Information on EC 1.2.5.2 - aldehyde dehydrogenase (quinone)

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.2.5.2
-
RECOMMENDED NAME
GeneOntology No.
aldehyde dehydrogenase (quinone)
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
an aldehyde + a quinone + H2O = a carboxylate + a quinol
show the reaction diagram
; wide specificity, acts on straight-chain aldehydes up to C10, aromatic aldehydes, glyoxylate and glyceraldehyde
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Fatty acid degradation
-
-
Pyruvate metabolism
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-
SYSTEMATIC NAME
IUBMB Comments
aldehyde:quinone oxidoreductase
Wide specificity; acts on straight-chain aldehydes up to C10, aromatic aldehydes, glyoxylate and glyceraldehyde. The enzymes contains a PQQ cofactor and multiple hemes that deliver the electrons to the membrane quinone pool.
CAS REGISTRY NUMBER
COMMENTARY hide
75536-77-5
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SKU 14; strain SKU 14, isolated in Thailand
-
-
Manually annotated by BRENDA team
SKU 14; strain SKU 14, isolated in Thailand
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-
Manually annotated by BRENDA team
strain Bo
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1-butanol + acceptor
butanal + reduced acceptor
show the reaction diagram
3-methylbenzaldehyde + ferricyanide
3-methylbenzoic acid + ferrocyanide + H+
show the reaction diagram
acetaldehyde + 2 ferricyanide + H2O
acetate + 2 ferrocyanide + 2 H+
show the reaction diagram
acetaldehyde + 2,6-dichlorophenol indophenol
acetate + reduced 2,6-dichlorophenol indophenol
show the reaction diagram
acetaldehyde + 2,6-dichlorophenolindophenol
acetate + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
acetaldehyde + a quinone + H2O
acetate + a quinol
show the reaction diagram
acetaldehyde + acceptor + H2O
acetic acid + reduced acceptor
show the reaction diagram
-
potassium ferricyanide, 2,6-dichlorophenolindophenol, phenazine methosulfate, Wurster's blue and nitroblue tetrazolium are utilized as electron acceptors in aldehyde oxidation
-
-
?
acetaldehyde + ferricyanide
acetic acid + ferrocyanide + H+
show the reaction diagram
acetaldehyde + oxidized 2,6-dichlorophenolindophenol
acetate + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
acetaldehyde + oxidized tetramethylphenylenediamine
acetate + reduced tetramethylphenylenediamine
show the reaction diagram
acetaldehyde + oxydized phenazine methosulfate
acetic acid + reduced phenazine methosulfate
show the reaction diagram
acetaldehyde + phenazine methosulfate
acetate + reduced phenazine methosulfate
show the reaction diagram
acetaldehyde + ubiquinone
acetate + ubiquinol
show the reaction diagram
-
electrons removed from substrate by alcohol dehydrogenase complex are initially transferred to the pyrroloquinoline quinone centre and further tunnelled across four cytochromes c to the membrane ubiquinone
-
-
?
benzaldehyde + a quinone + H2O
benzoate + a quinol
show the reaction diagram
butanal + 2 ferricyanide + H2O
butanoate + 2 ferrocyanide + 2 H+
show the reaction diagram
butanal + a quinone + H2O
butanoate + a quinone
show the reaction diagram
butanal + acceptor + H2O
butanoate + reduced acceptor
show the reaction diagram
-
potassium ferricyanide, 2,6-dichlorophenolindophenol, phenazine methosulfate, Wurster's blue and nitroblue tetrazolium are utilized as electron acceptors in aldehyde oxidation
-
-
?
butanal + ferricyanide
butanoic acid + ferrocyanide + H+
show the reaction diagram
butyraldehyde + 2,6-dichlorophenol indophenol
butanoate + reduced 2,6-dichlorophenol indophenol
show the reaction diagram
butyraldehyde + 2,6-dichlorophenolindophenol
butanoate + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
butyraldehyde + oxidized tetramethylphenylenediamine
butanoate + reduced tetramethylphenylenediamine
show the reaction diagram
-
-
-
-
?
