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Information on EC 1.1.99.22 - glycerol dehydrogenase (acceptor)
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EC Tree
1.1.99.22 glycerol dehydrogenase (acceptor)IUBMB Comments
A quinoprotein. Also acts, more slowly, on a number of other polyols including D-sorbitol, D-arabinitol, meso-erythritol, ribitol and propane-1,2-diol.
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Word Map
- 1.1.99.22
- gluconobacter
- suboxydans
- l-sorbose
- frateurii
-
fad-containing
- oxydans
- dehydrogenases
-
mesophilic
-
thermotolerant
The enzyme appears in viruses and cellular organisms
Synonyms
pqq-gldh, pqq-sldh, d-pentonate 4-dehydrogenase, quinone-dependent glycerol dehydrogenase, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
5-keto-D-gluconate-producing enzyme
D-pentonate 4-dehydrogenase
D-sorbitol dehydrogenase subunit SldA
GLD
GLDH
glycerol dehydrogenase
NBRC3255_0235
PQQ-dependent GLDH
PQQ-GLDH
PQQ-SLDH
pyrroloquinoline quinone-dependent glycerol dehydrogenase
quinone-dependent glycerol dehydrogenase
additional information
pyrroloquinoline quinone-dependent glycerol dehydrogenase
-
-
-
additional information
-
could be identical with non-purified EC 1.1.2.2 or D-arabitol dehydrogenase
additional information
-
could be identical with non-purified EC 1.1.2.2 or D-arabitol dehydrogenase
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
glycerol + acceptor = glycerone + reduced acceptor
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
glycerol:acceptor 1-oxidoreductase
A quinoprotein. Also acts, more slowly, on a number of other polyols including D-sorbitol, D-arabinitol, meso-erythritol, ribitol and propane-1,2-diol.
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CAS REGISTRY NUMBER
COMMENTARY
249285-11-8
EC 1.1.99.22 is undistinguishable from EC 1.1.1.6 in Chemical Abstracts
9028-14-2
EC 1.1.99.22 is undistinguishable from EC 1.1.1.6 in Chemical Abstracts
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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
(S)-2-hydroxyglutarate + pyrroloquinoline quinone
2-oxoglutarate + pyrroloquinoline quinol
D-arabitol + 2,6-dichlorophenolindophenol
D-xylulose + reduced 2,6-dichlorophenolindophenol
-
-
-
?
D-arabonate + 2,6-dichlorophenolindophenol
4-dehydro-D-arabonate + reduced 2,6-dichlorophenolindophenol
D-erythronate + 2,6-dichlorophenolindophenol
3-dehydro-D-erythronate + reduced 2,6-dichlorophenolindophenol
D-fructose + oxidized 2,6-dichlorophenolindophenol
5-dehydro-D-fructose + reduced 2,6-dichlorophenolindophenol
D-gluconate + 2,6-dichlorophenolindophenol
5-dehydro-D-gluconate + reduced 2,6-dichlorophenolindophenol
-
-
-
?
D-psicose + 2,6-dichlorophenolindophenol
5-dehydro-D-psicose + reduced 2,6-dichlorophenolindophenol
D-ribonate + 2,6-dichlorophenolindophenol
4-dehydro-D-ribonate + reduced 2,6-dichlorophenolindophenol
D-sorbitol + 2,6-dichlorophenolindophenol
? + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
D-sorbitol + 2,6-dichlorophenolindophenol
L-sorbose + reduced 2,6-dichlorophenolindophenol
-
-
-
?
galactitol + acceptor
?
-
i.e. dulcitol, 29% of activity with glycerol
-
-
?
glycerol + 2,6-dichlorophenolindophenol
dihydroxyacetone + reduced 2,6-dichlorophenolindophenol
-
-
-
?
glycerol + 2,6-dichlorophenolindophenol
glycerone + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
glycerol + phenazine methosulfate
glycerone + reduced phenazine methosulfate
-
-
-
-
?
glycerol + potassium ferricyanide
glycerone + potassium ferrocyanide
-
-
-
-
?
(S)-2-hydroxyglutarate + pyrroloquinoline quinone
2-oxoglutarate + pyrroloquinoline quinol
-
-
-
-
?
(S)-2-hydroxyglutarate + pyrroloquinoline quinone
2-oxoglutarate + pyrroloquinoline quinol
-
coupling with 2,6-dichlorophenolindophenol
-
-
?
(S)-2-hydroxyglutarate + pyrroloquinoline quinone
2-oxoglutarate + pyrroloquinoline quinol
-
-
-
-
?
