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
1.1.1.6
-
RECOMMENDED NAME
GeneOntology No.
glycerol dehydrogenase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
glycerol + NAD+ = glycerone + NADH + H+
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
glycerol degradation II
-
glycerol degradation V
-
Glycerolipid metabolism
-
Metabolic pathways
-
SYSTEMATIC NAME
IUBMB Comments
glycerol:NAD+ 2-oxidoreductase
Also acts on propane-1,2-diol.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
CglD
-
CglD is a virulence factor and has glycerol dehydrogenase activity
dehydrogenase, glycerol
-
-
-
-
GDH2
-
-
-
-
GLD
Escherichia coli JM109
-
-
-
GLDH
-
-
-
-
glycerin dehydrogenase
-
-
-
-
glycerol dehydrogenase
-
-
glycerol dehydrogenase
-
-
glycerol dehydrogenase
Enterobacter aerogenes NBRC12010
-
-
-
glycerol dehydrogenase
Escherichia coli JM109
-
;
-
glycerol dehydrogenase
-
-
glycerol dehydrogenase
-
-
glycerol dehydrogenase
A0MLR7
-
glycerol dehydrogenase
Klebsiella pneumoniae KG1
-, A0MLR7
-
-
glycerol dehydrogenase
Klebsiella pneumoniae MGH78578
-
-
-
glycerol dehydrogenase
-
-
glycerol dehydrogenase
Mucor circinelloides YR-1
-
-
-
glycerol dehydrogenase
-
-
glycerol dehydrogenase
Salmonella enterica ATCC 9150
-
-
-
glycerol dehydrogenase
-
type III polyol dehydrogenase family
glycerol dehydrogenase
O13702
-
glycerol dehydrogenase
Schizosaccharomyces pombe ARC039
O13702
-
-
glycerol NAD 2-oxidoreductase
-
-
-
-
glycerol:NAD+ 2-oxidoreductase
-
-
-
-
Gro dehydrogenase
-
-
GroDHase
-
-
NAD-linked glycerol dehydrogenase
-
-
-
-
NAD-specific glycerol dehydrogenase
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
249285-11-8
-
9028-14-2
this number also refers to EC 1.1.99.22
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
isolated from antarctic soil
-
-
Manually annotated by BRENDA team
strain E5, E5 mutant D
-
-
Manually annotated by BRENDA team
Clostridium butyricum E5
strain E5, E5 mutant D
-
-
Manually annotated by BRENDA team
Clostridium difficile
-
-
-
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
Enterobacter aerogenes 1033
strain 1033
-
-
Manually annotated by BRENDA team
Enterobacter aerogenes 2103
strain 2103
-
-
Manually annotated by BRENDA team
Enterobacter aerogenes NBRC12010
strain NBRC12010
-
-
Manually annotated by BRENDA team
Enterobacter aerogenes P14
strain P14
-
-
Manually annotated by BRENDA team
; strain JM109
-
-
Manually annotated by BRENDA team
; strain JM109, gene gld
-
-
Manually annotated by BRENDA team
gene gldA
-
-
Manually annotated by BRENDA team
strain ECFS
-
-
Manually annotated by BRENDA team
Escherichia coli ECFS
strain ECFS
-
-
Manually annotated by BRENDA team
Escherichia coli JM109
strain JM109
-
-
Manually annotated by BRENDA team
Escherichia coli JM109
strain JM109, gene gld
-
-
Manually annotated by BRENDA team
strain MG1655
-
-
Manually annotated by BRENDA team
strain KG1
-
-
Manually annotated by BRENDA team
strain KG1
UniProt
Manually annotated by BRENDA team
Klebsiella pneumoniae KG1
strain KG1
-
-
Manually annotated by BRENDA team
Klebsiella pneumoniae KG1
strain KG1
UniProt
Manually annotated by BRENDA team
Klebsiella pneumoniae MGH78578
-
-
-
Manually annotated by BRENDA team
Mucor circinelloides YR-1
-
-
-
Manually annotated by BRENDA team
strain DL-1
-
-
Manually annotated by BRENDA team
strain Dl-1, induced by growth on methanol or glycerol
-
-
Manually annotated by BRENDA team
strain H 112
-
-
Manually annotated by BRENDA team
Pichia membranifaciens H 112
strain H 112
-
-
Manually annotated by BRENDA team
serovar typhimurium
-
-
Manually annotated by BRENDA team
Salmonella enterica ATCC 9150
-
-
-
Manually annotated by BRENDA team
Schizosaccharomyces pombe ARC039
-
UniProt
Manually annotated by BRENDA team
strain TM0423
-
-
Manually annotated by BRENDA team
Thermotoga maritima TM0423
strain TM0423
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
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 ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(2R,3R)-2,3-butanediol + NAD+
(3R)-acetoin + NADH
show the reaction diagram
-
-
more than 99% enantiomeric excess of R-product
-
r
(2R,3R)-2,3-butanediol + NAD+
? + NADH
show the reaction diagram
-
better substrate than glycerol
-
-
?