decanal + a quinone + H2O
decanoate + a quinol
show the reaction diagram
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15% of acetaldehyde oxidation
-
?
dodecanal + a quinone + H2O
dodecanoate + a quinol
show the reaction diagram
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15% of acetaldehyde oxidation
-
?
formaldehyde + 2 ferricyanide + H2O
formate + 2 ferrocyanide + 2 H+
show the reaction diagram
formaldehyde + oxidized 2,6-dichlorophenolindophenol
formate + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
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-
-
-
?
formaldehyde + oxidized tetramethylphenylenediamine
formate + reduced tetramethylphenylenediamine
show the reaction diagram
furfural + 2 ferricyanide + H2O
2-furoic acid + 2 ferrocyanide + 2 H+
show the reaction diagram
-
-
-
-
?
glutaraldehyde + 2 ferricyanide + H2O
glutarate + 2 ferrocyanide + 2 H+
show the reaction diagram
-
26.4% compared to the activity with acetaldehyde
-
-
?
glutaraldehyde + 4 ferricyanide + 2 H2O
glutarate + 4 ferrocyanide + 4 H+
show the reaction diagram
glutaraldehyde + oxydized phenazine methosulfate
glutaric acid + reduced phenazine methosulfate
show the reaction diagram
-
26.5% of the activity with acetaldehyde
-
-
?
glycolaldehyde + ferricyanide
hydroxyacetic acid + ferrocyanide + H+
show the reaction diagram
glyoxal + ferricyanide
oxoacetic acid + ferrocyanide + H+
show the reaction diagram
heptanal + a quinone + H2O
heptanoate + a quinol
show the reaction diagram
-
46% of acetaldehyde oxidation
-
?
heptanal + oxidized 2,6-dichlorophenolindophenol
heptanoate + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
heptanal + oxidized tetramethylphenylenediamine
heptanoate + reduced tetramethylphenylenediamine
show the reaction diagram
-
-
-
-
?
hexanal + a quinone + H2O
hexanoate + a quinol
show the reaction diagram
L-sorbosone + ferricyanide
? + ferrocyanide + H+
show the reaction diagram
-
-
-
?
methylglyoxal + ferricyanide
oxopropanoic acid + ferrocyanide + H+
show the reaction diagram
-
-
-
?
octanal + a quinone + H2O
octanoate + a quinol
show the reaction diagram
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48% of acetaldehyde oxidation
-
?
octanal + oxidized tetramethylphenylenediamine
octanoate + reduced tetramethylphenylenediamine
show the reaction diagram
pentanal + 2 ferricyanide + H2O
pentanoate + 2 ferrocyanide + 2 H+
show the reaction diagram
pentanal + a quinone + H2O
pentanoate + a quinol
show the reaction diagram
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58% of acetaldehyde oxidation
-
?
phenylglyoxal + ferricyanide
oxo(phenyl) acetic acid + ferrocyanide + H+
show the reaction diagram
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-
-
?
propanal + 2 ferricyanide + H2O
propanoate + 2 ferrocyanide + 2 H+
show the reaction diagram
propanal + a quinone + H2O
propanoate + a quinol
show the reaction diagram
-
-
-
?
propanal + acceptor + H2O
propanoate + reduced acceptor
show the reaction diagram
-
potassium ferricyanide, 2,6-dichlorophenolindophenol, phenazine methosulfate, Wurster's blue and nitroblue tetrazolium are utilized as electron acceptors in aldehyde oxidation
-
-
?
propanal + ferricyanide
propanoic acid + ferrocyanide + H+
show the reaction diagram
-
-
-
?
propanal + oxidized tetramethylphenylenediamine
propionate + reduced tetramethylphenylenediamine
show the reaction diagram
-
-
-
-
?
propanal + oxydized phenazine methosulfate
propanoic acid + reduced phenazine methosulfate
show the reaction diagram
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72.7% of the activity with acetaldehyde
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-
?