(S)-2-hydroxyglutarate + pyrroloquinoline quinone
2-oxoglutarate + pyrroloquinoline quinol
-
coupling with 2,6-dichlorophenolindophenol
-
-
?
(S)-2-hydroxyglutarate + pyrroloquinoline quinone
2-oxoglutarate + pyrroloquinoline quinol
-
-
-
-
?
(S)-2-hydroxyglutarate + pyrroloquinoline quinone
2-oxoglutarate + pyrroloquinoline quinol
-
-
-
-
?
(S)-2-hydroxyglutarate + ubiquinone
2-oxoglutarate + ubiquinol
-
-
-
-
?
(S)-2-hydroxyglutarate + ubiquinone
2-oxoglutarate + ubiquinol
-
-
-
-
?
D-arabitol + 2,6-dichlorophenolindophenol
? + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
D-arabitol + 2,6-dichlorophenolindophenol
? + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
D-arabitol + acceptor
?
-
136% of activity with glycerol oxidation
-
-
?
D-arabitol + acceptor
?
-
136% of activity with glycerol oxidation
-
-
?
D-arabonate + 2,6-dichlorophenolindophenol
4-dehydro-D-arabonate + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
D-arabonate + 2,6-dichlorophenolindophenol
4-dehydro-D-arabonate + reduced 2,6-dichlorophenolindophenol
-
-
-
?
D-arabonate + 2,6-dichlorophenolindophenol
4-dehydro-D-arabonate + reduced 2,6-dichlorophenolindophenol
-
-
-
?
D-arabonate + 2,6-dichlorophenolindophenol
4-dehydro-D-arabonate + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
D-erythronate + 2,6-dichlorophenolindophenol
3-dehydro-D-erythronate + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
D-erythronate + 2,6-dichlorophenolindophenol
3-dehydro-D-erythronate + reduced 2,6-dichlorophenolindophenol
-
-
-
?
D-erythronate + 2,6-dichlorophenolindophenol
3-dehydro-D-erythronate + reduced 2,6-dichlorophenolindophenol
-
-
-
?
D-erythronate + 2,6-dichlorophenolindophenol
3-dehydro-D-erythronate + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
D-fructose + oxidized 2,6-dichlorophenolindophenol
5-dehydro-D-fructose + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
D-fructose + oxidized 2,6-dichlorophenolindophenol
5-dehydro-D-fructose + reduced 2,6-dichlorophenolindophenol
-
-
-
?
D-fructose + oxidized 2,6-dichlorophenolindophenol
5-dehydro-D-fructose + reduced 2,6-dichlorophenolindophenol
-
-
-
?
D-fructose + oxidized 2,6-dichlorophenolindophenol
5-dehydro-D-fructose + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
D-mannitol + acceptor
D-fructose + reduced acceptor
-
26% of activity with glycerol
-
?
D-psicose + 2,6-dichlorophenolindophenol
5-dehydro-D-psicose + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
D-psicose + 2,6-dichlorophenolindophenol
5-dehydro-D-psicose + reduced 2,6-dichlorophenolindophenol
-
-
-
?
D-psicose + 2,6-dichlorophenolindophenol
5-dehydro-D-psicose + reduced 2,6-dichlorophenolindophenol
-
-
-
?
D-psicose + 2,6-dichlorophenolindophenol
5-dehydro-D-psicose + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
D-ribitol + 2,6-dichlorophenolindophenol
? + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
D-ribitol + 2,6-dichlorophenolindophenol
? + reduced 2,6-dichlorophenolindophenol
-
-
-
?
D-ribitol + 2,6-dichlorophenolindophenol
? + reduced 2,6-dichlorophenolindophenol
-
-
-
?
D-ribonate + 2,6-dichlorophenolindophenol
4-dehydro-D-ribonate + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
D-ribonate + 2,6-dichlorophenolindophenol
4-dehydro-D-ribonate + reduced 2,6-dichlorophenolindophenol
-
-
-
?
D-sorbitol + acceptor
L-sorbose + reduced acceptor
-
45% of acticvity with glycerol
-
?
