Any feedback?
Information on EC 1.1.9.1 - alcohol dehydrogenase (azurin)
for references in articles please use BRENDA:EC1.1.9.1Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
1.1.9.1 alcohol dehydrogenase (azurin)IUBMB Comments
A soluble, periplasmic PQQ-containing quinohemoprotein. Also contains a single heme c. Occurs in Comamonas and Pseudomonas. Does not require an amine activator. Oxidizes a wide range of primary and secondary alcohols, and also aldehydes and large substrates such as sterols; methanol is not a substrate. Usually assayed with phenazine methosulfate or ferricyanide. Like all other quinoprotein alcohol dehydrogenases it has an 8-bladed 'propeller' structure, a calcium ion bound to the PQQ in the active site and an unusual disulfide ring structure in close proximity to the PQQ.
Specify your search results
The enzyme appears in viruses and cellular organisms
Synonyms
ADH IIB, ADH IIG, EC 1.1.98.1, QH-ADH, quinohaemoprotein alcohol dehydrogenase, quinohemoprotein alcohol dehydrogenase, 
more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ADH IIB
ADH IIG
EC 1.1.98.1
-
-
formerly
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a primary alcohol + azurin = an aldehyde + reduced azurin
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
alcohol:azurin oxidoreductase
A soluble, periplasmic PQQ-containing quinohemoprotein. Also contains a single heme c. Occurs in Comamonas and Pseudomonas. Does not require an amine activator. Oxidizes a wide range of primary and secondary alcohols, and also aldehydes and large substrates such as sterols; methanol is not a substrate. Usually assayed with phenazine methosulfate or ferricyanide. Like all other quinoprotein alcohol dehydrogenases it has an 8-bladed 'propeller' structure, a calcium ion bound to the PQQ in the active site and an unusual disulfide ring structure in close proximity to the PQQ.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
(R)-2-butanol + ferricyanide
butan-2-one + ferrocyanide
-
enzyme electrode, 6.5% of vmax with 1-butanol, soluble enzyme, 6% of vmax with 1-butanol. With enzyme electrode, (S)-enantiomer is 13fold preferred over (R)-enantiomer, with soluble enzyme 13.5fold, respectively
-
-
?
(R)-2-heptanol + ferricyanide
heptan-2-one + ferrocyanide
-
enzyme electrode, 10% of vmax with 1-butanol, soluble enzyme, 5.5% of vmax with 1-butanol. With enzyme electrode, (S)-enantiomer is 82fold preferred over (R)-enantiomer, with soluble enzyme 315fold, respectively
-
-
?
(R)-2-hexanol + ferrocyanide
hexan-2-one + ferricyanide
-
enzyme electrode, 14% of vmax with 1-butanol, soluble enzyme, 9% of vmax with 1-butanol. With enzyme electrode, (S)-enantiomer is 35fold preferred over (R)-enantiomer, with soluble enzyme 105fold, respectively
-
-
?
(R)-2-octanol + ferrocyanide
octan-2-one + ferricyanide
-
enzyme electrode, 8% of vmax with 1-butanol. With enzyme electrode, (S)-enantiomer is 82fold preferred over (R)-enantiomer, with soluble enzyme 800fold, respectively
-
-
?
(R)-3-bromo-2-methyl-1-propanol + ferricyanide
(R)-3-bromo-2-methyl-propanal + ferrocyanide
-
-
-
-
r
(R)-glycidol + ferrocyanide
? + ferricyanide
-
enzyme electrode, 37% of vmax with 1-butanol, soluble enzyme, 1.6% of vmax with 1-butanol. With enzyme electrode, (S)-enantiomer is 0.9fold preferred over (R)-enantiomer, with soluble enzyme no distinction
-
-
?
(R)-solketal + 2 ferricyanide
(R)-solketal aldehyde + 2 ferrocyanide + 2 H+
-
(R)-enantiomer is prefered, enantiomeric ratio is 30
-
-
r
(R)-solketal + ferrocyanide
? + ferricyanide
-
enzyme electrode, 35% of vmax with 1-butanol, soluble enzyme, 10% of vmax with 1-butanol. With enzyme electrode, (S)-enantiomer is 39fold preferred over (R)-enantiomer, with soluble enzyme 117fold, respectively
-
-
?
(S)-2-butanol + ferricyanide
butan-2-one + ferrocyanide
-
enzyme electrode, 14% of vmax with 1-butanol, soluble enzyme, 13% of vmax with 1-butanol. With enzyme electrode, (S)-enantiomer is 13fold preferred over (R)-enantiomer, with soluble enzyme 13.5fold, respectively
-
-
?
