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Information on EC 1.1.1.6 - glycerol dehydrogenase
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1.1.1.6 glycerol dehydrogenaseIUBMB Comments
Also acts on propane-1,2-diol.
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The enzyme appears in viruses and cellular organisms
Synonyms
CglD, dehydrogenase, glycerol, GDH, GDH2, GLD, GldA, GLDH 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
dehydrogenase, glycerol
-
-
-
-
GDH
GDH2
-
-
-
-
GLD
GldA
GLDH
-
-
-
-
glycerin dehydrogenase
-
-
-
-
glycerol dehydrogenase
glycerol NAD 2-oxidoreductase
-
-
-
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glycerol:NAD+ 2-oxidoreductase
-
-
-
-
GlyDH
NAD-linked glycerol dehydrogenase
-
-
-
-
NAD-specific glycerol dehydrogenase
-
-
-
-
TmGlyDH
TTHADH
glycerol dehydrogenase
-
type III polyol dehydrogenase family
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
glycerol + NAD+ = glycerone + NADH + H+
-
-
-
-
glycerol + NAD+ = glycerone + NADH + H+
catalytic bi-bi mechanism
glycerol + NAD+ = glycerone + NADH + H+
the enzyme follows an ordered Bi-Bi mechanism kinetic model and shows product inhibition
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
glycerol:NAD+ 2-oxidoreductase
Also acts on propane-1,2-diol.
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CAS REGISTRY NUMBER
COMMENTARY
249285-11-8
-
9028-14-2
this number also refers to EC 1.1.99.22
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1,2,3-butanetriol + NAD+
1,3-dihydroxybutane-2-one + NADH
-
-
-
?
1,3-butanediol + NAD+
?
-
relative activity is 6.5% compared to oxidation of glycerol
-
-
?
3-chloro-1,2-propanediol + NAD+
?
-
130% of the activity with glycerol
-
-
?
3-mercapto-1,2-propanediol + NAD+
?
-
155% of the activity with glycerol
-
-
?
beta-glycerophosphate + NAD+
?
-
relative activity is 2% compared to oxidation of glycerol
-
-
?
diglycerol + NAD+
?
-
relative activity is 21% compared to oxidation of glycerol
-
-
?
ethanol + NAD+
acetaldehyde + NADH
-
relative activity is 1% compared to oxidation of glycerol
-
-
?
glycerol + NAD+
D-glyceraldehyde + NADH + H+
-
no activity with NADP+. The enzyme shows much higher activity towards glycerol as compared to short chain primary and secondary alcohols. The thermostable enzyme is highly stereospecific in oxidation of glycerol and converts glycerol into D-glyceraldehyde
-
-
r
hydroxy-2-propanone + NADH
propylene glycol + NAD+
-
relative activity is 27% compared to oxidation of glycerol
-
-
?
i-inositol + NAD+
?
-
relative activity is 18% compared to oxidation of glycerol
-
-
?
isopropanol + NAD+
acetone + NADH
-
relative activity is 17% compared to oxidation of glycerol
-
-
?
sorbitol + NAD+
?
-
relative activity is 3% compared to oxidation of glycerol
-
-
?
(2R,3R)-2,3-butanediol + NAD+
(3R)-acetoin + NADH
-
-
more than 99% enantiomeric excess of R-product
-
r
(2R,3R)-2,3-butanediol + NAD+
(3R)-acetoin + NADH
-
-
more than 99% enantiomeric excess of R-product
-
r
(2R,3R)-2,3-butanediol + NAD+
? + NADH
-
better substrate than glycerol
-
-
?
(2R,3R)-2,3-butanediol + NAD+
? + NADH
-
better substrate than glycerol
-
-
?
(R)-1,2-propanediol + NAD+
? + NADH
-
better substrate than glycerol
-
-
?
(R)-1,2-propanediol + NAD+
hydroxyacetone + NADH
the enzyme prefers the R-enantiomer
-
-
r
(R)-1,2-propanediol + NAD+
hydroxyacetone + NADH
Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589
the enzyme prefers the R-enantiomer
-
-
r
1,2-propanediol + NAD+
hydroxyacetone + NADH
-
105% of the activity with glycerol
-
-
?
1,2-propanediol + NAD+
hydroxyacetone + NADH
-
relative activity is 116% compared to oxidation of glycerol
-
-
?
1,2-propanediol + NAD+
hydroxyacetone + NADH
-
relative activity is 116% compared to oxidation of glycerol
-
-
?
1,2-propanediol + NAD+
hydroxyacetone + NADH
-
as active as glycerol
-
-
?
1,2-propanediol + NAD+
hydroxyacetone + NADH
-
1,2-propanediol represses the global activator HilA that induces an invasive phenotype and repression of HilA could be weakened by glycerol dehydrogenase activity
-
-
?
1,3-butanediol + NAD+
4-hydroxy-2-butanone + NADH + H+
-
-
-
-
?
1,3-butanediol + NAD+
4-hydroxy-2-butanone + NADH + H+
-
-
-
-
?
1,3-dichloro-2-propanol + NAD+
1,3-dichloro-2-propanone + NADH
-
-
-
-
?
1,3-dichloro-2-propanol + NAD+
1,3-dichloro-2-propanone + NADH
-
-
-
-
?
1,3-propanediol + NAD+
?
-
relative rate of oxidation is 18% compared to oxidation of glycerol
-
-
?
1,3-propanediol + NAD+
?
-
relative rate of oxidation is 37% compared to oxidation of glycerol
-
-
?
1,4-butanediol + NAD+
?