D-sorbitol + acceptor
L-sorbose + reduced acceptor
-
45% of acticvity with glycerol
-
?
glycerol + acceptor
glycerone + reduced acceptor
-
2,6-dichlorophenolindophenol/phenazine methosulfate act as in vitro acceptor, broad specificity, no substrates are: xylitol, D-fructose, D-glucose, D-gluconate, 2-keto-D-gluconate, ethanol and acetaldehyde
i.e. dihydroxyacetone
?
glycerol + acceptor
glycerone + reduced acceptor
-
2,6-dichlorophenolindophenol/phenazine methosulfate act as in vitro acceptor, broad specificity, no substrates are: xylitol, D-fructose, D-glucose, D-gluconate, 2-keto-D-gluconate, ethanol and acetaldehyde
i.e. dihydroxyacetone
?
meso-erythritol + acceptor
?
-
111% of activity with glycerol
-
-
?
additional information
?
-
-
PQQ-GLDH plays a major role in L-sorbose production
-
-
?
additional information
?
-
-
the enzyme shows ubiquinol-2 oxidase activity
-
-
?
additional information
?
-
-
the enzyme shows ubiquinol-2 oxidase activity
-
-
?
additional information
?
-
-
PQQ-GLDH plays a major role in L-sorbose production
-
-
?
additional information
?
-
-
production of 5-keto-D-gluconate is solely dependent on enzyme
-
-
?
additional information
?
-
-
broad substrate specificity but high regio- and stereospecificity
-
-
?
additional information
?
-
-
broad substrate specificity but high regio- and stereospecificity
-
-
?
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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
(S)-2-hydroxyglutarate + pyrroloquinoline quinone
2-oxoglutarate + pyrroloquinoline quinol
(S)-2-hydroxyglutarate + pyrroloquinoline quinone
2-oxoglutarate + pyrroloquinoline quinol
-
-
-
-
?
(S)-2-hydroxyglutarate + pyrroloquinoline quinone
2-oxoglutarate + pyrroloquinoline quinol
-
-
-
-
?
(S)-2-hydroxyglutarate + pyrroloquinoline quinone
2-oxoglutarate + pyrroloquinoline quinol
-
-
-
-
?
(S)-2-hydroxyglutarate + pyrroloquinoline quinone
2-oxoglutarate + pyrroloquinoline quinol
-
-
-
-
?
(S)-2-hydroxyglutarate + ubiquinone
2-oxoglutarate + ubiquinol
-
-
-
-
?
(S)-2-hydroxyglutarate + ubiquinone
2-oxoglutarate + ubiquinol
-
-
-
-
?
additional information
?
-
-
PQQ-GLDH plays a major role in L-sorbose production
-
-
?
additional information
?
-
-
PQQ-GLDH plays a major role in L-sorbose production
-
-
?
additional information
?
-
-
production of 5-keto-D-gluconate is solely dependent on enzyme
-
-
?
additional information
?
-
-
broad substrate specificity but high regio- and stereospecificity
-
-
?
additional information
?
-
-
broad substrate specificity but high regio- and stereospecificity
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2,6-dichlorophenolindophenol
-
acts in vitro as acceptor together with phenazine methosulfate
phenazine methosulfate
-
acts in vitro as acceptor together with 2,6-dichlorophenolindophenol, linked to electron-transport chain of the organism
additional information
-
NAD+, NADP+ or molecular oxygen do not act as acceptors
-
additional information
-
the enzyme is actvie with 2,6-dichlorophenolindophenol
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
additional information
Ca2+
EDTA-treated enzyme is reactivated to almost the original level by the addition of pyrroloquinoline quinone and Ca2+
additional information
-
Mg2+, Sr2+, Ba2+, and several kinds of lantanides do not activate the enzyme
additional information
metallic ions, Mg2+, Sr2+, Ba2+, and several kinds of lantanides, are ineffective in reactivation of EDTA-trreated enzyme
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
EDTA
treatment of the membrane fraction causes a clear decrease in D-pentonate 4-dehydrogenase activity, activity is reactivated to almost the original level by the addition of pyrroloquinoline quinone and Ca2+
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
temperature increase reduces the enzyme activity, which can be restores by pyroloquinoline quinone. Adaptation of the CHM43 strain at 38.5°C
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
maximum activity at the end of exponential growth phase, activity occurs in various Gluconobacter species, such as Gluconobacter cerinus, Gluconobacter gluconicus, Gluconobacter suboxydans and Gluconobacter albidus
-
-
brenda
genes sldB and sldA encoding the small and the large subunit of the enzyme
-
-
brenda
genes sldB and sldA encoding the small and the large subunit of the enzyme
-
-
brenda
identical with D-sorbitol dehydrogenase, EC1.1.99.21, and D-arabitol dehydrogenase, EC1.1.1.11
-
-
brenda
maximum activity at the end of exponential growth phase, activity occurs in various Gluconobacter species, such as Gluconobacter cerinus, Gluconobacter gluconicus, Gluconobacter suboxydans and Gluconobacter albidus
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
additional information
-
temperature increase reduces the enzyme activity, which can be restored by pyroloquinoline quinone. Adaptation of the CHM43 strain at 38.5°C
brenda
additional information
-
temperature increase reduces the enzyme activity, which can be restored by pyroloquinoline quinone. Adaptation of the CHM43 strain at 38.5°C
-
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
additional information
-
the reactive center of th enzyme is orientated to the periplasmic space
-
brenda
additional information
-
the reactive center of th enzyme is orientated to the periplasmic space
-
-
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
metabolism
-
pyrroloquinoline quinone-dependent glycerol dehydrogenase is a primary dehydrogenase of the respiratory chain and responsible for L-sorbose production
metabolism
-
the enzyme is involved in biosynthesis of dihydroxyacetone, disruption of the membrane-bound alcohol dehydrogenase-encoding gene improved glycerol use and dihydroxyacetone productivity in Gluconobacter oxydans, overview
metabolism
-
pyrroloquinoline quinone-dependent glycerol dehydrogenase is a primary dehydrogenase of the respiratory chain and responsible for L-sorbose production
-
metabolism
-
the enzyme is involved in biosynthesis of dihydroxyacetone, disruption of the membrane-bound alcohol dehydrogenase-encoding gene improved glycerol use and dihydroxyacetone productivity in Gluconobacter oxydans, overview
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). A0A347WF32_9PROT
128
4
13500
TrEMBL
-
A0A221K5P1_9RHOB
815
5
87453
TrEMBL
-
A0A2H1PPK6_XANCH
809
5
86343
TrEMBL
-
A0A347WF31_9PROT
732
1
79357
TrEMBL
-
C6B8J5_RHILS
Rhizobium leguminosarum bv. trifolii (strain WSM1325)
798
5
85565
TrEMBL
-
A0A160TLL1_9ZZZZ
559
0
60093
TrEMBL
other Location (Reliability: 2)
C6VSN2_DYAFD
Dyadobacter fermentans (strain ATCC 700827 / DSM 18053 / CIP 107007 / KCTC 52180 / NS114)
722
0
79148
TrEMBL
-
A0A086P7V8_SPHHM
Sphingobium herbicidovorans (strain ATCC 700291 / DSM 11019 / NBRC 16415 / MH)
105
0
10963
TrEMBL
-
A0A067Z2Z6_GLUOY
743
0
79576
TrEMBL
-
A0A017HL94_9RHOB
884
5
94446
TrEMBL
-
A0A009G0Y2_ACIBA
799
5
88849
TrEMBL
-
A0A067Z3Q4_GLUOY
126
4
13724
TrEMBL
-
A0A067Z560_GLUOY
739
1
79883
TrEMBL
-
A0A067Z840_GLUOY
126
4
13607
TrEMBL
-
A0A2S6STM2_9PROT
737
1
84988
TrEMBL
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
large subunit DELTAsldA mutant strain show much slower growth compared to the wild-type strain, phenotype, overview
additional information
-
large subunit DELTAsldA mutant strain show much slower growth compared to the wild-type strain, phenotype, overview
-
additional information
-
enzyme disruption mutant, oxidation activity against D-arabitol, D-sorbitol, D-mannitol, ribitol, meso-erythritol and glycerol are diminished
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
amphoteric detergents, such as dimethyldodecylamineoxide, lauroylsarcosine, dodecylsulfobetaine, lauroylbetaine are effective solubilizers
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CM-Toyopearl C-650 column chromatography, and Sephadex G-200 gel filtration
-
n-octyl-beta-D-thioglucoside, n-octyl-beta-D-glucoside, Mydol 10, and Mydol 12 are effective detergents to solubilize the enzyme
to homogeneity by anion exchange chromatography and Ni-affinity chromatography
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
genes sldB and sldA encoding the small and the large subunit of the enzyme
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ameyama, M.; Shinagawa, E.; Matsushita, K.; Adachi, O.
Solubilization, purification and properties of membrane-bound glycerol dehydrogenase from Gluconobacter industrius
Agric. Biol. Chem.
49
1001-1010
1985
Gluconobacter oxydans, Gluconobacter oxydans IFO 3260
-
brenda
Matsushita, K.; Fujii, Y.; Ano, Y.; Toyama, H.; Shinjoh, M.; Tomiyama, N.; Miyazaki, T.; Sugisawa, T.; Hoshino, T.; Adachi, O.