(S)-2-heptanol + ferricyanide
heptan-2-one + ferrocyanide
-
enzyme electrode, 70% of vmax with 1-butanol, soluble enzyme, 63% of vmax with 1-butanol. With enzyme electrode, (S)-enantiomer is 82fold preferred over (R)-enantiomer, with soluble enzyme 315fold, respectively
-
-
?
(S)-2-hexanol + ferrocyanide
hexan-2-one + ferricyanide
-
enzyme electrode, 74% of vmax with 1-butanol, soluble enzyme, 71% of vmax with 1-butanol. With enzyme electrode, (S)-enantiomer is 35fold preferred over (R)-enantiomer, with soluble enzyme 105fold, respectively
-
-
?
(S)-2-octanol + ferrocyanide
octan-2-one + ferricyanide
-
enzyme electrode, 82% of vmax with 1-butanol, soluble enzyme, 80% of vmax with 1-butanol. With enzyme electrode, (S)-enantiomer is 82fold preferred over (R)-enantiomer, with soluble enzyme 800fold, respectively
-
-
?
(S)-glycidol + ferrocyanide
? + ferricyanide
-
enzyme electrode, 30% of vmax with 1-butanol, soluble enzyme, 1.6% of vmax with 1-butanol. With enzyme electrode, (S)-enantiomer is 0.9fold preferred over (R)-enantiomer, with soluble enzyme no disticnction
-
-
?
(S)-solketal + 2 ferricyanide
(S)-solketal aldehyde + 2 ferrocyanide + 2 H+
-
the second step in (S)-solketal conversion is much faster than the first one and that opposite enantiomeric preferences exist for the alcohol and the aldehyde substrates. (R)-enantiomer is prefered, enantiomeric ratio is 30 for initial rate measurement, 117 for progress curve analysis
-
-
r
(S)-solketal + ferrocyanide
? + ferricyanide
-
enzyme electrode, 9% of vmax with 1-butanol, 0.7% of vmax with 1-butanol. With enzyme electrode, (S)-enantiomer is 39fold preferred over (R)-enantiomer, with soluble enzyme 117fold, respectively
-
-
?
1,2-butanediol + ferricyanide
2-hydroxybutanal + ferrocyanide
-
ADH IIB, 84% of the activity with 1-butanol. ADH IIG, 86% of the activity with 1,2-propanediol
-
-
?
1,2-cyclohexanediol + ferricyanide
2-hydroxycyclohexanone + ferrocyanide
-
-
-
-
?
1,2-ethanediol + ferricyanide
hydroxyacetaldehyde + ferrocyanide
-
ADH IIB, 0% of the activity with 1-butanol. ADH IIG, 71% of the activity with 1,2-propanediol
-
-
?
1,2-propanediol + ferricyanide
2-hydroxypropanal + ferrocyanide
-
ADH IIB, 43% of the activity with 1-butanol. ADH IIG, maximum activity
-
-
?
1,3-butanediol + ferricyanide
3-hydroxybutanal + ferrocyanide
-
ADH IIB, 105% of the activity with 1-butanol. ADH IIG, 75% of the activity with 1,2-propanediol
-
-
?
1,3-butanediol + ferricyanide
? + ferrocyanide
-
enzyme electrode, 91% of vmax with 1-butanol
-
-
?
1,3-cyclohexanediol + ferricyanide
3-hydroxycyclohexanone + ferrocyanide
-
-
-
-
?
1,3-propandione + ferricyanide
3-hydroxypropanal + ferrocyanide
-
ADH IIB, 61% of the activity with 1-butanol. ADH IIG, 42% of the activity with 1,2-propanediol
-
-
?
1,4-butanediol + ferricyanide
4-hydroxybutanal + ferrocyanide
-
ADH IIB, 110% of the activity with 1-butanol. ADH IIG, 75% of the activity with 1,2-propanediol
-
-
?
1-butanol + N,N,N',N'-tetramethyl-p-phenylenediamine
butanal + ?
-
-
-
-
r
1-heptanol + ferricyanide
heptanal + ferrocyanide
-
ADH IIB, 99% of the activity with 1-butanol. ADH IIG, 39% of the activity with 1,2-propanediol
-
-
?
1-hexanol + ferricyanide
hexanal + ferrocyanide
-
ADH IIB, 70% of the activity with 1-butanol. ADH IIG, 46% of the activity with 1,2-propanediol
-
-
?
