Information on EC 1.1.1.6 - glycerol dehydrogenase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY hide
1.1.1.6
-
RECOMMENDED NAME
GeneOntology No.
glycerol dehydrogenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
glycerol + NAD+ = glycerone + NADH + H+
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
glycerol degradation II
-
-
glycerol degradation V
-
-
Glycerolipid metabolism
-
-
Metabolic pathways
-
-
Propanoate metabolism
-
-
SYSTEMATIC NAME
IUBMB Comments
glycerol:NAD+ 2-oxidoreductase
Also acts on propane-1,2-diol.
CAS REGISTRY NUMBER
COMMENTARY hide
249285-11-8
-
9028-14-2
this number also refers to EC 1.1.99.22
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
isolated from antarctic soil
-
-
Manually annotated by BRENDA team
strain NT3060
-
-
Manually annotated by BRENDA team
strain E5, E5 mutant D
-
-
Manually annotated by BRENDA team
strain E5, E5 mutant D
-
-
Manually annotated by BRENDA team
strain 1033
-
-
Manually annotated by BRENDA team
strain 2103
-
-
Manually annotated by BRENDA team
strain NBRC12010
-
-
Manually annotated by BRENDA team
strain P14
-
-
Manually annotated by BRENDA team
strain ECFS
-
-
Manually annotated by BRENDA team
DSM 2343
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
strain H 112
-
-
Manually annotated by BRENDA team
strain H 112
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
strain 972h-
-
-
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
strain TM0423
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
-
the enzyme belongs to the medium-chain dehydrogenase/reductase, MDRase, superfamily
metabolism
-
in Escherichia coli, the enzyme catalyzes the first step in fermentative glycerol metabolism to produce dihydroxyacetone, biochemical transformation pathway of glycerol, overview
physiological function
-
GroDHase is mainly involved in Gro utilization as a carbon and energy source
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(2R,3R)-2,3-butanediol + NAD+
(3R)-acetoin + NADH
show the reaction diagram
(2R,3R)-2,3-butanediol + NAD+
? + NADH
show the reaction diagram
(R)-1,2-propanediol + NAD+
? + NADH
show the reaction diagram
1,2,3-butanetriol + NAD+
1,3-dihydroxybutane-2-one + NADH
show the reaction diagram
-
-
-
?
1,2-butanediol + NAD+
1-hydroxybutane-2-one + NADH
show the reaction diagram
-
-
-
r
1,2-propanediol + NAD+
hydroxyacetone + NADH
show the reaction diagram
1,3-butanediol + NAD+
4-hydroxy-2-butanone + NADH + H+
show the reaction diagram
1,3-butanediol + NAD+
?
show the reaction diagram
-
relative activity is 6.5% compared to oxidation of glycerol
-
-
?
1,3-dichloro-2-propanol + NAD+
1,3-dichloro-2-propanone + NADH
show the reaction diagram
1,3-propanediol + NAD+
?
show the reaction diagram
1,4-butanediol + NAD+
?
show the reaction diagram
1-chloro-2,3-propanediol + NAD+
?
show the reaction diagram
1-phenylethan-1,2-diol + NAD+
? + NADH
show the reaction diagram
-
-
-
-
?
2,3-butanediol + NAD+
3-hydroxybutane-2-one + NADH
show the reaction diagram
3-amino-1,2-propanediol + NAD+
?
show the reaction diagram
-
104% of the activity with glycerol
-
-
?
3-bromo-1,2-propanediol + NAD+
?
show the reaction diagram
-
109% of the activity with glycerol
-
-
?
3-chloro-1,2-propanediol + NAD+
?
show the reaction diagram
-
130% of the activity with glycerol
-
-
?
3-hydroxypropionaldehyde + NADH
propan-1,3-diol + NAD+
show the reaction diagram
-
-
-
-
?
3-mercapto-1,2-propanediol + NAD+
?
show the reaction diagram
-
155% of the activity with glycerol
-
-
?
acetaldehyde + NADH + H+
ethanol + NAD+
show the reaction diagram
acetoin + NADH + H+
2,3-butanediol + NAD+
show the reaction diagram
beta-glycerophosphate + NAD+
?
show the reaction diagram
-
relative activity is 2% compared to oxidation of glycerol
-
-
?
butane-1,3-diol + NAD+
? + NADH
show the reaction diagram
-
-
-
-
?
diglycerol + NAD+
?
show the reaction diagram
-
relative activity is 21% compared to oxidation of glycerol
-
-
?
