanistic study of manganese-substituted glycerol dehydrogenase using a kinetic and thermodynamic analysis (2014), PLoS ONE, 9, e99162.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.1.1.6 gene gldA, recombinant expression in Escherichia coli strain BL21(DE3) Klebsiella pneumoniae

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.1.1.6 dihydroxyacetone noncompetitive product inhibition; noncompetitive product inhibition with respect to NAD+ Klebsiella pneumoniae
1.1.1.6 EDTA nearly complete inhibition Klebsiella pneumoniae
1.1.1.6 additional information enzyme inhibition simulations, overview Klebsiella pneumoniae
1.1.1.6 NADH competitive product inhibition; competitive product inhibition Klebsiella pneumoniae

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.1.6 additional information
-
 additional information kinetic model based on an ordered bi-bi mechanism, thermodynamics, simulations, overview Klebsiella pneumoniae
1.1.1.6 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

EC Number Metals/Ions Comment Organism Structure
1.1.1.6 Mn2+ improvement of activity by the substitution of a zinc ion with a manganese ion, accelerating the release of dioxyacetone Klebsiella pneumoniae
1.1.1.6 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
1.1.1.6 additional information comparison of the binding energy of enzyme ternary complex for Mn-GDH and Zn-GDH Klebsiella pneumoniae
1.1.1.6 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
1.1.1.6 Zn2+ a zinc-dependent metalloenzyme, improvement of activity by the substitution of a zinc ion with a manganese ion Klebsiella pneumoniae
1.1.1.6 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/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.1.6 glycerol + NAD+ Klebsiella pneumoniae
-
 glycerone + NADH + H+
-
 ?
1.1.1.6 glycerol + NAD+ Klebsiella pneumoniae
-
 glycerone + NADH + H+
-
 r

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.6 Klebsiella pneumoniae
-
-
-
1.1.1.6 Klebsiella pneumoniae B2ZPN8
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
1.1.1.6 glycerol + NAD+ = glycerone + NADH + H+ catalytic bi-bi mechanism Klebsiella pneumoniae
a
1.1.1.6 glycerol + NAD+ = glycerone + NADH + H+ the enzyme follows an ordered Bi-Bi mechanism kinetic model and shows product inhibition Klebsiella pneumoniae
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.6 glycerol + NAD+
-
 Klebsiella pneumoniae glycerone + NADH + H+
-
 ?
1.1.1.6 glycerol + NAD+
-
 Klebsiella pneumoniae glycerone + NADH + H+
-
 r

Synonyms

EC Number Synonyms Comment Organism
1.1.1.6 GDH
-
 Klebsiella pneumoniae
1.1.1.6 GldA
-
 Klebsiella pneumoniae
1.1.1.6 glycerol dehydrogenase
-
 Klebsiella pneumoniae

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.1.1.6 45
-
 assay at Klebsiella pneumoniae

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.1.6 12
-
 assay at Klebsiella pneumoniae

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.6 NAD+
-
 Klebsiella pneumoniae
1.1.1.6 NADH
-
 Klebsiella pneumoniae

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
1.1.1.6 additional information
-
 additional information preliminary kinetic parameters of substrate and product inhibition, overview Klebsiella pneumoniae

General Information

EC Number General Information Comment Organism
1.1.1.6 evolution NAD+-linked GDHs are members of the medium-chain alcohol dehydrogenase family, most of which are metalloenzymes Klebsiella pneumoniae
1.1.1.6 evolution the NAD+-linked GDHs are members of the medium-chain alcohol dehydrogenase family, most of which are metalloenzymes Klebsiella pneumoniae
1.1.1.6 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