1-octanol + ferrocyanide
octanal + ferricyanide
-
enzyme electrode, 95% of vmax with 1-butanol, soluble enzyme, 95% of vmax with 1-butanol
-
-
?
1-octanol + N,N,N',N'-tetramethyl-p-phenylenediamine
octanal + ?
-
-
-
-
r
1-pentanol + ferrocyanide
pentanal + ferricyanide
-
enzyme electrode, 93% of vmax with 1-butanol, soluble enzyme, 100% of vmax with 1-butanol
-
-
?
1-pentanol + N,N,N',N'-tetramethyl-p-phenylenediamine
pentanal + ?
-
-
-
-
r
1-propanol + N,N,N',N'-tetramethyl-p-phenylenediamine
propanal + ?
-
-
-
-
r
2,3-butanediol + ferricyanide
3-hydroxybutan-2-one + ferrocyanide
-
ADH IIB, 12% of the activity with 1-butanol. ADH IIG, 71% of the activity with 1,2-propanediol
-
-
?
2,4-pentanediol + ferricyanide
4-hydroxypentan-2-one + ferrocyanide
-
ADH IIB, 45% of the activity with 1-butanol. ADH IIG, 0% of the activity with 1,2-propanediol
-
-
?
2-butanol + ferrocyanide
butanone + ferricyanide
-
enzyme electrode, 17% of vmax with 1-butanol, soluble enzyme, 10% of vmax with 1-butanol
-
-
?
2-hexanol + ferricyanide
hexan-2-one + ferrocyanide
-
ADH IIB, 99% of the activity with 1-butanol. ADH IIG, 33% of the activity with 1,2-propanediol
-
-
?
2-methylcyclohexanol + ferricyanide
2-methylcyclohexanone + ferrocyanide
-
-
-
-
?
2-octanol + ferrocyanide
octan-2-one + ferricyanide
-
enzyme electrode, 84% of vmax with 1-butanol, soluble enzyme, 80% of vmax with 1-butanol
-
-
?
2-pentanol + ferrocyanide
pentan-2-one + ferricyanide
-
enzyme electrode, 40% of vmax with 1-butanol, soluble enzyme, 34% of vmax with 1-butanol
-
-
?
2-propanol + ferrocyanide
acetone + ferricyanide
-
enzyme electrode, 9% of vmax with 1-butanol, soluble enzyme, 6% of vmax with 1-butanol
-
-
?
3-heptanol + ferrocyanide
heptan-3-one + ferricyanide
-
enzyme electrode, 3.7% of vmax with 1-butanol, soluble enzyme, 1% of vmax with 1-butanol
-
-
?
3-hexanol + ferrocyanide
hexan-3-one + ferricyanide
-
enzyme electrode, 6.5% of vmax with 1-butanol, soluble enzyme, 9% of vmax with 1-butanol
-
-
?
3-methylcyclohexanol + ferricyanide
3-methylcyclohexanone + ferrocyanide
-
-
-
-
?
3-octanol + ferrocyanide
octan-3-one + ferricyanide
-
enzyme electrode, 10% of vmax with 1-butanol, soluble enzyme, 10% of vmax with 1-butanol
-
-
?
3-pentanol + ferrocyanide
pentan-3-one + ferricyanide
-
enzyme electrode, 1% of vmax with 1-butanol, soluble enzyme, 1.4% of vmax with 1-butanol
-
-
?
4-methyl-2-pentanol + ferricyanide
4-methylpentan-2-one + ferrocyanide
-
enzyme electrode, 5.6% of vmax with 1-butanol
-
-
?
5-methyl-2-hexanol + ferricyanide
5-methylhexan-2-one + ferrocyanide
-
-
-
-
r
6-aminohexan-1-ol + N,N,N',N'-tetramethyl-p-phenylenediamine
6-aminohexanal + ?
-
-
-
-
r
acetaldehyde + reduced N,N,N',N'-tetramethyl-p-phenylenediamine
ethanol + N,N,N',N'-tetramethyl-p-phenylenediamine
-
-
-
-
r
allyl alcohol + ferricyanide
prop-2-enal + ferrocyanide
-
ADH IIB, 160% of the activity with 1-butanol. ADH IIG, 46% of the activity with 1,2-propanediol
-
-
?
benzyl alcohol + N,N,N',N'-tetramethyl-p-phenylenediamine
benzaldehyde + ?