5-Keto-D-gluconate production is catalyzed by a quinoprotein glycerol dehydrogenase, major polyol dehydrogenase, in Gluconobacter species
Appl. Environ. Microbiol.
69
1959-1966
2003
Gluconobacter oxydans
brenda
Ichinose, H.; Kamiya, N.; Goto, M.
Enzymatic redox cofactor regeneration in organic media: functionalization and application of glycerol dehydrogenase and soluble transhydrogenase in reverse micelles
Biotechnol. Prog.
21
1192-1197
2005
Escherichia coli, Escherichia coli JM109
brenda
Michizoe, J.; Ichinose, H.; Kamiya, N.; Maruyama, T.; Goto, M.
Functionalization of the cytochrome P450cam monooxygenase system in the cell-like aqueous compartments of water-in-oil emulsions
J. Biosci. Bioeng.
99
12-17
2005
Escherichia coli, Escherichia coli JM109
brenda
Soemphol, W.; Adachi, O.; Matsushita, K.; Toyama, H.
Distinct physiological roles of two membrane-bound dehydrogenases responsible for D-sorbitol oxidation in Gluconobacter frateurii
Biosci. Biotechnol. Biochem.
72
842-850
2008
Gluconobacter frateurii, Gluconobacter frateurii THD32
brenda
Saichana, I.; Moonmangmee, D.; Adachi, O.; Matsushita, K.; Toyama, H.
Screening of thermotolerant Gluconobacter strains for production of 5-keto-D-gluconic acid and disruption of flavin adenine dinucleotide-containing D-gluconate dehydrogenase
Appl. Environ. Microbiol.
75
4240-4247
2009
Gluconobacter sp., Gluconobacter sp. THE42
brenda
Hattori, H.; Yakushi, T.; Matsutani, M.; Moonmangmee, D.; Toyama, H.; Adachi, O.; Matsushita, K.
High-temperature sorbose fermentation with thermotolerant Gluconobacter frateurii CHM43 and its mutant strain adapted to higher temperature
Appl. Microbiol. Biotechnol.
95
1531-1540
2012
Gluconobacter frateurii, Gluconobacter frateurii CHM43, NBRC 101659
brenda
Habe, H.; Fukuoka, T.; Morita, T.; Kitamoto, D.; Yakushi, T.; Matsushita, K.; Sakaki, K.
Disruption of the membrane-bound alcohol dehydrogenase-encoding gene improved glycerol use and dihydroxyacetone productivity in Gluconobacter oxydans
Biosci. Biotechnol. Biochem.
74
1391-1395
2010
Gluconobacter oxydans, Gluconobacter oxydans NBRC12528
brenda
Habe, H.; Shimada, Y.; Fukuoka, T.; Kitamoto, D.; Itagaki, M.; Watanabe, K.; Yanagishita, H.; Yakushi, T.; Matsushita, K.; Sakaki, K.
Use of a Gluconobacter frateurii mutant to prevent dihydroxyacetone accumulation during glyceric acid production from glycerol
Biosci. Biotechnol. Biochem.
74
2330-2332
2010
Gluconobacter frateurii, Gluconobacter frateurii THD32
brenda
Ano, Y.; Hours, R.A.; Akakabe, Y.; Kataoka, N.; Yakushi, T.; Matsushita, K.; Adachi, O.
Membrane-bound glycerol dehydrogenase catalyzes oxidation of D-pentonates to 4-dehydro-D-pentonates, D-fructose to 5-dehydro-D-fructose, and D-psicose to 5-dehydro-D-psicose
Biosci. Biotechnol. Biochem.
81
411-418
2017
Gluconobacter thailandicus, Gluconobacter thailandicus NBRC 3258
brenda
Ano, Y.; Hours, R.; Akakabe, Y.; Kataoka, N.; Yakushi, T.; Matsushita, K.; Adachi, O.
Membrane-bound glycerol dehydrogenase catalyzes oxidation of D-pentonates to 4-keto-D-pentonates, D-fructose to 5-keto-D-fructose, and D-psicose to 5-keto-D-psicose
Biosci. Biotechnol. Biochem.
81
411-418
2017
Gluconobacter thailandicus (M9MJR9), Gluconobacter thailandicus NBRC 3255 (M9MJR9)
brenda
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Release 2023.1 (January 2023)
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