-
relative activity is 0.3% compared to oxidation of glycerol
-
-
?
1,4-butanediol + NAD+
?
-
relative activity 17% compared to oxidation of glycerol
-
-
?
2,3-butanediol + NAD+
3-hydroxybutane-2-one + NADH
-
as active as glycerol
-
-
?
DL-alpha-glycerophosphate + NAD+
?
-
oxidation at 16% compared to oxidation of glycerol
-
-
?
DL-alpha-glycerophosphate + NAD+
?
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relative activity 11%compared to oxidation of glycerol
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-
?
DL-glyceraldehyde + NAD+
3-hydroxypyruvaldehyde + NADH
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relative rate of reduction is 14%compared to reduction of dihydroxyacetone
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-
?
DL-glyceraldehyde + NAD+
3-hydroxypyruvaldehyde + NADH
-
-
-
-
?
DL-glyceraldehyde + NAD+
3-hydroxypyruvaldehyde + NADH
-
-
-
?
ethanediol + NAD+
glycolaldehyde + NADH
-
-
reduction at concentration of 50 mM
r
ethanediol + NAD+
glycolaldehyde + NADH
-
-
reduction at concentration of 50 mM
r
ethylene glycol + NAD+
?
-
relative activity is 20% compared to oxidation of glycerol
-
-
?
glycerol + N6-carboxymethyl-NAD+
glycerone +N6-carboxymethyl-NADH + H+
-
-
-
r
glycerol + N6-carboxymethyl-NAD+
glycerone +N6-carboxymethyl-NADH + H+
Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589
-
-
-
r
glycerol + N6-CM-NAD+
glycerone +N6-carboxymethyl-NADH + H+
-
-
-
r
glycerol + N6-CM-NAD+
glycerone +N6-carboxymethyl-NADH + H+
Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589
-
-
-
r
glycerol + NAD+
dihydroxyacetone + NADH
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Glycerol dehydrogenase was immobilised in a polycarbamoyl sulfonate-hydrogel to be used as a sensor for glycerol. Glycerol oxidation leads to the reduction of NAD+ to NADH and electrons are transferred to ferricyanide on an electrode surface
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-
?
glycerol + NAD+
dihydroxyacetone + NADH
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the reaction is performed in reverse micelles harboring glycerol and NAD+ in a solution of isooctane containing 250 mM diocytlsulfosuccinate
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-
?
glycerol + NAD+
dihydroxyacetone + NADH
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the reaction is performed in reverse micelles harboring glycerol and NAD+ in a solution of isooctane containing 250 mM diocytlsulfosuccinate
-
-
?
glycerol + NAD+
dihydroxyacetone + NADH
-
-
-
-
?
glycerol + NAD+
glycerone + NADH + H+
activity of the enzyme is confirmed by proteome analysis and enzyme assays with cell extract glycerol-grown cells
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-
?
glycerol + NAD+
glycerone + NADH + H+
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-
-
r
glycerol + NAD+
glycerone + NADH + H+
no activity detected with NADP+
-
-
?
glycerol + NAD+
glycerone + NADH + H+
no activity detected with NADP+
-
-
?
glycerol + NAD+
glycerone + NADH + H+
-
glycerone reduction is the dominant reaction
i.e. 1,3-dihydroxypropranone
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r
glycerol + NAD+
glycerone + NADH + H+
-
-
-
-
r
glycerol + NAD+
glycerone + NADH + H+
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glycerone reduction is the dominant reaction
i.e. 1,3-dihydroxypropranone
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r
glycerol + NADP+
glyceraldehyde + NADPH + H+
-
activity observed with pentan-1-ol, 3-methyl-butan-1-ol, 1-decanol, low activity as ethanol dehydrogenase with NAD+ or NADPH+ as cofactor
-
-
?
glycerol + NADP+
glyceraldehyde + NADPH + H+
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activity observed with pentan-1-ol, 3-methyl-butan-1-ol, 1-decanol, low activity as ethanol dehydrogenase with NAD+ or NADPH+ as cofactor
-
-
?
glycerol-alpha-monochlorohydrin + NAD+
?
-
relative rate of oxidation is 71% compared to oxidation of glycerol
-
-
?
glycerol-alpha-monochlorohydrin + NAD+
?
-
relative rate of oxidation is 26% compared to oxidation of glycerol
-
-
?
meso-2,3-butanediol + NAD+
(3S)-acetoin + NADH
-
-
more than 99% enantiomeric excess of S-product
-
?
meso-2,3-butanediol + NAD+
(3S)-acetoin + NADH
-
-
more than 99% enantiomeric excess of S-product
-
?
methylglyoxal + NADH
lactaldehyde + NAD+
-
relative rate of reduction is 56% compared to reduction of dihydroxyacetone
-
-
?
additional information
?
-
-
ability of the enzyme to use glycerol from biodiesel waste as substrate, overview
-
-
?
additional information
?
-
-
efficiency of a cofactor regeneration enzyme co-expressed with a glycerol dehydrogenase for the production of 1,3-dihydroxyacetone. In vitro biotransformation of glycerol is achieved with the cell-free extracts containing recombinant glycerol dehydrogenase from Escherichia coli, lactate dehydrogenase form Bacillus subtilis, or NADH oxidase LpNox1 from Lactobacillus pentosus, giving1,3-dihydroxyacetone, overview
-
-
?
additional information
?
-
the enzyme is also active with substrates 4-chloroacetoacetate, 3-chloroacetylpyridine, 4-chloroacetophenone, and acetophenone, substrate specificities of enzyme with bound Zn2+, Mn2+, or Mg2+, overview
-
-
?
additional information
?
