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Literature summary for 1.1.1.6 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)

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

Inhibitors

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 [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

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/ Products (Substrates)

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

Organism UniProt Comment Textmining
Klebsiella pneumoniae
-
-
-
Klebsiella pneumoniae B2ZPN8
-
-

Reaction

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 and Products (Substrate)

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

Synonyms Comment Organism
GDH
-
Klebsiella pneumoniae
GldA
-
Klebsiella pneumoniae
glycerol dehydrogenase
-
Klebsiella pneumoniae

Temperature Optimum [°C]

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

pH Optimum

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

Cofactor

Cofactor Comment Organism Structure
NAD+
-
Klebsiella pneumoniae
NADH
-
Klebsiella pneumoniae

Ki Value [mM]

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

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