propionaldehyde + 2 ferricyanide + H2O
propionate + 2 ferrocyanide + 2 H+
show the reaction diagram
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72.7% compared to the activity with acetaldehyde
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-
?
propionaldehyde + 2,6-dichlorophenol indophenol
propanoate + reduced 2,6-dichlorophenol indophenol
show the reaction diagram
propionaldehyde + 2,6-dichlorophenolindophenol
propanoate + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
propionaldehyde + oxidized 2,6-dichlorophenolindophenol
propionate + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
valeraldehyde + ferricyanide
pentanoic acid + ferrocyanide + H+
show the reaction diagram
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-
-
?
additional information
?
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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
1-butanol + acceptor
butanal + reduced acceptor
show the reaction diagram
acetaldehyde + a quinone + H2O
acetate + a quinol
show the reaction diagram
acetaldehyde + ubiquinone
acetate + ubiquinol
show the reaction diagram
-
electrons removed from substrate by alcohol dehydrogenase complex are initially transferred to the pyrroloquinoline quinone centre and further tunnelled across four cytochromes c to the membrane ubiquinone
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-
?
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cytochrome b
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; the enzyme complex contains one cytochrome b
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cytochrome c
heme c
pyrroloquinoline quinone
additional information
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Butyraldehyde
substrate inhibition
CuSO4
FeCl3
10 mM, almost complete inhibition
HgCl2
-
1 mM, cosubstate ferricyanide, strong inhibition; 1 mM, strong inhibition
pentanal
substrate inhibition
propionaldehyde
substrate inhibition
ZnSO4
10 mM, almost complete inhibition
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ethylamine
little ADH I activity is detected in the absence of ethylamine or ammonium ions
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.007
1-butanol
-
-
0.075 - 4.5
acetaldehyde
3.3
acetic acid
-
cosubstrate ferricyandie, pH 3.5, 30C
12.3
Butanal
pH 8, 25C
0.033
Butyraldehyde
pH 8.2
1.93 - 4
formaldehyde
0.038
octanal
-
-
0.061
pentanal
pH 8.2
0.057
propionaldehyde
pH 8.2
additional information
additional information
-
the Km value for formaldehyde is measured to be 1013 mM using the formaldehyde solution containing methanol. 2325 mM is obtained with freshly prepared formaldehyde solution only with distilled water. A Km value over 50 mM is observed when using the substrate solution stored in a refrigerator over one month
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
22000
acetic acid
Gluconacetobacter diazotrophicus
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cosubstrate ferricyandie, pH 3.5, 30C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
6720
acetic acid
Gluconacetobacter diazotrophicus
-
cosubstrate ferricyandie, pH 3.5, 30C
751
43
Butanal
Sphingomonas wittichii
A5VEL7
pH 8, 25C
540
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.95
Butyraldehyde
pH 8.2
0.33
pentanal
pH 8.2
8.2
propionaldehyde
pH 8.2
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0018
-
cell-free extracts, horse heart cytochrome c as electron acceptor, pH 5.5
0.0019
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lactate-grown cell extract
0.0044
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2-butanol-grown cell extract
0.01
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cell-free extracts, horse heart cytochrome c as electron acceptor, pH 7.8
0.0106
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1-butanol-grown cell extract
0.066
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cell-free extracts, 2,6-dichlorophenol-indophenol as electron acceptor, pH 7.8
0.096
-
cell-free extracts, O2 as electron acceptor, pH 7.8
0.318