-
the enzyme is also active with substrates 4-chloroacetoacetate, 3-chloroacetylpyridine, 4-chloroacetophenone, and acetophenone, substrate specificities of enzyme with bound Zn2+, Mn2+, or Mg2+, overview
-
-
?
additional information
?
-
-
high specificity of enzyme for secondary alcohols in R-configuration
-
-
?
additional information
?
-
-
no substrate: 1,3-propanediol, ethanol, 1-propanol, 2-propanol, propionic acid, 1,4-butanediol, sorbitol, L-iditol. Stereospecificity for R-form
-
-
?
additional information
?
-
-
high specificity of enzyme for secondary alcohols in R-configuration
-
-
?
additional information
?
-
-
no substrate: 1,3-propanediol, ethanol, 1-propanol, 2-propanol, propionic acid, 1,4-butanediol, sorbitol, L-iditol. Stereospecificity for R-form
-
-
?
additional information
?
-
-
enzyme TtGlyDH preferentially catalyzes 1,3-dihydroxypropranone reduction rather than alcohol compound oxidation. Glycerol oxidization activity is faintly detected in the presence of a high concentration of glycerol (137 mM). No activity is detected with primary alcohols or diols. The highest glycerol oxidation activity is observed at the optimal growth temperature of 60°C in Tris-HCl buffer (50 mM, pH 8.0). Maximum DHA reduction activity is also observed at 60°C, and TtGlyDH exhibits the highest activity in an acetate buffer, compared with 91% maximum activity in an imidazole buffer at the same pH of 6.0
-
-
?
additional information
?
-
-
enzyme TtGlyDH preferentially catalyzes 1,3-dihydroxypropranone reduction rather than alcohol compound oxidation. Glycerol oxidization activity is faintly detected in the presence of a high concentration of glycerol (137 mM). No activity is detected with primary alcohols or diols. The highest glycerol oxidation activity is observed at the optimal growth temperature of 60°C in Tris-HCl buffer (50 mM, pH 8.0). Maximum DHA reduction activity is also observed at 60°C, and TtGlyDH exhibits the highest activity in an acetate buffer, compared with 91% maximum activity in an imidazole buffer at the same pH of 6.0
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
glycerol + NAD+
glycerone + NADH + H+
-
-
-
r
glycerol + NAD+
glycerone + NADH + H+
-
-
-
-
r
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
N6-carboxymethyl-NAD+
wild-type enzyme TmGlyDH shows little activity with N6-carboxymethyl-NAD+ (N6-CM-NAD), an NAD+ analogue modified for easy immobilization to amino groups, but the double mutation V44A/K157G increases catalytic efficiency with N6-CMNAD+ by 10fold. kinetics with N6-CM-NAD+ and modelling, overview. N6-CM-NAD+ is immobilized on cyanogen bromide-activated Sepharose 4b
additional information
-
the enzyme's atypical dinucleotide binding motif (GGG motif) and basic residue Arg43 are both related to dinucleotide binding
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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+
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
additional information
-
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
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1,3-Propanediol
-
competitive inhibitor versus glycerol in direction of glycerol oxidation, noncompetitive inhibitor versus NAD+, competitive inhibitor versus dihydroxyacetone in direction of glycerol reduction, noncompetitive inhibitor versus NADH
2-amino-2-(hydroxymethyl)-1,3-propanediol
-
strong inhibition, IC50 2 mM
catechol
-
i.e. 1,2-butanediol, inactivation, enzyme regains activity after removal of alcohol
ethanol
-
10% v/v: 25-75% loss of activity, depending on substrate, enzyme regains activity after removal of alcohol
isobutanol
-
5% v/v: 0-50% loss of activity, depending on substrate, enzyme regains activity after removal of alcohol
methanol
-
10% v/v: 25-75% loss of activity, 5% v/v, 50-95% loss of activity, depending on substrate, enzyme regains activity after removal of alcohol
n-amyl alcohol
-
2% v/v: 0-50% loss of activity, depending on substrate, enzyme regains activity after removal of alcohol
n-butanol
-
5% v/v: 0-50% loss of activity, depending on substrate, enzyme regains activity after removal of alcohol
n-Propanol
-
5% v/v: 25-60% loss of activity, depending on substrate, enzyme regains activity after removal of alcohol
o-phthalaldehyde
-
inactivation due to intramolecular thioisoindole formation, glycerol partially protects
2-mercaptoethanol
-
strongly inhibitory at 100 mM, but slight activation in lower concentration, 1 mM
dihydroxyacetone
noncompetitive product inhibition; noncompetitive product inhibition with respect to NAD+
NADH
-
competitive inhibitor versus NAD+ in direction of glycerol oxidation, noncompetitive inhibitor versus glycerol
NADH
competitive product inhibition; competitive product inhibition
additional information
enzyme inhibition simulations, overview
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
citrate
-
the enzyme is more active in presence of multivalent anions, citrate, phosphate or sulfate, in comparison to monovalent anions, e.g. acetate or chloride
iodoacetamide
-
at 1 mM 140% of the activity without activator, at 10 mM 220% of the activity without activator
N-ethylmaleimide
-
at 0.1 mM 145% of the activity without activator
p-chloromercuribenzoic acid
-
at 0.1 mM 133% of the activity without activator
phosphate
-
the enzyme is more active in presence of multivalent anions, citrate, phosphate or sulfate, in comparison to monovalent anions, e.g. acetate or chloride
polyethyleneimines
PEI, activating at 0.5 mM, inhibitory at 1 mM
-
SO42-
-
the enzyme is more active in presence of multivalent anions, citrate, phosphate or sulfate, in comparison to monovalent anions, e.g. acetate or chloride
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Adrenocortical Hyperfunction
Effect of serum storage, anti-inflammatory oral doses of prednisone, and spontaneous hyperadrenocorticism on serum glutamate dehydrogenase activity in dogs.