DL-alpha-glycerophosphate + NAD+
?
show the reaction diagram
DL-glyceraldehyde + NAD+
3-hydroxypyruvaldehyde + NADH
show the reaction diagram
DL-glyceraldehyde + NADH
glycerol + NAD+
show the reaction diagram
erythrite + NAD+
?
show the reaction diagram
-
-
-
-
?
ethanediol + NAD+
glycolaldehyde + NADH
show the reaction diagram
ethanol + NAD+
acetaldehyde + NADH
show the reaction diagram
-
relative activity is 1% compared to oxidation of glycerol
-
-
?
ethylene glycol + NAD+
?
show the reaction diagram
glycerol + NAD+
D-glyceraldehyde + NADH
show the reaction diagram
glycerol + NAD+
dihydroxyacetone + NADH
show the reaction diagram
glycerol + NAD+
dihydroxyacetone + NADH + H+
show the reaction diagram
glycerol + NAD+
glycerone + NADH
show the reaction diagram
-
-
-
-
?
glycerol + NAD+
glycerone + NADH + H+
show the reaction diagram
glycerol + NADP+
glyceraldehyde + NADPH + H+
show the reaction diagram
glycerol-alpha-monochlorohydrin + NAD+
?
show the reaction diagram
glycerol-alpha-monomethyl ether + NAD+
?
show the reaction diagram
glycerone + NADH + H+
glycerol + NAD+
show the reaction diagram
hydroxy-2-propanone + NADH
propylene glycol + NAD+
show the reaction diagram
-
relative activity is 27% compared to oxidation of glycerol
-
-
?
i-inositol + NAD+
?
show the reaction diagram
-
relative activity is 18% compared to oxidation of glycerol
-
-
?
isopropanol + NAD+
acetone + NADH
show the reaction diagram
-
relative activity is 17% compared to oxidation of glycerol
-
-
?
meso-2,3-butanediol + NAD+
(3S)-acetoin + NADH
show the reaction diagram
methylglyoxal + NADH
lactaldehyde + NAD+
show the reaction diagram
N-butyraldehyde + NADH
1-butanol + NAD+
show the reaction diagram
-
-
-
-
?
propane-1,2-diol + NAD+
propane-1-ol-2-one + NADH
show the reaction diagram
-
-
-
-
?
propionaldehyde + NADH
1-propanol + NAD+
show the reaction diagram
-
-
-
-
?
R-1-amino-2-propanol + NAD+
?
show the reaction diagram
-
33% of the activity with glycerol
-
-
?
S-1-amino-2-propanol + NAD+
?
show the reaction diagram
-
9% of the activity with glycerol
-
-
?
sorbitol + NAD+
?
show the reaction diagram
-
relative activity is 3% compared to oxidation of glycerol
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
glycerol + NAD+
D-glyceraldehyde + NADH
show the reaction diagram
glycerol + NAD+
dihydroxyacetone + NADH
show the reaction diagram
glycerol + NAD+
glycerone + NADH + H+
show the reaction diagram
-
-
-
-
r
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
-
1 mM, stimulates 64.5% compared to 1 mM Mn2+
Fe2+
-
1 mM, stimulates 26.3% compared to 1 mM Mn2+
Na+
-
oxidation and reduction slightly increased
Tl+
-
activates
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
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
1-ethyl-3(3-dimethylaminopropyl)carbodiimide
-
-
2,2'-bipyridyl
2,2'dipyridyl
-
1 mM, complete inhibition
2,4,6-Trinitrobenzene sulfonate
-
-
2-amino-2-(hydroxymethyl)-1,3-propanediol
-
strong inhibition, IC50 2 mM
2-mercaptoethanol
3,4-dimercaptotoluol
-
-
8-hydroxyquinoline
-
-
8-Quinolinol
acetone
-
inactivation, enzyme regains activity after removal of ketone
ADP
-
3 mM, 10% inhibition
AMP
-
3 mM, 13% inhibition
Anhitol 24B
-
-
ATP
-
3 mM, 6% inhibition
catechol
-
i.e. 1,2-butanediol, inactivation, enzyme regains activity after removal of alcohol
Cd2+
-
strongly inhibitory
Cetylpyridinium chloride
-
strong inhibition at low concentration
Cetyltrimethylammonium bromide
-
strong inhibition at low concentration
CuCl2
-
strong
D-xylose
-
-
diacetyl
-
inactivation, enzyme regains activity after removal of ketone
diethyldithiocarbamate
-
slight inhibition, 2 mM, 10 mM
dihydroxyacetone
dihydroxyacetone phosphate
-
-
dimethylformamide
-
inactivation
Dimethylsulfoxide
-
inactivation
dioxane
-
inactivation, enzyme regains activity after removal of ketone
diphosphate
-
-
dithioerythritol
-
10 mM
dithiothreitol
ethanol
-
10% v/v: 25-75% loss of activity, depending on substrate, enzyme regains activity after removal of alcohol
ethylene glycol
-
strong inhibition, IC50 4 mM
FeCl3
-
strong
glycerol 3-phosphate
-
-
HgCl2
-
strong
Hydroxyacetone
-
-
iodoacetamide
-
strong inhibition, 10 mM
iodoacetate
-
-
isobutanol
-
5% v/v: 0-50% loss of activity, depending on substrate, enzyme regains activity after removal of alcohol
K+
-
reduction of dihydroxyacetone
L-cysteine
Li+
-
competitive, forward reaction
meso-erythritol
-
-
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
methylene blue
-
enzyme activity is decreased by photooxidation
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-ethylmaleimide
n-Propanol
-
5% v/v: 25-60% loss of activity, depending on substrate, enzyme regains activity after removal of alcohol
Na+
-
competitive, forward reaction
o-phthalaldehyde
-
inactivation due to intramolecular thioisoindole formation, glycerol partially protects
p-chloromercuribenzoate
p-hydroxymercuribenzoate
-
0.1 mM, strong
Phenanthroline
-
1 mM, complete inhibition
pyridin-2,6-dicarboxylic acid
-
-
pyridoxyl-5'-phosphate
-
inactivation, NAD+ or NADH protect
Sodium dodecyl sulfate
-
-
sodium tetraborate
-
1 mM, 53% inhibition
Sucrose
-
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
-
at 1.85 mM 135% of the activity without activator
2-mercaptoethanol
-
1 mM, slight activation
8-Quinolinol
-
1 mM, slight activation
ammonium sulfate
-
about 100% activation at 10 mM
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
dithioerythritol
-
1 mM, slight activation
iodoacetamide
-
at 1 mM 140% of the activity without activator, at 10 mM 220% of the activity without activator
K+
-
activates NADH production
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
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
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.06 - 0.202
1,2-propanediol
11.9 - 77.8
1,3-butanediol
0.0238
2,3-Butanediol
-
-
180
3-amino-1,2-propanediol
-
pH 8.8, 25C
6.1
3-bromo-1,2-propanediol
-
pH 8.8, 25C
6
3-Chloro-1,2-propanediol
-
pH 8.8, 25C
4
3-mercapto-1,2-propanediol
-
pH 8.8, 25C
0.06 - 4.87
dihydroxyacetone
10.9
glycero
-
-
-
0.5 - 118
glycerol
0.15 - 0.24
Glycerone
0.0165 - 4.7
NAD+
0.014 - 0.12
NADH
4.4
R-1-amino-2-propanol
-
pH 8.8, 25C
500
S-1-amino-2-propanol
-
pH 8.8, 25C
additional information
additional information
-
kinetic study with different effectors, overview
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.6 - 87.2
1,3-butanediol
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.09 - 1.26
1,3-butanediol
105 - 500
NAD+
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
11.1
dihydroxyacetone
-
-
11.6
Hydroxyacetone
-
-
1.09
NAD+
-
25C
0.025
NADH
-
25C
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2
2-amino-2-(hydroxymethyl)-1,3-propanediol
Pichia membranifaciens
-
strong inhibition, IC50 2 mM
0.3
2-mercaptoethanol
Pichia membranifaciens
-
strong inhibition, IC50 0.3 mM
4
ethylene glycol
Pichia membranifaciens
-
strong inhibition, IC50 4 mM
0.2
N-ethylmaleimide
Pichia membranifaciens
-
rapid inactivation, IC50: 0.2 mM
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.01
wild type, crude cell extract, pH not specified in the publication, temperature not specified in the publication
0.033
-
anaerobic growth conditions, cells permeabilized with chloroform
0.049
overexpressing cells, crude cell extract, pH not specified in the publication, temperature not specified in the publication
1.05
-
cell free extract
1.26
-
; pH 8.2, 25C
3.7
-
pH 9.5, 30C
3.9
-
pH 9.5, 30C
4.7
cell free extract, wild type; wild type, crude extract, pH not specified in the publication, temperature not specified in the publication
4.8
-
wild type protein, pH 9.5, 30C
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, 30C
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, 30C
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, 30C
13.2
-
mutant protein Q70H/G193C/E291Q/A310T, pH 9.5, 30C
90.7
-
mutant protein D121A, pH 9.5, 30C
107
-
commercial preparation
126.6
-
mutant protein Q70H/D121A/G193C/E291Q/A310T, pH 9.5, 30C
220
cell free extract, recombinant strain (over-expression of gycerol dehydrogenase); recombinant strain (overexpression), crude extract, pH not specified in the publication, temperature not specified in the publication
additional information
-
assay development for NADH production by recombinant enzyme in reverse micelles, micelle size optimization, overview
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5
-
reduction of hydroxyacetone
5 - 6
-
reduction of dihydroxyacetone
7.2
-
oxidation of glycerol, wild-type enzyme
7.5
-
oxidation of glycerol, mutant D
7.5 - 8.5
-
reduction of dihydroxyacetone, phosphate buffer
8 - 8.5
-
oxidation of 1,2-propanediol
8.3
-
reduction of dihydroxyacetone, mutant D
8.6
-
reduction of dihydroxyacetone, wild-type enzyme
9.5 - 10
-
-
9.5
-
in an aqueous buffer system
9.5 - 10.5
-
oxidation of glycerol, diphosphate buffer
10 - 10.5
-
-
10.5 - 11
-
NADH production
10.5
-
in reverse micelles
11
-
glycerol oxidation reaction
11 - 12
-
oxidation of glycerol
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
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
6.5 - 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
-
pH 7.0: about 60% of maximal activity, pH 10.0: about 85% of maximal activity, oxidation of glycerol
7.5 - 12
-
glycerol oxidation reaction, activity range, profile overview
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
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
assay at, in reverse micelles
65
-
oxidation of propanediol
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6
-
43% residual activity
20 - 80
-
activity range, profile overview
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
72000
-
gel filtration
76000 - 80000
-
gel filtration, PAGE under nondenaturing conditions
132000
-
gel filtration
156000 - 160000
-
density gradient centrifugation, gel filtration
180000
-
gel filtration
181000
-
gel filtration
320000
-
recombinant His-tagged enzyme, gel filtration
324000
-
gel filtration
336000 - 390000
400000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
octamer
tetramer
additional information
-
GST-CglD fusion protein: 67000Da, SDS-PAGE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystal obtained by hanging-drop vaour-diffusion method, S305C mutant
-
preliminary X-ray characterization; sitting drop vapor-diffusion method
in presence of glycerol
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4
-
25C, 10 min, 30% loss of activity
636294
5.5 - 10
-
30C, 60 min, stable
636289
10
-
25C, 10 min, 40% loss of activity
636294
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
-
60 min, stable in the pH range pH 5.5-10
60
-
10 min, inactivation
70
-
30 min stable
75
-
10 min stable
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-15C, with 5% culture filtrate or 5% boiled crude cell extract, 10% Ficoll, pH 7.5, stable for 1 month
-
-70C, long term storage
-
0-5C, 50 to 55% loss of original activity within 48 h
-
4C, in 2 M (NH4)2SO4, 1 M glycerol, several months
-
frozen, retains about 42% of initial activity for 2 months
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
GST-tagged protein
-
immobilized metal ion affinity chromatography (Co2+)
immobilized metal ion affinity chromatography (Ni2+); purity estimated from SDS-PAGE: 95%
purified by Ni-affinity chromatography; recombinant His-tagged enzyme from strain BL21(DE3) by nickel affinity chromatography
-
recombinant His-tagged enzyme from Escherichia coli strain BL21 (DE3) by immobilized metal affinity chromatography or by heat shock treatment, both resulting in about the same protein purity of over 90%
-
recombinant mutant enzyme S305C
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
CglD, GST-tagged protein, expressed in E. coli BL21 (DE3)
-
expressed in E. coli
-
expressed in Klebsiella pneumoniae KG1
expressed in Klebsiella pneumoniae KG1; overexpressed in Klebsiella pneumoniae KG1
expression as His-tag fusion protein in Escherichia coli BL21 (DE3) pLysS; gene gld, expression of His-tagged enzyme in strain BL21(DE3)
-
expression in Saccharomyces cerevisiae
-
gene gldA from Escherichia coli strain JM109, expression of His-tagged enzyme in Escherichia coli strain BL21 (DE3), subcloning in Escherichia coli TOP10 cells
-
His-tag, expressed in E. coli JM109; His-tagged version
-
His-tagged version expressed in Escherichia coli BL21 STAR (DE3); N-terminal His-tag, expressed in E. coli BL21 STAR (DE3)
His-tagged version expressed in Escherichia coli BL21(DE3)
overexpressed in Schizosaccharomyces pombe
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
induced by alcohols and aliphatic or aromatic hydrocarbons when glycerol used as the only substrate; induced by n-decanol (as sole carbon source)
induced by glucose starvation, essential for glycerol assimilation
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
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
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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)
S305C
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S305C mutant used for crystallisation
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
biotechnology
-
production of 1,2-propanediol in yeast
brewing
molecular biology
synthesis
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