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cell-free extracts, ferricyanide as electron acceptor, pH 5.3
4.8
-
purified enzyme
14
purified ADH IIG, substrate glycerol with cofactor ferricyanide
26.8
purified ADH I, substrate ethanol with cofactors
39.7
-
purified enzyme
180
substrate L-sorbosone, pH 8, 25C
293
-
purified native enzyme
1050
substrate glyoxal, pH 8, 25C
1060
substrate glycolaldehyde, pH 8, 25C
1170
substrate 3-methylbenzaldehyde, pH 8, 25C
1450
substrate valeraldehyde, pH 8, 25C
1690
substrate methylglyoxal, pH 8, 25C
1740
substrate propanal, pH 8, 25C
1900
substrate phenylglyoxal, pH 8, 25C
2470
substrate butanal, pH 8, 25C
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.5
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electron accceptor ferricyanide; using ferricyanide as an electron acceptor, the enzyme shows an optimum pH of 3.5 that shifts to pH 7.0 when phenazine methosulfate plus 2,6-dichlorophenolindophenol are the electron acceptors
5 - 6
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; substrate: formaldehyde
6
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substrate: acetaldehyde
7
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electron acceptor phenazine methosulfate plus 2,6-dichlorophenolindophenol; using ferricyanide as an electron acceptor, the enzyme shows an optimum pH of 3.5 that shifts to pH 7.0 when phenazine methosulfate plus 2,6-dichlorophenolindophenol are the electron acceptors
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 9
-
pH 5-6: optimum, pH 9: about 60% of maximal activity
5 - 7.5
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pH 5.0: about 50% of maximal activity, pH 7.5: about 55% of maximal activity, substrate: acetaldehyde
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
-
; substrate: formaldehyde
60
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phenazine methosulfate/2,6-dichlorophenolindophenol-dependent activity
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25 - 50
-
25C: about 75% of maximal activity, 50C: about 60% of maximal activity
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5
ADH IIG, isoelectric focusing
5.2
-
isoelectric focusing
6.1
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gradient electrophoresis, determined in pH range 3.4-9.0
6.5
ADH IIB, isoelectric focusing
7.6
ADH I, isoelectric focusing
8.2
-
isoelectric focusing, pH-range 3.5-9.5
9.1
-
isoelectric focusing
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
14000
-
1 * 78000, + 1 * 45000 + 1 * 14000, SDS-PAGE
18000
-
1 * 18000 + 1 * 55000 + 1 * 78000, SDS-PAGE; x * 78000 + x * 55000 + x * 18000, SDS-PAGE
39300
12 * 39400, SDS-PAGE, 12 * 39300, calculated, 12 * 39329, MALDI-TOF, plus some octamer; minor protein band, 12 * 39400, SDS-PAGE, 12 * 39300, calculated, 12 * 39329, MALDI-TOF, plus dodecamer
39329
12 * 39400, SDS-PAGE, 12 * 39300, calculated, 12 * 39329, MALDI-TOF, plus some octamer; minor protein band, 12 * 39400, SDS-PAGE, 12 * 39300, calculated, 12 * 39329, MALDI-TOF, plus dodecamer
39400
12 * 39400, SDS-PAGE, 12 * 39300, calculated, 12 * 39329, MALDI-TOF, plus some octamer; minor protein band, 12 * 39400, SDS-PAGE, 12 * 39300, calculated, 12 * 39329, MALDI-TOF, plus dodecamer
43500
-
1 * 71400 + 1 * 43500, SDS-PAGE
45000
-
1 * 78000, + 1 * 45000 + 1 * 14000, SDS-PAGE
55000
-
1 * 18000 + 1 * 55000 + 1 * 78000, SDS-PAGE; x * 78000 + x * 55000 + x * 18000, SDS-PAGE
60000
-
2 * 60000, SDS-PAGE
61000
-
2 * 61000, SDS-PAGE
62000
-
2 * 62000, SDS-PAGE
63000
ADH IIB, gel filtration
64000
2 * 64000, ADH I, SDS-PAGE
66000
-
1 * 66000, SDS-PAGE
67553
x * 67553, BOH, calculated from sequence
68000
ADH IIG, gel filtration
70000
-
gel filtration
71400
-
1 * 71400 + 1 * 43500, SDS-PAGE
72000
1 * 72000, ADH IIG
72689
x * 72689, calculated from sequence
73600
-
1 * 73600, SDS-PAGE
79500
-
gel filtration
79700
-
1 * 79700 + 1 * 50000, SDS-PAGE under denaturing conditions; 1 * 79700 and 1 * 50000,SDS-PAGE
80000
-
1 * 80000 + 1 * 50000, SDS-PAGE
100000
-
gel filtration
105500
-
analytical ultracentrifugation
115000
-
non-denaturing PAGE
120000
-
gel filtration
129000
-