-
-
-
-
r
butanal + ferrocyanide
1-butanol + ferricyanide
-
ADH IIB, 32% of the activity with 1-butanol. ADH IIG, 13% of the activity with 1,2-propanediol
-
-
?
butanal + reduced N,N,N',N'-tetramethyl-p-phenylenediamine
1-butanol + N,N,N',N'-tetramethyl-p-phenylenediamine
-
-
-
-
r
butane-1,3-diol + N,N,N',N'-tetramethyl-p-phenylenediamine
?
-
-
-
-
r
cyclohexanol + ferricyanide
cyclohexanone + ferrocyanide
-
enzyme electrode, 11% of vmax with 1-butanol, soluble enzyme, 9% of vmax with 1-butanol
-
-
?
ethanol + cytochrome c
ethanal + reduced cytochrome c
-
5% of the activity with Wurster's Blue. In presence of phenazine methosulfate, 60% of the activity with Wurster's Blue
-
-
r
ethanol + N,N,N',N'-tetramethyl-p-phenylenediamine
ethanal + ?
-
i.e. Wurster's Blue
-
-
?
ethanol + oxidized 2,6-dichlorophenolindophenol
ethanal + reduced 2,6-dichlorophenolindophenol
-
10% of the activity with Wurster's Blue. In presence of phenazine methosulfate, 75% of the activity with Wurster's Blue
-
-
r
formaldehyde + N,N,N',N'-tetramethyl-p-phenylenediamine
methanol + ?
-
-
-
-
r
glycerol + ferrocyanide
2,3-dihydroxypropanal + ferricyanide
-
ADH IIB, 0% of the activity with 1-butanol. ADH IIG, 63% of the activity with 1,2-propanediol
-
-
?
iso-amyl alcohol + ferricyanide
3-methylbutanol + ferrocyanide
-
ADH IIB, 100% of the activity with 1-butanol. ADH IIG, 93% of the activity with 1,2-propanediol
-
-
?
octanal + reduced N,N,N',N'-tetramethyl-p-phenylenediamine
1-octanol + N,N,N',N'-tetramethyl-p-phenylenediamine
-
-
-
-
r
propanal + ferrocyanide
1-propanol + ferricyanide
-
ADH IIB, 125% of the activity with 1-butanol. ADH IIG, 58% of the activity with 1,2-propanediol
-
-
?
rac-2,2-dimethyl-4-hydroxymethyl-1,3-dioxolane + ferricyanide
? + ferrocyanide
-
i.e. solketal. Enantiomeric ratio is 30 for solketal and 6 for rac-2,2-dimethyl-4-[1,1-2H]hydroxymethyl-1,3-[5,5,4-2H]dioxolane, d5-solketal. Isotopic substitution affects the relative kinetic weights of the initial hydron/deuteron transfer from substrate to cofactor and the subsequent proton/deuteron shift in the cofactor-product complex
-
-
?
(R)-solketal aldehyde + ferrocyanide
(R)-solketal + ferricyanide
-
-
-
-
r
(R)-solketal aldehyde + ferrocyanide
(R)-solketal + ferricyanide
-
(R)-enantiomer is prefered, enantiomeric ratio is 2.8 for initial rate measurement
-
-
r
1-butanol + ferricyanide
butanal + ferrocyanide
-
maximum velocity rate for both enzyme electrode and soluble enzyme
-
-
?
1-butanol + ferricyanide
butanal + ferrocyanide
-
ADH IIG, 42% of the activity with 1,2-propanediol
-
-
?
1-octanol + ferricyanide
octanal + ferrocyanide
-
ADH IIB, 44% of the activity with 1-butanol. ADH IIG, 24% of the activity with 1,2-propanediol
-
-
?
1-pentanol + ferricyanide
pentanal + ferrocyanide
-
ADH IIB, 100% of the activity with 1-butanol. ADH IIG, 40% of the activity with 1,2-propanediol
-
-
?
1-propanol + ferricyanide
propanal + ferrocyanide
-
enzyme electrode, 93% of vmax with 1-butanol, soluble enzyme, 90% of vmax with 1-butanol
-
-
?
1-propanol + ferricyanide
propanal + ferrocyanide
-
ADH IIB, 70% of the activity with 1-butanol. ADH IIG, 41% of the activity with 1,2-propanediol
-
-
?
2-butanol + ferricyanide
butanone + ferrocyanide
-
ADH IIB, 90% of the activity with 1-butanol. ADH IIG, 15% of the activity with 1,2-propanediol
-
-
?
2-pentanol + ferricyanide
pentan-2-one + ferrocyanide
-
ADH IIB, 120% of the activity with 1-butanol. ADH IIG, 19% of the activity with 1,2-propanediol
-
-
?