(R)-1,2-propanediol + NAD+
? + NADH
show the reaction diagram
-
better substrate than glycerol
-
-
?
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
-
-
-
-
-
1,2-propanediol + NAD+
hydroxyacetone + NADH
show the reaction diagram
-
-
-
-
-
1,2-propanediol + NAD+
hydroxyacetone + NADH
show the reaction diagram
-
-
-
r
1,2-propanediol + NAD+
hydroxyacetone + NADH
show the reaction diagram
-
-
-
-
-
1,2-propanediol + NAD+
hydroxyacetone + NADH
show the reaction diagram
-
-
-
-
-
1,2-propanediol + NAD+
hydroxyacetone + NADH
show the reaction diagram
-
-
-
r
1,2-propanediol + NAD+
hydroxyacetone + NADH
show the reaction diagram
-
105% of the activity with glycerol
-
-
-
1,2-propanediol + NAD+
hydroxyacetone + NADH
show the reaction diagram
-
relative activity is 116% compared to oxidation of glycerol
-
-
-
1,2-propanediol + NAD+
hydroxyacetone + NADH
show the reaction diagram
-
as active as glycerol
-
-
-
1,2-propanediol + NAD+
hydroxyacetone + NADH
show the reaction diagram
-
1,2-propanediol represses the global activator HilA that induces an invasive phenotype and repression of HilA could be weakened by glycerol dehydrogenase activity
-
-
?
1,2-propanediol + NAD+
hydroxyacetone + NADH
show the reaction diagram
Enterobacter aerogenes P14
-
-
-
-
-
1,2-propanediol + NAD+
hydroxyacetone + NADH
show the reaction diagram
-
-
-
r
1,2-propanediol + NAD+
hydroxyacetone + NADH
show the reaction diagram
-
relative activity is 116% compared to oxidation of glycerol
-
-
-
1,2-propanediol + NAD+
hydroxyacetone + NADH
show the reaction diagram
-
-
-
-
-
1,2-propanediol + NAD+
hydroxyacetone + NADH
show the reaction diagram
Pichia membranifaciens H 112
-
-
-
-
-
1,3-butanediol + NAD+
?
show the reaction diagram
-
relative activity is 6.5% compared to oxidation of glycerol
-
-
?
1,3-butanediol + NAD+
4-hydroxy-2-butanone + NADH + H+
show the reaction diagram
Escherichia coli, Klebsiella pneumoniae, Salmonella enterica, Salmonella enterica ATCC 9150, Klebsiella pneumoniae MGH78578
-
-
-
-
?
1,3-dichloro-2-propanol + NAD+
1,3-dichloro-2-propanone + NADH
show the reaction diagram
Enterobacter aerogenes, Enterobacter aerogenes P14
-
-
-
-
?
1,3-propanediol + NAD+
?
show the reaction diagram
-
-
-
-
?
1,3-propanediol + NAD+
?
show the reaction diagram
-
relative rate of oxidation is 37% compared to oxidation of glycerol
-
-
?
1,3-propanediol + NAD+
?
show the reaction diagram
-
relative rate of oxidation is 18% compared to oxidation of glycerol
-
-
?
1,3-propanediol + NAD+
?
show the reaction diagram
Clostridium butyricum E5
-
-
-
-
?
1,4-butanediol + NAD+
?
show the reaction diagram
-
relative activity 17% compared to oxidation of glycerol
-
-
?
1,4-butanediol + NAD+
?
show the reaction diagram
-
relative activity is 0.3% compared to oxidation of glycerol
-
-
?
1-chloro-2,3-propanediol + NAD+
?
show the reaction diagram
Enterobacter aerogenes, Enterobacter aerogenes P14
-
-
-
-
?
1-phenylethan-1,2-diol + NAD+
? + NADH
show the reaction diagram
-
-
-
-
?