Brain Neoplasms
Levels of glutamic acid decarboxylase (GAD), gamma amino butyric acid transaminase (GABA-T), glutamic acid dehydrogenase (GLDH) and proteins in cerebrospinal fluid of certain neurological disorders.
Carcinoma
Changes in serum enzyme activity after transcatheter arterial embolization for hepatic neoplasm.
Carcinoma, Hepatocellular
Changes in serum enzyme activity after transcatheter arterial embolization for hepatic neoplasm.
Chemical and Drug Induced Liver Injury
A longitudinal assessment of miR-122 and GLDH as biomarkers of drug-induced liver injury in the rat.
Chemical and Drug Induced Liver Injury
Serum glutamate dehydrogenase activity enables early detection of liver injury in subjects with underlying muscle impairments.
Cholestasis
Activities of APh, gamma-GT, GlDH and GPT and bile acid concentrations in serum after bile duct obstruction and cycloheximide in the rat.
Cholestasis
The serum activities of AP, gamma-GT, GlDH and GPT after bile duct obstruction and ethionine in the rat.
Dystocia
Effects of dystocia, fetotomy and caesarian sections on the liver enzymes activities and concentrations of some serum biochemical parameters in dairy cattle.
Eosinophilia
Host responses during experimental infection with Fasciola gigantica and Fasciola hepatica in Merino sheep II. Development of a predictive index for Fasciola gigantica worm burden.
Eosinophilia
Pre-exposure of cattle to drug-abbreviated Fasciola hepatica infections: the effect upon subsequent challenge infection and the early immune response.
Fatty Liver
[Increased gamma-GT, minimal changes in liver histology, abdominal complaints--a functional liver liver disease]
Hemoglobinuria
Serum glutamic oxalacetic transaminase, glutamic pyruvic transaminase, gamma-glutamyl transpeptidase and glutamic dehydrogenase levels in favism.
Hepatic Encephalopathy
A study of lipid peroxidation and vitamin E in dairy cows with hepatic insufficiency.
Hepatitis
[Diagnostic and prognostic significance of massively increased serum glutamate dehydrogenase activity]
Hepatitis, Autoimmune
Relation between autoimmune liver diseases and viral hepatitis: clinical and serological characteristics in 859 patients.
Infections
Acquisition of resistance against Fasciola gigantica by Indonesian thin tail sheep.
Infections
An experimental study on triclabendazole resistance of Fasciola hepatica in sheep.
Infections
Epidemiology, genetic variants and clinical course of natural infections with Anaplasma phagocytophilum in a dairy cattle herd.
Leukopenia
Epidemiology, genetic variants and clinical course of natural infections with Anaplasma phagocytophilum in a dairy cattle herd.
Liver Failure
A study of lipid peroxidation and vitamin E in dairy cows with hepatic insufficiency.
Lymphopenia
Epidemiology, genetic variants and clinical course of natural infections with Anaplasma phagocytophilum in a dairy cattle herd.
Meningitis
Levels of glutamic acid decarboxylase (GAD), gamma amino butyric acid transaminase (GABA-T), glutamic acid dehydrogenase (GLDH) and proteins in cerebrospinal fluid of certain neurological disorders.
Meningitis
Tentative identification of glycerol dehydrogenase as Escherichia coli K1 virulence factor cglD and its involvement in the pathogenesis of experimental neonatal meningitis.
Muscular Dystrophies
Serum glutamate dehydrogenase activity enables early detection of liver injury in subjects with underlying muscle impairments.
Neoplasm Metastasis
Alpha 1 isoenzyme of alkaline phosphatases. Clinical importance and value for the detection of liver metastases.
Neutropenia
Epidemiology, genetic variants and clinical course of natural infections with Anaplasma phagocytophilum in a dairy cattle herd.
Pancreatitis
[Impairment of glycerophosphate and glycerol turnover in myocardium under conditions of experimental pancreatitis]
Pneumonia
A non-pathogenic and optically high concentrated (R,R)-2,3-butanediol biosynthesizing Klebsiella strain.
Rhabdomyolysis
Serum glutamate dehydrogenase activity enables early detection of liver injury in subjects with underlying muscle impairments.
Scabies
Histology of the skin and determination of blood and serum parameters during the recovery phase of sarcoptic manage in cattle after avermectin (Ivomec) treatment.
Toxemia
[Value of placental enzymes, endocrinologic parameters of pregnancy and placental perfusion in cases of intrauterine growth retardation]
Tuberculosis, Meningeal
Levels of glutamic acid decarboxylase (GAD), gamma amino butyric acid transaminase (GABA-T), glutamic acid dehydrogenase (GLDH) and proteins in cerebrospinal fluid of certain neurological disorders.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.07
D-glyceraldehyde
-
pH and temperature not specified in the publication
56
ethylene glycol
-
pH and temperature not specified in the publication
77.8
1,3-butanediol
-
mutant protein Q70H/D121A/G193C/E291Q/A310T, pH 9.5, 30°C
19.4
glycerol
recombinant chimeric enzyme GDH-NOX, pH 11.0, 37°C
30.29
glycerol
-
pH 8.0, 60°C, recombinant enzyme
0.22
Glycerone
-
pH 6.5, 30°C, recombinant enzyme, in presence of 30 mM NH4Cl
1.08
Glycerone
-
pH 6.0, 60°C, recombinant enzyme
0.08
N6-carboxymethyl-NAD+
mutant enzyme K157G, at pH 7.4 and 50°C
0.186
N6-carboxymethyl-NAD+
pH 7.4, 50°C, recombinant mutant V44A/K157N
0.186
N6-carboxymethyl-NAD+
mutant enzyme V44A/ K157N, at pH 7.4 and 50°C
0.25
N6-carboxymethyl-NAD+
pH 7.4, 50°C, recombinant mutant V44A/K157G
0.25
N6-carboxymethyl-NAD+
mutant enzyme V44A/K157G, at pH 7.4 and 50°C
0.36
N6-carboxymethyl-NAD+
mutant enzyme K157N, at pH 7.4 and 50°C
0.37
N6-carboxymethyl-NAD+
pH 7.4, 50°C, recombinant wild-type enzyme
0.73
N6-carboxymethyl-NAD+
mutant enzyme I154A, at pH 7.4 and 50°C
1.5
N6-carboxymethyl-NAD+
pH 7.4, 50°C, recombinant mutant I154A/K157G
1.5
N6-carboxymethyl-NAD+
mutant enzyme I154A/K157G, at pH 7.4 and 50°C
2.3
N6-carboxymethyl-NAD+
pH 7.4, 50°C, recombinant mutant V44A/I154A/K157G
2.3
N6-carboxymethyl-NAD+
mutant enzyme V44A/I154A/K157G, at pH 7.4 and 50°C
2.9
N6-carboxymethyl-NAD+
pH 7.4, 50°C, recombinant mutant V44A/I154A
2.9
N6-carboxymethyl-NAD+
mutant enzyme V44A/ I154A, at pH 7.4 and 50°C
0.23
NAD+
Mg-GDH, pH 12.0, 45°C, recombinant enzyme
0.38
NAD+
wild-type Zn-GDH, pH 12.0, 45°C, recombinant enzyme
1.12
NAD+
Mg-GDH, pH 12.0, 45°C, recombinant enzyme
additional information
additional information
-
kinetic study with different effectors, overview
-
additional information
additional information
kinetic and thermodynamic analysis, Michaelis-Menten kinetics, overview
-
additional information
additional information
-
kinetic model based on an ordered bi-bi mechanism, thermodynamics, simulations, overview
-
additional information
additional information
kinetic model based on an ordered bi-bi mechanism, thermodynamics, simulations, overview
-
additional information
additional information
-
kinetic modeling based on an ordered Bi-Bi mechanism, nonlinear regression-based kinetic parameter estimation. Thermodynamics, overview
-
additional information
additional information
kinetic modeling based on an ordered Bi-Bi mechanism, nonlinear regression-based kinetic parameter estimation. Thermodynamics, overview
-
additional information
additional information
kinetic study of the metal ion-chelated polyethyleneimines-immobilized enzyme
-
additional information
additional information
Michaelis-Menten kinetics, cooperative behavior of TmGlyDH
-
additional information
additional information
-
Michaelis-Menten kinetics, cooperative behavior of TmGlyDH
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
98.44
Glycerone
-
pH 6.0, 60°C, recombinant enzyme
87.2
1,3-butanediol
-
mutant protein Q70H/D121A/G193C/E291Q/A310T, pH 9.5, 30°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
91.15
Glycerone
-
pH 6.0, 60°C, recombinant enzyme
1.12
1,3-butanediol
-
mutant protein Q70H/D121A/G193C/E291Q/A310T, pH 9.5, 30°C
46.1
NAD+
wild-type Zn-GDH, pH 12.0, 45°C, recombinant enzyme
83.6
NAD+
Mg-GDH, pH 12.0, 45°C, recombinant enzyme
120.3
NAD+
Mg-GDH, pH 12.0, 45°C, recombinant enzyme
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
preliminary kinetic parameters of substrate and product inhibition, overview
-
additional information
additional information
preliminary kinetic parameters of substrate and product inhibition, overview
-
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2
2-amino-2-(hydroxymethyl)-1,3-propanediol
Pichia membranifaciens
-
strong inhibition, IC50 2 mM
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.01
wild type, crude cell extract, pH not specified in the publication, temperature not specified in the publication
0.049
overexpressing cells, crude cell extract, pH not specified in the publication, temperature not specified in the publication
1.26
15.7
recombinant His-tagged chimeric enzyme GDH-NOX, pH 11.0, 37°C
220
4.7
45
purified recombinant enzyme, oxidation of glycerol, 80°C, pH 7.4
6
-
mutant protein D16N/N19A/E23D/L28M/E30N/R31N/Q45E/S46E/V48L/E49R/F52L/K53T/D54G/V58S/G78V/I79V/T82K/A83S/I88V/G108N/R139S/L142M/N145R/K155Q/L211I/G248S/V256I/H268Y/D317E/P319L, pH 9.5, 30°C
6.8
-
mutant protein A15T/D16G/V17A/N19K/E23D/Q45E/S46E/T47M/V48L/E49R/F52L/K53A/V58A/V59A/Q70H/D74N/G78D/E81G/T82N/Q83K/G86T/I88V/G108N/R139S/L142M/N145R/K155Q/V256I/L260M, pH 9.5, 30°C
7.4
-
mutant protein Q70H/D74N/G78D/E81G/T82N/Q83K/C84Y/G86T/I88V/G108N/E134A/E204K/L211I/E215K/I234V/V256I/L260M/E291D/S300C/A302S/E316G/V318I/A320T/I324L/T344D/P345S, pH 9.5, 30°C
additional information
-
assay development for NADH production by recombinant enzyme in reverse micelles, micelle size optimization, overview
220
cell free extract, recombinant strain (over-expression of gycerol dehydrogenase)
220
recombinant strain (overexpression), crude extract, pH not specified in the publication, temperature not specified in the publication
4.7
wild type, crude extract, pH not specified in the publication, temperature not specified in the publication
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10
10 - 11
the immobilized GDH changes the optimal pH from pH 11 to 10 and exhibits high activity in a relatively wide range of pH from pH 7 to 12, while free GDH only achieves high activity at pH 11
11
12
7.5
9.5
additional information