2-propanol + ferricyanide
acetone + ferrocyanide
-
ADH IIB, 52% of the activity with 1-butanol. ADH IIG, 0% of the activity with 1,2-propanediol
-
-
?
3-methyl-2-pentanol + ferricyanide
3-methylpentan-2-one + ferrocyanide
-
enzyme electrode, 3.7% of vmax with 1-butanol
-
-
?
3-methyl-2-pentanol + ferricyanide
3-methylpentan-2-one + ferrocyanide
-
enzyme electrode, 9.3% of vmax with 1-butanol
-
-
?
3-nonanol + ferricyanide
nonan-3-one + ferrocyanide
-
enzyme electrode, 4.7% of vmax with 1-butanol, soluble enzyme, 4.5% of vmax with 1-butanol
-
-
?
3-pentanol + ferricyanide
pentan-3-one + ferrocyanide
-
ADH IIB, 43% of the activity with 1-butanol. ADH IIG, 15% of the activity with 1,2-propanediol
-
-
?
4-decanol + ferricyanide
decan-4-one + ferrocyanide
-
enzyme electrode, 3.7% of vmax with 1-butanol, soluble enzyme, 3.6% of vmax with 1-butanol
-
-
?
4-heptanol + ferricyanide
heptan-4-one + ferrocyanide
-
enzyme electrode, 9.3% of vmax with 1-butanol, soluble enzyme, 10% of vmax with 1-butanol
-
-
?
ethanal + ferrocyanide
ethanol + ferricyanide
-
ADH IIB, 78% of the activity with 1-butanol. ADH IIG, 16% of the activity with 1,2-propanediol
-
-
?
ethanol + ferricyanide
ethanal + ferrocyanide
-
100% of the activity with Wurster's Blue
-
-
r
ethanol + ferricyanide
ethanal + ferrocyanide
-
86% of vmax with 1-butanol, soluble enzyme, 75% of vmax with 1-butanol
-
-
?
ethanol + ferricyanide
ethanal + ferrocyanide
-
ADH IIB, 78% of the activity with 1-butanol. ADH IIG, 22% of the activity with 1,2-propanediol
-
-
?
additional information
?
-
-
no substrate: D-glucose, D-galactose, D-fructose, Alpha-D-methylglucoside, mannitol
-
-
?
additional information
?
-
-
The affinity of the enzyme for aliphatic alcohols increases with the chain length of the substrate. The same property is observed for secondary alcohols in the series 2-propanol to 2-octanol
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
heme
-
binding of pyrroloquinoline quinone induces shifts in the resonances of the methyl groups of the heme porphyrin ring in the oxidized form of the apoenzyme and a shift in the methionine heme ligand resonance of the reduced form of the apoenzyme. A major effect of pyrroloquinoline quinone binding to apo-QH-EDH is a rotation of the methionine ligand of heme c. Pyrroloquinoline quinone becomes tightly bound, the event leading to a compact enzyme conformation which is able to catalyze rapid intramolecular electron transfer
heme
-
holoenzyme contains equimolar amounts of pyrroloquinoline quinone, Ca2+ and covalently bound heme. Low-spin heme protein
heme
-
in the crystals, the four hemes in the unit cell have only two different orientations, related by an 180° rotation about the b axis. The heme rings are oriented parallel to the b axis
pyrroloquinoline quinone
-
binding of pyrroloquinoline quinone induces shifts in the resonances of the methyl groups of the heme porphyrin ring in the oxidized form of the apoenzyme and a shift in the methionine heme ligand resonance of the reduced form of the apoenzyme. A major effect of pyrroloquinoline quinone binding to apo-QH-EDH is a rotation of the methionine ligand of heme c. Pyrroloquinoline quinone becomes tightly bound, the event leading to a compact enzyme conformation which is able to catalyze rapid intramolecular electron transfer
pyrroloquinoline quinone
-
holoenzyme contains equimolar amounts of pyrroloquinoline quinone, Ca2+ and covalently bound heme. Reconstitution of apoenzyme with pyrroloquinoline quinone analogues results in a decreased activity and enantioselectivity for the oxidation of chiral alcohols. Possession of the o-quinone or o-quinol moiety is not essential for binding but it is for activity
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Ca2+
-
holoenzyme contains equimolar amounts of pyrroloquinoline quinone, Ca2+ and covalently bound heme
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.75
4-methyl-2-pentanol
-
enzyme electrode, pH 7.7, presence of CaCl2
0.24
5-methyl-2-hexanol
-
enzyme electrode, pH 7.7, presence of CaCl2
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE