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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Engineering
Engineering on EC 1.1.1.6 - glycerol dehydrogenase
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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
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mutant selected from a DNA shuffling library (Escherichia coli, Salmonella enterica, Klebsiella pneumoniae)
D121A
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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
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mutant selected from a DNA shuffling library (Escherichia coli, Salmonella enterica, Klebsiella pneumoniae)
Q70H/D121A/G193C/E291Q/A310T
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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
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mutant selected from a DNA shuffling library (Escherichia coli, Salmonella enterica, Klebsiella pneumoniae)
Q70H/G193C/E291Q/A310T
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mutant selected from a DNA shuffling library (Escherichia coli, Salmonella enterica, Klebsiella pneumoniae)
D123N
mutation abolishes the oxidative activity. The carboxylate of D123 is the base needed for abstracting the proton to form the alkoxy intermediate that precedes the hydride transfer to the nicotinamide cofactor
L252A
Y142A
mutation reduces the enzyme activity to less than 10% of wild-type activity
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
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site-directed mutagenesis, the mutant shows altered activity with cofactor derivative N6-CM-NAD+ immobilized on Sepharose beads compared to the wild-type enzyme
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K157N
Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589
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site-directed mutagenesis, the mutant shows altered activity with cofactor derivative N6-CM-NAD+ immobilized on Sepharose beads compared to the wild-type enzyme
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V44A
Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589
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site-directed mutagenesis, the mutant shows altered activity with cofactor derivative N6-CM-NAD+ immobilized on Sepharose beads compared to the wild-type enzyme
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V44A/K157G
D121N
mutation lowers the activity of the enzyme with most all the tested substrates relative to the native enzyme
D121N/F245S
mutant acquires D-lactate dehydrogenase activiy, the alteration increases the capacity of the glycerol binding site and facilitated hydrogen bonding between the S245 gamma-O and the C1 carboxylate of pyruvate
F245S
mutant acquires D-lactate dehydrogenase activiy, the alteration increases the capacity of the glycerol binding site and facilitated hydrogen bonding between the S245 gamma-O and the C1 carboxylate of pyruvate
additional information
mutation reduces the enzyme activity to less than 10% of wild-type activity and sculpts the active site to accommodate a productive configuration of 3-monoalkyl glycerols
L252A
the mutation sculpts the active site to accommodate a productive configuration of 3-monoalkyl glycerols. This mutation enhances the kcat 163-fold towards 3-ethoxypropan-1,2-diol, resulting in a specific activity similar to the one found for the wild-type towards glycerol. No activity with 3-phenoxypropane-1,2-diol
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
Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589
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site-directed mutagenesis, the mutant shows altered activity with cofactor derivative N6-CM-NAD+ immobilized on Sepharose beads compared to the wild-type enzyme
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V44A/K157G
Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589
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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
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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 250650 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
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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
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additional information
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bioinspired immobilization of glycerol dehydrogenase by metal ion-chelated polyethyleneimines (PEI) as artificial polypeptides. Nanoparticles with diameters from 250650 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
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additional information
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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
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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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