nondenaturing PAGE; PAGE
130000
ADH I, gel filtration
137000
-
3 components, MW 78000 dehydrogenase protein, MW 45000 cytochrome component, MW 14000 component with unknown function, SDS-PAGE
140000
-
2 components, MW 86000 dehydrogenase protein, MW 55000 cytochrome c, SDS-PAGE
141000
-
gel filtration
330000
PAGE, minor protein band
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dodecamer
heterodimer
monomer
octamer
trimer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging drop method
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3 - 9
-
stable at 6C, overnight
685650
3
-
overnight, at 6C, about 20% loss of activity
685650
5 - 7
-
overnight, at 6C, stable
685650
9
-
overnight, at 6C, about 20% loss of activity
685650
9.5
half-life below 5 min
731204
10
-
at 6C, overnight, about 75% inactivation; overnight, at 6C, about 60% loss of activity
685650
11
-
at 6C, overnight, complete inactivation; overnight, at 6C, complete loss of activity
685650
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25 - 32
-
purified enzyme, maximally stable within this range
45
-
10 min, about 50% loss of activity
50
-
10 min, 95% loss of activity
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
instable enzyme, needs a substrate and a detergent as stabilizing agent
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, purified enzyme, 30 days, remains stable
-
-70C, stable for prolonged periods
-
-70C, stable for several months
-
-70C, stable for weeks without appreciable loss of activity
-
-80C, purified enzyme, 25 mM Tris-HCl, pH 8.0, stable for more than 6 months
-
-80C, stable for prolonged periods in 20 mM Tris-HCl, pH 8.0, containing 5 mM CaCl2
-
4C, 1% Triton X-100, 10 mM benzaldehyde, pH 4.0, several weeks, no loss of activity
4C, purified enzyme, few days, remains stable
-
4C, stable for several weeks
-
4C, stable for several weeks without appreciable loss of activity
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
; native enzyme 130fold from membranes of glycerol-grown cells by two different steps of anion exchange chromatography, solubilization with 0.1% Triton X-100 or Tween 20, copurification with a cytochrome c
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DEAE Toyo-Pearl 650M column chromatography and Sephadex G-100 gel filtration
-
native enzyme 211fold to homogeneity
-
native enzyme 37fold to near homogeneity by ammonium sulfate fractionation and anion exchange chromatography
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native isozyme ADH I, a procedure using anion exchange and hydrophobic interaction chromatographies with elution buffers containing 50% glycerol or PEG 600, ultrafiltration, and gel filtration, overview; native isozyme ADH IIB, a procedure using anion exchange and hydrophobic interaction chromatographies with elution buffers containing 50% glycerol or PEG 600, ultrafiltration, and gel filtration, overview; native isozyme ADH IIG, a procedure using anion exchange and hydrophobic interaction chromatographies with elution buffers containing 50% glycerol or PEG 600, ultrafiltration, and gel filtration, overview
solubilization with Triton X-100, DEAE-cellulose, CM-cellulose
-
solubilization with Triton X-100/cetylpyridinium chloride, PEG precipitation, DEAE-cellulose, hydroxyapatite
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
expression in Gluconobacter sp. DSM 3504
-
gene boh, DNA and amino acid sequence determination and analysis
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
insertional disruption of boh affects, but not fully eliminates butane utilization in the mutant organism, the double boh/bdh mutant with both genes boh and bdh inactivated is unable to grow on butane or 1-butanol, but does, when grown in citrate and incubated in butane, develop butane oxidation capability and accumulates 1-butanol, overview
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Ca2+ ions facilitate the reconstitution of inactive apoenzyme
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
Show AA Sequence (248 entries)
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