2,3-butanediol + NAD+
3-hydroxybutane-2-one + NADH
show the reaction diagram
-
-
-
r
2,3-butanediol + NAD+
3-hydroxybutane-2-one + NADH
show the reaction diagram
-
-
-
-
-
2,3-butanediol + NAD+
3-hydroxybutane-2-one + NADH
show the reaction diagram
-
-
-
-
-
2,3-butanediol + NAD+
3-hydroxybutane-2-one + NADH
show the reaction diagram
-
-
-
r
2,3-butanediol + NAD+
3-hydroxybutane-2-one + NADH
show the reaction diagram
-
as active as glycerol
-
-
-
2,3-butanediol + NAD+
3-hydroxybutane-2-one + NADH
show the reaction diagram
-
-
-
r
2,3-butanediol + NAD+
3-hydroxybutane-2-one + NADH
show the reaction diagram
-
-
-
-
-
2,3-butanediol + NAD+
3-hydroxybutane-2-one + NADH
show the reaction diagram
Clostridium butyricum E5
-
-
-
-
-
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
Clostridium butyricum, Clostridium butyricum E5
-
-
-
-
?
acetoin + NADH + H+
2,3-butanediol + NAD+
show the reaction diagram
-
-
-
-
r
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
-
relative activity 11%compared to oxidation of glycerol
-
-
?
DL-alpha-glycerophosphate + NAD+
?
show the reaction diagram
-
oxidation at 16% compared to oxidation of glycerol
-
-
?
DL-glyceraldehyde + NAD+
3-hydroxypyruvaldehyde + NADH
show the reaction diagram
-
-
-
?
DL-glyceraldehyde + NAD+
3-hydroxypyruvaldehyde + NADH
show the reaction diagram
-
-
-
-
?
DL-glyceraldehyde + NAD+
3-hydroxypyruvaldehyde + NADH
show the reaction diagram
-
-
-
?
DL-glyceraldehyde + NAD+
3-hydroxypyruvaldehyde + NADH
show the reaction diagram
-
relative rate of reduction is 14%compared to reduction of dihydroxyacetone
-
-
?
DL-glyceraldehyde + NAD+
3-hydroxypyruvaldehyde + NADH
show the reaction diagram
Pichia membranifaciens H 112
-
-
-
-
?
DL-glyceraldehyde + NADH
glycerol + NAD+
show the reaction diagram
Clostridium butyricum, Clostridium butyricum E5
-
-
-
-
?
erythrite + NAD+
?
show the reaction diagram
-
-
-
-
?
ethanediol + NAD+
glycolaldehyde + NADH
show the reaction diagram
-
-
-
-
ethanediol + NAD+
glycolaldehyde + NADH
show the reaction diagram
-
-
reduction at concentration of 50 mM
r
ethanol + NAD+
acetaldehyde + NADH
show the reaction diagram
-
relative activity is 1% compared to oxidation of glycerol
-
-
?
ethylene glycol + NAD+
?
show the reaction diagram
-
-
-
-
?
ethylene glycol + NAD+
?
show the reaction diagram
-
relative activity is 20% compared to oxidation of glycerol
-
-
?
glycerol + NAD+
dihydroxyacetone + NADH
show the reaction diagram
-
-
-
-
-
glycerol + NAD+
dihydroxyacetone + NADH
show the reaction diagram
-
-
-
-
-
glycerol + NAD+
dihydroxyacetone + NADH
show the reaction diagram
-
-
-
-
?
glycerol + NAD+
dihydroxyacetone + NADH
show the reaction diagram
-
-
-
-
-
glycerol + NAD+
dihydroxyacetone + NADH
show the reaction diagram
-
-
-
r
glycerol + NAD+
dihydroxyacetone + NADH
show the reaction diagram
-
-
-
-
-
glycerol + NAD+
dihydroxyacetone + NADH
show the reaction diagram
-
-
-
-
glycerol + NAD+
dihydroxyacetone + NADH
show the reaction diagram
-
-
-
-
-
glycerol + NAD+
dihydroxyacetone + NADH
show the reaction diagram
-
-
-
-
?
glycerol + NAD+
dihydroxyacetone + NADH
show the reaction diagram
-
-
-
r
glycerol + NAD+
dihydroxyacetone + NADH
show the reaction diagram
-
-
-
r
glycerol + NAD+
dihydroxyacetone + NADH
show the reaction diagram
-
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
-
-
?
glycerol + NAD+
dihydroxyacetone + NADH
show the reaction diagram
-
the reaction is performed in reverse micelles harboring glycerol and NAD+ in a solution of isooctane containing 250 mM diocytlsulfosuccinate
-
-
?
glycerol + NAD+
dihydroxyacetone + NADH
show the reaction diagram
Enterobacter aerogenes P14
-
-
-
-
-
glycerol + NAD+
dihydroxyacetone + NADH
show the reaction diagram
-
-
-
-
glycerol + NAD+
dihydroxyacetone + NADH
show the reaction diagram
-
-
-
-
-
glycerol + NAD+
dihydroxyacetone + NADH
show the reaction diagram
-
-
-
r
glycerol + NAD+
dihydroxyacetone + NADH
show the reaction diagram
-
-
-
-
-
glycerol + NAD+
dihydroxyacetone + NADH
show the reaction diagram
Pichia membranifaciens H 112
-
-
-
-
-
glycerol + NAD+
dihydroxyacetone + NADH
show the reaction diagram
-
-
-
-
-
glycerol + NAD+
dihydroxyacetone + NADH
show the reaction diagram
Escherichia coli JM109
-
the reaction is performed in reverse micelles harboring glycerol and NAD+ in a solution of isooctane containing 250 mM diocytlsulfosuccinate
-
-
?