kinetic study of the metal ion-chelated polyethyleneimines-immobilized enzyme
8
-
oxidation of glycerol, tetraethyl ammonium chloride/tetraethylammonium hydroxide buffer
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3 - 9
-
dihydroxyaceton reduction reaction, activity range, profile overview
4.8 - 7.8
-
pH 4.8: about 40% of maximal activity, pH 7.8: about 50% of maximal activity, reduction of dihydroxyacetone
5.5 - 9
-
pH 5.5: about 70% of maximal activity, pH 9.0: about 45% of maximal activity, reduction of dihydroxyacetone
6 - 11
6.8 - 11
-
the initial rate of reaction increases upon increasing the pH from pH 6.8 to 11.0, past pH 11.0 the initial rate falls rapidly, oxidation of glycerol
7 - 10
8 - 10.5
-
pH 8.0: about 40% of maximal activity, pH 10.5: about 70% of maximal activity, oxidation of glycerol
9 - 11
-
pH 9.0: maximal activity, pH 11.0.: nearly inactive, oxidation of glycerol
9 - 12
-
pH 9.0: about 45% of maximal activity, pH 11-12: maximal activity, oxidation of glycerol
7 - 10
-
pH 7.0: about 60% of maximal activity, pH 10.0: about 85% of maximal activity, oxidation of glycerol
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
45
50
60
80
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
kinetic study of the metal ion-chelated polyethyleneimines-immobilized enzyme
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.7
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
soluble, isolation from crude cell extract
brenda
-
soluble, isolation from crude cell extract
brenda
-
soluble, isolation from crude cell extract
brenda
-
soluble, isolation from crude cell extract
brenda
-
soluble, isolation from crude cell extract
-
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
metabolism
physiological function
additional information
evolution
-
the enzyme belongs to the medium-chain dehydrogenase/reductase, MDRase, superfamily
evolution
NAD+-linked GDHs are members of the medium-chain alcohol dehydrogenase family, most of which are metalloenzymes
evolution
-
the enzyme belongs to the Fe-ADH family. The GXGXXG motif is not present in TtGlyDH or other members of the Fe-ADH family, the GGG motif forms a more flexible turn and provides enough space to accommodate the pyrophosphate moiety of dinucleotides
evolution
the NAD+-linked GDHs are members of the medium-chain alcohol dehydrogenase family, most of which are metalloenzymes
evolution
-
the Serratia marcescens enzyme belongs to the type III Fe-ADH superfamily, three consecutive glycine residues belong to a 14-amino acid residue motif (GDK motif) as the coenzyme NAD(H) binding site, and three conserved histidine residues belong to a 16-residue segment that is homologous to the 15-residue stretch as the binding site of metal
evolution
-
the enzyme belongs to the Fe-ADH family. The GXGXXG motif is not present in TtGlyDH or other members of the Fe-ADH family, the GGG motif forms a more flexible turn and provides enough space to accommodate the pyrophosphate moiety of dinucleotides
-
evolution
-
the Serratia marcescens enzyme belongs to the type III Fe-ADH superfamily, three consecutive glycine residues belong to a 14-amino acid residue motif (GDK motif) as the coenzyme NAD(H) binding site, and three conserved histidine residues belong to a 16-residue segment that is homologous to the 15-residue stretch as the binding site of metal
-
metabolism
-
in Escherichia coli, the enzyme catalyzes the first step in fermentative glycerol metabolism to produce dihydroxyacetone, biochemical transformation pathway of glycerol, overview
metabolism
-
glycerol is one of the key metabolites for propionic acid synthesis in Propionibacterium jensenii. It is a precursor for metabolic pathways for propionic acid, lactic acid, and acetic acid biosynthesis in Propionibacterium
metabolism
anaerobic fermentative metabolism of glycerol: proteome analysis as well as enzyme assays performed in cell-free extracts demonstrate that glycerol is degraded via glyceraldehyde-3-phosphate, which is further metabolized through the lower part of glycolysis leading to formation of mainly ethanol and hydrogen
metabolism
-
glycerol is one of the key metabolites for propionic acid synthesis in Propionibacterium jensenii. It is a precursor for metabolic pathways for propionic acid, lactic acid, and acetic acid biosynthesis in Propionibacterium
-
physiological function
-
GroDHase is mainly involved in Gro utilization as a carbon and energy source
physiological function
-
glycerol dehydrogenase is the enzyme responsible for the oxidation of glycerol to dihydroxyacetone. This permits its entrance into the glycolytic pathway
physiological function
-
glycerol dehydrogenases (GlyDHs) are essential for glycerol metabolism in vivo, catalyzing its reversible reduction to 1,3-dihydroxypropranone
physiological function
-
glycerol dehydrogenases (GlyDHs) are essential for glycerol metabolism in vivo, catalyzing its reversible reduction to 1,3-dihydroxypropranone
-
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
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
additional information
-
molecular modeling and site-directed mutagenesis analyses demonstrate that TtGlyDH has an atypical dinucleotide binding motif (GGG motif) and a basic residue Arg43, both related to dinucleotide binding
additional information
-
molecular modeling and site-directed mutagenesis analyses demonstrate that TtGlyDH has an atypical dinucleotide binding motif (GGG motif) and a basic residue Arg43, both related to dinucleotide binding
-
Show AA Sequence and Transmembrane Helices (3025 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
336000 - 390000
38000
38742
x * 38742 , calculated, 367 amino acid residues
39000
39500
39800
-
8 * 40000, recombinant His-tagged enzyme, SDS-PAGE, 8 * 39800, about, sequence calculation
40000
40000
-
8 * 40000, recombinant His-tagged enzyme, SDS-PAGE, 8 * 39800, about, sequence calculation
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homotetramer
monomer
octamer
tetramer
additional information
?
x * 38742 , calculated, 367 amino acid residues
octamer
-
8 * 40000, recombinant His-tagged enzyme, SDS-PAGE, 8 * 39800, about, sequence calculation
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal obtained by hanging-drop vaour-diffusion method, S305C mutant
-
preliminary X-ray characterization
sitting drop vapor-diffusion method
hanging drop vapour diffusion, mixing of 0.001 ml 6 mg/ml protein in 150 mM ammonium acetate, 50 mM sodium chloride, 20 mM Tris, pH 7.4, 5% glycerol with 0.001 ml reservoir solution containing 5-10% PEG 3350, 0.2 M calcium acetate, and 4% glycerol, X-ray diffraction structure determination and analysis at 1.90 A resolution, molecular replacement using PDB entry 1jpu as a search model
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A15T/D16G/V17A/N19K/E23D/Q45E/S46E/T47M/V48L/E49R/F52L/K53A/V58A/V59A/Q70H/D74N/G78D/E81G/T82N/Q83K/G86T/I88V/G108N/R139S/L142M/N145R/K155Q/V256I/L260M
-
mutant selected from a DNA shuffling library (Escherichia coli, Salmonella enterica, Klebsiella pneumoniae)
D121A
-
D121 can potentially hinder the proper binding of substrate 1,3-butanediol due to steric hindrance
D16N/N19A/E23D/L28M/E30N/R31N/Q45E/S46E/V48L/E49R/F52L/K53T/D54G/V58S/G78V/I79V/T82K/A83S/I88V/G108N/R139S/L142M/N145R/K155Q/L211I/G248S/V256I/H268Y/D317E/P319L
-
mutant selected from a DNA shuffling library (Escherichia coli, Salmonella enterica, Klebsiella pneumoniae)
Q70H/D121A/G193C/E291Q/A310T
-
mutant selected from a DNA shuffling library (Escherichia coli, Salmonella enterica, Klebsiella pneumoniae) and site-directed mutation D121A
Q70H/D74N/G78D/E81G/T82N/Q83K/C84Y/G86T/I88V/G108N/E134A/E204K/L211I/E215K/I234V/V256I/L260M/E291D/S300C/A302S/E316G/V318I/A320T/I324L/T344D/P345S
-
mutant selected from a DNA shuffling library (Escherichia coli, Salmonella enterica, Klebsiella pneumoniae)
Q70H/G193C/E291Q/A310T
-
mutant selected from a DNA shuffling library (Escherichia coli, Salmonella enterica, Klebsiella pneumoniae)
I154A
site-directed mutagenesis, the mutant shows altered activity with cofactor derivative N6-CM-NAD+ immobilized on Sepharose beads compared to the wild-type enzyme
I154A/K157G
site-directed mutagenesis, the mutant shows altered activity with cofactor derivative N6-CM-NAD+ immobilized on Sepharose beads compared to the wild-type enzyme
I154A/K157N
site-directed mutagenesis, the mutant shows altered activity with cofactor derivative N6-CM-NAD+ immobilized on Sepharose beads compared to the wild-type enzyme
K157G
site-directed mutagenesis, the mutant shows altered activity with cofactor derivative N6-CM-NAD+ immobilized on Sepharose beads compared to the wild-type enzyme
K157N
site-directed mutagenesis, the mutant shows altered activity with cofactor derivative N6-CM-NAD+ immobilized on Sepharose beads compared to the wild-type enzyme
V44A
site-directed mutagenesis, the mutant shows altered activity with cofactor derivative N6-CM-NAD+ immobilized on Sepharose beads compared to the wild-type enzyme
V44A/I154A
site-directed mutagenesis, the mutant shows altered activity with cofactor derivative N6-CM-NAD+ immobilized on Sepharose beads compared to the wild-type enzyme
V44A/K157G
V44A/K157N
site-directed mutagenesis, the mutant shows altered activity with cofactor derivative N6-CM-NAD+ immobilized on Sepharose beads compared to the wild-type enzyme
I154A
Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589
-
site-directed mutagenesis, the mutant shows altered activity with cofactor derivative N6-CM-NAD+ immobilized on Sepharose beads compared to the wild-type enzyme
-
K157N
Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589
-
site-directed mutagenesis, the mutant shows altered activity with cofactor derivative N6-CM-NAD+ immobilized on Sepharose beads compared to the wild-type enzyme
-
V44A
Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589
-
site-directed mutagenesis, the mutant shows altered activity with cofactor derivative N6-CM-NAD+ immobilized on Sepharose beads compared to the wild-type enzyme
-
V44A/K157G
additional information
V44A/K157G
site-directed mutagenesis, the mutant shows altered activity with cofactor derivative N6-CM-NAD+ immobilized on Sepharose beads compared to the wild-type enzyme
V44A/K157G
site-directed mutagenesis, wild-type enzyme TmGlyDH shows little activity with N6-carboxymethyl-NAD+ (N6-CM-NAD), an NAD+ analogue modified for easy immobilization to amino groups, but the double mutation V44A/K157G increases catalytic efficiency with N6-CMNAD+ by 10fold
V44A/K157G
Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589
-
site-directed mutagenesis, the mutant shows altered activity with cofactor derivative N6-CM-NAD+ immobilized on Sepharose beads compared to the wild-type enzyme
-
V44A/K157G
Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589
-
site-directed mutagenesis, wild-type enzyme TmGlyDH shows little activity with N6-carboxymethyl-NAD+ (N6-CM-NAD), an NAD+ analogue modified for easy immobilization to amino groups, but the double mutation V44A/K157G increases catalytic efficiency with N6-CMNAD+ by 10fold
-
additional information
-
efficiency of a cofactor regeneration enzyme co-expressed with a glycerol dehydrogenase for the production of 1,3-dihydroxyacetone. In vitro biotransformation of glycerol is achieved with the cell-free extracts containing recombinant glycerol dehydrogenase from Escherichia coli, lactate dehydrogenase form Bacillus subtilis, or NADH oxidase LpNox1 from Lactobacillus pentosus, giving1,3-dihydroxyacetone, coexpression of all enzymes in Escherichia coli strain BL21(DE3)
additional information
bioinspired immobilization of glycerol dehydrogenase by metal ion-chelated polyethyleneimines (PEI) as artificial polypeptides. Nanoparticles with diameters from 250–650 nm are prepared that exhibit a 1.4fold enhancement catalytic efficiency. The oligomeric GDH assemblies are coated and stabilized by the excessive manganese-chelated PEIs, which further prevents the disassociation of the GDH subunits, metal-mediated oligomeric assemblies of the enzyme. Half-life of immobilized GDH is enhanced by 5.6folds in aqueous phase at 85°C. Formation of multi-level interactions in the PEI-metal-GDH complex, mechanism, overview. A potential technique for multimeric enzyme immobilization with the advantages of low cost, easy operation, high activity reservation, and high stability. The activity of PEI-Mn2+-GDH gradually decreases over 5 cycles. PEI-Mn2+-GDH retains 71% and 53% of its initial activity after cycling through 3 and 5 successive reactions, respectively. The decrease in the activity of the recycled catalyst may be due to the leakage of GDH
additional information
the glycerol dehydrogenase gene from Klebsiella pneumoniae is fused to codon-optimized NADH oxidase gene from Lactobacillus brevis. Gene fusion of glycerol dehydrogenase (GDH) and NOX forms a bifunctional multienzyme for bioconversion of glycerol coupled with coenzyme regeneration
additional information
-
the glycerol dehydrogenase gene from Klebsiella pneumoniae is fused to codon-optimized NADH oxidase gene from Lactobacillus brevis. Gene fusion of glycerol dehydrogenase (GDH) and NOX forms a bifunctional multienzyme for bioconversion of glycerol coupled with coenzyme regeneration
-
additional information
-
bioinspired immobilization of glycerol dehydrogenase by metal ion-chelated polyethyleneimines (PEI) as artificial polypeptides. Nanoparticles with diameters from 250–650 nm are prepared that exhibit a 1.4fold enhancement catalytic efficiency. The oligomeric GDH assemblies are coated and stabilized by the excessive manganese-chelated PEIs, which further prevents the disassociation of the GDH subunits, metal-mediated oligomeric assemblies of the enzyme. Half-life of immobilized GDH is enhanced by 5.6folds in aqueous phase at 85°C. Formation of multi-level interactions in the PEI-metal-GDH complex, mechanism, overview. A potential technique for multimeric enzyme immobilization with the advantages of low cost, easy operation, high activity reservation, and high stability. The activity of PEI-Mn2+-GDH gradually decreases over 5 cycles. PEI-Mn2+-GDH retains 71% and 53% of its initial activity after cycling through 3 and 5 successive reactions, respectively. The decrease in the activity of the recycled catalyst may be due to the leakage of GDH
-
additional information
-
recombinant co-overexpression of enzymes glycerol dehydrogenase, malate dehydrogenase, and fumarate hydratase from Klebsiella pneumoniae subsp. pneumoniae strain ATCC 12657 in Propionibacterium jensenii leads to increased increased propionic acid production. The transcription levels of the corresponding enzymes in the engineered strains are 2.85 to 8.07fold higher than those in the wild type. The coexpression of GDH and MDH increases the propionic acid titer from 26.95 g/liter in wild-type to 39.43 g/liter in the engineered strains. Fed-batch culture kinetics of propionic acid production from glycerol, overview
additional information
-
recombinant co-overexpression of enzymes glycerol dehydrogenase, malate dehydrogenase, and fumarate hydratase from Klebsiella pneumoniae subsp. pneumoniae strain ATCC 12657 in Propionibacterium jensenii leads to increased increased propionic acid production. The transcription levels of the corresponding enzymes in the engineered strains are 2.85 to 8.07fold higher than those in the wild type. The coexpression of GDH and MDH increases the propionic acid titer from 26.95 g/liter in wild-type to 39.43 g/liter in the engineered strains. Fed-batch culture kinetics of propionic acid production from glycerol, overview
-
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
additional information
immobilization of the enzyme by metal ion-chelated polyethyleneimines greatly broadens the pH adaptability of GDH from strong alkaline into alkalescence
741417