glycerol + NAD+
dihydroxyacetone + NADH
show the reaction diagram
Enterobacter aerogenes 1033
-
-
-
-
-
glycerol + NAD+
glycerone + NADH + H+
show the reaction diagram
-
-
-
-
?
glycerol + NAD+
glycerone + NADH + H+
show the reaction diagram
-
-
-
-
r
glycerol + NAD+
glycerone + NADH + H+
show the reaction diagram
-
-
-
-
r
glycerol + NAD+
glycerone + NADH + H+
show the reaction diagram
O13702, -
no activity detected with NADP+
-
-
?
glycerol + NAD+
glycerone + NADH + H+
show the reaction diagram
Escherichia coli JM109
-
-
-
-
?
glycerol + NAD+
glycerone + NADH + H+
show the reaction diagram
Schizosaccharomyces pombe ARC039
O13702
no activity detected with NADP+
-
-
?
glycerol + NAD+
glycerone + NADH
show the reaction diagram
-
-
-
-
?
glycerol + NAD+
D-glyceraldehyde + NADH
show the reaction diagram
Escherichia coli, Escherichia coli JM109
-
-
-
-
r
glycerol + NAD+
dihydroxyacetone + NADH + H+
show the reaction diagram
-
-
-
-
?
glycerol + NAD+
dihydroxyacetone + NADH + H+
show the reaction diagram
A0MLR7, -
-
-
-
?
glycerol + NAD+
dihydroxyacetone + NADH + H+
show the reaction diagram
-
-
-
-
?
glycerol + NAD+
dihydroxyacetone + NADH + H+
show the reaction diagram
-
-
-
-
?
glycerol + NAD+
dihydroxyacetone + NADH + H+
show the reaction diagram
A0MLR7
-
-
-
?
glycerol + NAD+
dihydroxyacetone + NADH + H+
show the reaction diagram
Klebsiella pneumoniae KG1
-
-
-
-
?
glycerol + NAD+
dihydroxyacetone + NADH + H+
show the reaction diagram
Klebsiella pneumoniae KG1
A0MLR7
-
-
-
?
glycerol + NAD+
dihydroxyacetone + NADH + H+
show the reaction diagram
Escherichia coli JM109
-
-
-
-
?
glycerol + NADP+
glyceraldehyde + NADPH + H+
show the reaction diagram
-
-, 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+
show the reaction diagram
Mucor circinelloides YR-1
-
-, 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+
?
show the reaction diagram
-
relative rate of oxidation is 26% compared to oxidation of glycerol
-
-
?
glycerol-alpha-monochlorohydrin + NAD+
?
show the reaction diagram
-
relative rate of oxidation is 71% compared to oxidation of glycerol
-
-
?
glycerol-alpha-monomethyl ether + NAD+
?
show the reaction diagram
Enterobacter aerogenes, Enterobacter aerogenes P14
-
-
-
-
?
glycerone + NADH + H+
glycerol + NAD+
show the reaction diagram
-
-
-
-
r
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
-
-
more than 99% enantiomeric excess of S-product
-
-
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
-
-
?
methylglyoxal + NADH
lactaldehyde + NAD+
show the reaction diagram
-
relative rate of reduction is 56% compared to reduction of dihydroxyacetone
-
-
?
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
?
-
-
ability of the enzyme to use glycerol from biodiesel waste as substrate, overview
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
glycerol + NAD+
dihydroxyacetone + NADH
show the reaction diagram
-
-
-
-
-
glycerol + NAD+
dihydroxyacetone + NADH
show the reaction diagram
-
-
-
-
-
glycerol + NAD+
dihydroxyacetone + NADH
show the reaction diagram
-
-
-
-
-
glycerol + NAD+
dihydroxyacetone + NADH
show the reaction diagram
-
-
-
-
-
glycerol + NAD+
dihydroxyacetone + NADH
show the reaction diagram
-
-
-
-
-
glycerol + NAD+
glycerone + NADH + H+
show the reaction diagram
-
-
-
-
r
glycerol + NAD+
D-glyceraldehyde + NADH
show the reaction diagram
-
-
-
-
r
glycerol + NAD+
dihydroxyacetone + NADH
show the reaction diagram
Enterobacter aerogenes P14
-
-
-
-
-
glycerol + NAD+
dihydroxyacetone + NADH
show the reaction diagram
-
-
-
-
-
glycerol + NAD+
dihydroxyacetone + NADH
show the reaction diagram
Pichia membranifaciens H 112
-
-
-
-
-
glycerol + NAD+
dihydroxyacetone + NADH
show the reaction diagram
-
-
-
-
-
glycerol + NAD+
D-glyceraldehyde + NADH
show the reaction diagram
Escherichia coli JM109
-
-
-
-
r
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ca2+
-
1 mM, stimulates 64.5% compared to 1 mM Mn2+
Fe2+
-
1 mM, stimulates 26.3% compared to 1 mM Mn2+
K+
-
oxidation of glycerol os greatly increased
K+
-
required for enzymatic activity and glycerol binding
K+
-
activates, less effective than NH4+
Li+
-
oxidation slightly increased
Mn2+
-
increases activity significantly
Mn2+
-
1 mM, activates
Na+
-
oxidation and reduction slightly increased
NH4+
-
80% activation at 10 mM
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
Rb+
-
oxidation greatly increased
Rb+
-
activates
Tl+
-
activates
Zn2+
-
increases activity
Zn2+
-
1.6 mol Zn2+ bound per subunit
Zn2+
-
enzyme is dependent on Zn2+
Zn2+
-
one ion per monomer, crystallization data
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1,10-phenanthroline
-
-
1,10-phenanthroline
-
1 mM
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'-Bipyridyl
-
powerful inhibition
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
-
-
2-mercaptoethanol
-
strong inhibition, IC50 0.3 mM
2-mercaptoethanol
-
strongly inhibitory at 100 mM, but slight activation in lower concentration, 1 mM
3,4-dimercaptotoluol
-
-
8-hydroxyquinoline
-
-
8-Quinolinol
-
1 mM, 10 mM
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
Cu2+
-
strong inhibition
Diacetyl
-
inactivation, enzyme regains activity after removal of ketone
diethyldithiocarbamate
-
slight inhibition, 2 mM, 10 mM
Dihydroxyacetone
-
noncompatible inhibitor, at saturated level of glycerol
Dihydroxyacetone
-
above 0.5 mM
dihydroxyacetone phosphate
-
-
Dimethylformamide
-
inactivation
Dimethylsulfoxide
-
inactivation
Dioxane
-
inactivation, enzyme regains activity after removal of ketone
dithioerythritol
-
10 mM
dithiothreitol
-
slight inhibition
EDTA
-
slight inhibition, 10 mM
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
glycerol 3-phosphate
-
-
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
-
slight inhibition
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
-
rapid inactivation, IC50: 0.2 mM
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
NADH
-
product inhibition , competitive with NAD+
NADH
-
competitive inhibitor versus NAD+ in direction of glycerol oxidation, noncompetitive inhibitor versus glycerol
NADP+
-
inhibits oxidation of glycerol
o-phthalaldehyde
-
inactivation due to intramolecular thioisoindole formation, glycerol partially protects
p-chloromercuribenzoate
-
-
p-chloromercuribenzoate
-
95% inhibition at 0.01 mM
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
Zn2+
-
strong inhibitory
Zn2+
-
50% inhibition at 0.021 mM
Zn2+
-
over 90% inhibition at 0.01 mM
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
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
NH4+
-
oxidation and reduction greatly increased
NH4+
-
activates NADH production
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]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.06
-
1,2-Propanediol
-
pH 8.8, 25C
0.202
-
1,2-Propanediol
-
-
11.9
-
1,3-butanediol
-
mutant protein Q70H/G193C/E291Q/A310T, pH 9.5, 30C
16.2
-
1,3-butanediol
-
wild type protein, pH 9.5, 30C
20.9
-
1,3-butanediol
-
pH 9.5, 30C
29.2
-
1,3-butanediol
-
pH 9.5, 30C
49.9
-
1,3-butanediol
-
mutant protein D121A, pH 9.5, 30C
77.8
-
1,3-butanediol
-
mutant protein Q70H/D121A/G193C/E291Q/A310T, pH 9.5, 30C
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
-
Dihydroxyacetone
-
pH 6.0
0.385
-
Dihydroxyacetone
-
-
0.385
-
Dihydroxyacetone
-
pH 6.0, 25C
0.77
-
Dihydroxyacetone
-
25C
1.18
-
Dihydroxyacetone
-
pH 9.1, 37C, wild-type enzyme
1.3
-
Dihydroxyacetone
-
-
2
-
Dihydroxyacetone
-
pH 9.1, 37C, mutant D
4.87
-
Dihydroxyacetone
-
-
10.9
-
glycero
-
-
-
0.5
-
glycerol
-
pH 10.0
0.8
-
glycerol
-
pH 10, 35C
1.4
-
glycerol
-
pH 9.0, 25C
5.1
-
glycerol
-
pH 8.8, 25C
10.9
-
glycerol
-
-
10.9
-
glycerol
-
pH 9.0, 25C
47
-
glycerol
-
pH 10.3, 30C, recombinant enzyme, in presence of 20 mM KCl
58
-
glycerol
-
25C
73.3
-
glycerol
-
pH 9.7, 37C, mutant D 76.3 mM
74.3
-
glycerol
-
in the presence of NH4+
76
-
glycerol
-
pH 10.3, 30C, recombinant enzyme
81
-
glycerol
-
pH 10.3, 30C, recombinant enzyme, in presence of 30 mM NH4Cl
91.7
-
glycerol
-
pH 9.7, 37C, wild-type enzyme
118
-
glycerol
-
-
0.15
-
Glycerone
-
pH 6.5, 30C, recombinant enzyme
0.22
-
Glycerone
-
pH 6.5, 30C, recombinant enzyme, in presence of 30 mM NH4Cl
0.0165
-
NAD+
-
wild type protein, pH 9.5, 30C
0.0182
-
NAD+
-
mutant protein Q70H/G193C/E291Q/A310T, pH 9.5, 30C
0.089
-
NAD+
-
pH 9.0, 25C
0.13
-
NAD+
-
pH 10.0
0.3
-
NAD+
-
pH 9.0, 25C
0.4614
-
NAD+
-
mutant protein Q70H/D121A/G193C/E291Q/A310T, pH 9.5, 30C
0.5946
-
NAD+
-
mutant protein D121A, pH 9.5, 30C
0.81
-
NAD+
-
pH 10.3, 30C, recombinant enzyme
1
-
NAD+
-
pH 10.3, 30C, recombinant enzyme, in presence of 30 mM NH4Cl
3.2
-
NAD+
-
pH 10.3, 30C, recombinant enzyme, in presence of 20 mM KCl
4.07
-
NAD+
-
pH 9.7, 37C, wild-type enzyme
4.7
-
NAD+
-
pH 9.7, 37C, mutant D
0.05
-
NADH
-
pH 6.5, 30C, recombinant enzyme
0.07
-
NADH
-
pH 6.5, 30C, recombinant enzyme, in presence of 20 mM KCl
0.08
-
NADH
-
pH 9.1, 37C, wild-type enzyme
0.08
-
NADH
-
pH 6.5, 30C, recombinant enzyme, in presence of 30 mM NH4Cl
0.12
-
NADH
-
pH 9.1, 37C, mutant D
4.4
-
R-1-amino-2-propanol
-
pH 8.8, 25C
500
-
S-1-amino-2-propanol
-
pH 8.8, 25C
0.24
-
Glycerone
-
pH 6.5, 30C, recombinant enzyme, in presence of 20 mM KCl
additional information
-
additional information
-
kinetic study with different effectors, overview
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2.6
-
1,3-butanediol
-
pH 9.5, 30C
2.7
-
1,3-butanediol
-
pH 9.5, 30C
3.3
-
1,3-butanediol
-
wild type protein, pH 9.5, 30C
9.1
-
1,3-butanediol
-
mutant protein Q70H/G193C/E291Q/A310T, pH 9.5, 30C
62.4
-
1,3-butanediol
-
mutant protein D121A, pH 9.5, 30C
87.2
-
1,3-butanediol
-
mutant protein Q70H/D121A/G193C/E291Q/A310T, pH 9.5, 30C
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.09
-
1,3-butanediol
-
pH 9.5, 30C
706
0.12
-
1,3-butanediol
-
pH 9.5, 30C
706
0.2
-
1,3-butanediol
-
wild type protein, pH 9.5, 30C
706
0.77
-
1,3-butanediol
-
mutant protein Q70H/G193C/E291Q/A310T, pH 9.5, 30C
706
1.12
-
1,3-butanediol
-
mutant protein Q70H/D121A/G193C/E291Q/A310T, pH 9.5, 30C
706
1.26
-
1,3-butanediol
-
mutant protein D121A, pH 9.5, 30C
706
105
-
NAD+
-
mutant protein D121A, pH 9.5, 30C
14330
188
-
NAD+
-
mutant protein Q70H/D121A/G193C/E291Q/A310T, pH 9.5, 30C
14330
200
-
NAD+
-
wild type protein, pH 9.5, 30C
14330
500
-
NAD+
-
mutant protein Q70H/G193C/E291Q/A310T, pH 9.5, 30C
14330
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
11.1
-
Dihydroxyacetone
-
-
11.6
-
Hydroxyacetone
-
-
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2
-
2-amino-2-(hydroxymethyl)-1,3-propanediol
-
strong inhibition, IC50 2 mM
0.3
-
2-mercaptoethanol
-
strong inhibition, IC50 0.3 mM
4
-
ethylene glycol
-
strong inhibition, IC50 4 mM
0.2
-
N-ethylmaleimide
-
rapid inactivation, IC50: 0.2 mM
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.01
-
O13702, -
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
-
O13702, -
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
-
A0MLR7, -
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
-
A0MLR7, -
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
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5
6
-
reduction of dihydroxyacetone
5
-
-
reduction of hydroxyacetone
6
-
-
reduction of dihydroxyacetone or 3-hydroxybutane-2-one
6
-
-
reaction of dihydroxyacetone
7.2
-
-
oxidation of glycerol, wild-type enzyme
7.5
8.5
-
reduction of dihydroxyacetone, phosphate buffer
7.5
-
-
oxidation of glycerol, mutant D
8
8.5
-
oxidation of 1,2-propanediol
8
-
-
oxidation of glycerol, tetraethyl ammonium chloride/tetraethylammonium hydroxide buffer
8
-
-
dihydroxyaceton reduction reaction
8.3
-
-
reduction of dihydroxyacetone, mutant D
8.6
-
-
reduction of dihydroxyacetone, wild-type enzyme
9
-
-
oxidation of glycerol or butanediol
9
-
-
oxidation of glycerol
9
-
-
oxidation of glycerol
9.5
10.5
-
oxidation of glycerol, diphosphate buffer
9.5
-
-
in an aqueous buffer system
10
10.5
-
-
10
-
-
oxidation of glycerol
10.5
11
-
NADH production
10.5
-
-
in reverse micelles
11
12
-
oxidation of glycerol
11
-
-
glycerol oxidation reaction
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
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
6.8
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
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
37
-
-
assay at, in reverse micelles
50
-
-
oxidation of butanediol; oxidation of glycerol
50
-
-
oxidation of glycerol
65
-
-
oxidation of propanediol
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6
-
-
43% residual activity
20
80
-
activity range, profile overview
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4.7
-
Q8ZKM9, -
calculated; theoretical value
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
Escherichia coli JM109
-
-
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
soluble, isolation from crude cell extract
Manually annotated by BRENDA team
-
soluble, isolation from crude cell extract
Manually annotated by BRENDA team
-
soluble, isolation from crude cell extract
Manually annotated by BRENDA team
-
soluble, isolation from crude cell extract
Manually annotated by BRENDA team
-
soluble, isolation from crude cell extract
Manually annotated by BRENDA team
-
soluble, isolation from crude cell extract
Manually annotated by BRENDA team
-
soluble, isolation from crude cell extract
Manually annotated by BRENDA team
-
soluble, isolation from crude cell extract
Manually annotated by BRENDA team
Clostridium beijerinckii, Clostridium difficile
-
soluble, isolation from crude cell extract
Manually annotated by BRENDA team
-
soluble, isolation from crude cell extract
Manually annotated by BRENDA team
-
soluble, isolation from crude cell extract; soluble, isolation from crude cell extract; soluble, isolation from crude cell extract
-
Manually annotated by BRENDA team
Clostridium butyricum E5, Enterobacter aerogenes 1033, Enterobacter aerogenes 2103, Enterobacter aerogenes P14, Escherichia coli ECFS, Pichia membranifaciens H 112, Schizosaccharomyces pombe 972h-
-
soluble, isolation from crude cell extract
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
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
-
gel filtration; sedimentation equilibrium method
336000
390000
-
gel filtration
400000
-
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
Q8ZKM9, -
x * 38742 , calculated, 367 amino acid residues
?
-
x * 40000, SDS-PAGE
?
A0MLR7
x * 42000, SDS-PAGE
?
Escherichia coli JM109
-
x * 40000, SDS-PAGE
-
?
Klebsiella pneumoniae KG1
-
x * 42000, SDS-PAGE
-
?
Klebsiella pneumoniae MGH78578, Salmonella enterica ATCC 9150
-
x * 39000, SDS-PAGE
-
dimer
-
2 * 38000, SDS-PAGE
dimer
-
2 or 4 * 40000, SDS-PAGE
dimer
-
2 * 36000, SDS-PAGE
dimer
Enterobacter aerogenes 2103
-
2 or 4 * 40000, SDS-PAGE
-
dimer
Pichia membranifaciens H 112
-
2 * 38000, SDS-PAGE
-
monomer
-
crystallization data
octamer
-
8 * 47000, SDS-PAGE
octamer
-
8 * 42000-43000, SDS-PAGE
octamer
-
8 * 39500, SDS-PAGE
octamer
-
8 * 40000, recombinant His-tagged enzyme, SDS-PAGE, 8 * 39800, about, sequence calculation
octamer
-
8 * 42000-43000, SDS-PAGE
-
tetramer
-
4 * 38000, SDS-PAGE
tetramer
-
2 or 4 * 40000, SDS-PAGE
tetramer
Enterobacter aerogenes 2103
-
2 or 4 * 40000, SDS-PAGE
-
monomer
Thermotoga maritima TM0423
-
crystallization data
-
additional information
-
GST-CglD fusion protein: 67000Da, SDS-PAGE
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
crystal obtained by hanging-drop vaour-diffusion method, S305C mutant
-
preliminary X-ray characterization; sitting drop vapor-diffusion method
Q8ZKM9, -
in presence of glycerol
-
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4
-
-
25C, 10 min, 30% loss of activity
5.5
10
-
30C, 60 min, stable
7.5
-
-
most stable
7.5
-
-
25C, 10 min, maximal stability, 10% loss of activity
10
-
-
25C, 10 min, 40% loss of activity
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
30
-
-
60 min, stable in the pH range pH 5.5-10
50
-
-
10 min stable
50
-
-
15 min, stable around pH 7.0
60
-
-
10 min, inactivation
70
-
-
30 min stable
75
-
-
10 min stable
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
frozen, retains about 42% of initial activity for 2 months
-
0-5C, 50 to 55% loss of original activity within 48 h
-
-15C, with 5% culture filtrate or 5% boiled crude cell extract, 10% Ficoll, pH 7.5, stable for 1 month
-
-70C, long term storage
-
4C, in 2 M (NH4)2SO4, 1 M glycerol, several months
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-
Clostridium difficile
-
GST-tagged protein
-
immobilized metal ion affinity chromatography (Co2+)
-
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
-
immobilized metal ion affinity chromatography (Co2+)
-
immobilized metal ion affinity chromatography (Co2+)
-
immobilized metal ion affinity chromatography (Ni2+); purity estimated from SDS-PAGE: 95%
Q8ZKM9, -
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
CglD, GST-tagged protein, expressed in E. coli BL21 (DE3)
-
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(DE3)
-
expressed in E. coli
-
expressed in Klebsiella pneumoniae KG1
A0MLR7
expressed in Klebsiella pneumoniae KG1; overexpressed in Klebsiella pneumoniae KG1
A0MLR7, -
His-tagged version expressed in Escherichia coli BL21(DE3)
-
His-tagged version expressed in Escherichia coli BL21 STAR (DE3); N-terminal His-tag, expressed in E. coli BL21 STAR (DE3)
Q8ZKM9, -
overexpressed in Schizosaccharomyces pombe
O13702, -
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
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 alcohols and aliphatic or aromatic hydrocarbons when glycerol used as the only substrate; induced by n-decanol (as sole carbon source)
Mucor circinelloides YR-1
-
-
induced by glucose starvation, essential for glycerol assimilation
O13702, -
induced by glucose starvation, essential for glycerol assimilation
Schizosaccharomyces pombe ARC039
-
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
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)
S305C
-
S305C mutant used for crystallisation
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
analysis
-
glycerol dehydrogenase can be immobilised in a polycarbamoyl sulfonate-hydrogel and used as a sensor for glycerol
analysis
-
development of an integrated multienzyme electrochemical biosensor for the determination of glycerol in wines. The biosensor is based on the glycerol dehydrogenase/diaphorase bienzyme system. The enzyme system is immobilized together with the mediator tetrathiafulvalene on a 3-mercaptopropionic acid self-assembled monolayer-modified gold electrode by using a dialysis membrane
brewing
-
enzymatic assay for the determination of glycerol in wine and beer
biotechnology
-
production of 1,2-propanediol in yeast
molecular biology
-
enzymatic redox cofactor regeneration in organic media: functionalization and application of recombinant glycerol dehydrogenase and soluble transhydrogenase in reverse micelles, overview
molecular biology
Escherichia coli JM109
-
enzymatic redox cofactor regeneration in organic media: functionalization and application of recombinant glycerol dehydrogenase and soluble transhydrogenase in reverse micelles, overview
-
synthesis
-
biotransformation of glycerol to dihydroxyacetone by recombinant Gluconobacter oxydans DSM 2343. Overproduction of the glycerol dehydrogenase to improve production of dihydroxyacetone
synthesis
-
high specificity of enzyme for secondary alcohols in R-configuration, use of enzyme for production of chiral compounds