Any feedback?
No. of entries
Information on EC 1.1.1.80 - isopropanol dehydrogenase (NADP+)
for references in articles please use BRENDA:EC1.1.1.80
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree 1 Oxidoreductases
1.1 Acting on the CH-OH group of donors
1.1.1 With NAD+ or NADP+ as acceptor
1.1.1.80 isopropanol dehydrogenase (NADP+)
IUBMB Comments
Also acts on other short-chain secondary alcohols and, slowly, on primary alcohols.
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
- 1.1.1.80
- acetone
-
biocatalyst
-
diode
-
biofuels
- autoethanogenum
- 2-propanol
- 2,3-butanediol
-
acetogenic
-
biocatalytic
-
emitted
-
nadh-dependent
- n-butanol
- diagnostics
showSynonyms
s-adh, isopropanol dehydrogenase, nadph-dependent primary-secondary 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
IDH
isopropanol dehydrogenase
NADPH-dependent primary-secondary alcohol dehydrogenase
isopropanol dehydrogenase
-
-
-
-
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
propan-2-ol + NADP+ = acetone + NADPH + H+
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
MetaCyc
acetone degradation I (to methylglyoxal), acetone degradation II (to acetoacetate), acetone degradation III (to propane-1,2-diol), isopropanol biosynthesis (engineered)
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
propan-2-ol:NADP+ oxidoreductase
Also acts on other short-chain secondary alcohols and, slowly, on primary alcohols.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
37250-18-3
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-butanone + NADPH + H+
2-butanol + NADP+
Substrates: -
Products: -
Products: -
r
4-methyl-1-pentanol + NAD+
4-methyl-1-pentanal + NADH
-
Substrates: -
Products: -
Products: -
?
4-methyl-1-pentanol + NADP+
4-methyl-1-pentanal + NADPH
-
Substrates: -
Products: -
Products: -
?
4-phenyl-2-butanone + NADPH + H+
4-phenyl-2-butanol + NADP+
Substrates: -
Products: -
Products: -
r
6-methyl-2-heptanol + NAD+
6-methyl-2-heptanone + NADH + H+
-
Substrates: -
Products: -
Products: -
?
6-methyl-2-heptanol + NADP+
6-methyl-2-heptanone + NADPH
-
Substrates: -
Products: -
Products: -
?
acetaldehyde + NADPH + H+
ethanol + NADP+
Substrates: -
Products: -
Products: -
r
butan-2-ol + NADP+
butanone + NADPH + H+
Substrates: preferred direction of the reaction is reduction rather than oxidation
Products: -
Products: -
r
butanone + NADPH + H+
butan-2-ol + NADP+
Substrates: -
Products: -
Products: -
r
ethanol + NADP+
acetaldehyde + NADPH + H+
Substrates: -
Products: -
Products: -
r
pentan-2-ol + NADP+
pentan-2-one + NADPH + H+
Substrates: -
Products: -
Products: -
r
pentan-3-ol + NADP+
pentan-3-one + NADPH + H+
Substrates: -
Products: -
Products: -
r
pentan-3-one + NADPH + H+
pentan-3-ol + NADP+
Substrates: -
Products: -
Products: -
r
propan-1-ol + NADP+
propanal + NADPH + H+
Substrates: -
Products: -
Products: -
r
propan-2-ol + NAD+
acetone + NADH
-
Substrates: NAD+ effectively substitutes for NADP+
Products: -
Products: -
?
acetone + NADPH + H+
propan-2-ol + NADP+
-
Substrates: -
Products: -
Products: -
?
acetone + NADPH + H+
propan-2-ol + NADP+
-
Substrates: -
Products: -
Products: -
?
acetone + NADPH + H+
propan-2-ol + NADP+
Substrates: -
Products: -
Products: -
r
n-butanol + NAD+
butanone + NADH + H+
-
Substrates: -
Products: -
Products: -
?
n-butanol + NADP+
butanone + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
propan-2-ol + NAD+
acetone + NADH + H+
-
Substrates: -
Products: -
Products: -
?
propan-2-ol + NADP+
acetone + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
propan-2-ol + NADP+
acetone + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
propan-2-ol + NADP+
acetone + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
propan-2-ol + NADP+
acetone + NADPH + H+
Substrates: preferred direction of the reaction is reduction rather than oxidation
Products: -
Products: -
r
additional information
?
-
-
Substrates: also acts on short-chain secondary alcohols and, slowly, on primary alcohols
Products: -
Products: -
?
additional information
?
-
-
Substrates: possibly takes part in the further metabolic reactions of the fragments formed from the side-chain of the steroid hormone precursor in the adrenals or gonads
Products: -
Products: -
?
additional information
?
-
Substrates: enzyme transfers the pro-R hydrogen from the pyridine 4 position of the reduced coenzyme. This stereospecificity is stable over a broad range of temperatures up to 70°C and different concentrations of the coenzyme (catalytic or stoichiometric). NADP+ and its synthetic analogs, 3-acetylpyridine-ADP+ and thio-NADP+, can be used successfully
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
butan-2-ol + NADP+
butanone + NADPH + H+
Substrates: preferred direction of the reaction is reduction rather than oxidation
Products: -
Products: -
r
propan-2-ol + NADP+
acetone + NADPH + H+
Substrates: preferred direction of the reaction is reduction rather than oxidation
Products: -
Products: -
r
additional information
?
-
-
Substrates: possibly takes part in the further metabolic reactions of the fragments formed from the side-chain of the steroid hormone precursor in the adrenals or gonads
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADPH
enzyme transfers the pro-R hydrogen from the pyridine 4 position of the reduced coenzyme. This stereospecificity is stable over a broad range of temperatures up to 70°C and different concentrations of the coenzyme (catalytic or stoichiometric)
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
Zn2+
required, analysis of the zion ion bound in the crystal structure of TbADH complexed to NADP+ (PDB ID 1YKF)
additional information
replacement of the zinc from Thermoanaerobacter brockii alcohol dehydrogenase (TbADH) with Rh(III) catalysts possessing nitrogen donor ligands, by covalent conjugation to the active site cysteine, to create artificial metalloenzymes for NADP+ reduction. Compatibility between bioconjugated Rh catalysts and TbADH, overview. Formate dehydrogenase activity of artificial brominated metalloenzymes is observed
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
0.03
propan-2-ol
-
pH 7.0, temperature not specified in the publication
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
0.066
propan-2-ol
-
pH 7.0, temperature not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2.36
propan-2-ol
-
pH 7.0, temperature not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
35 - 50
-
35°C: about 70% of maximal activity, 50°C: about 60% of maximal activity, substrate: n-butanol
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
additional information
replacment of the zinc from Thermoanaerobacter brockii alcohol dehydrogenase (TbADH) with Rh(III) catalysts possessing nitrogen donor ligands, by covalent conjugation to the active site cysteine, to create artificial metalloenzymes for NADP+ reduction. TbADH is used as protein scaffold for both alcohol synthesis and the recycling of the cofactor, by combination of the chemically modified species with the non-modified recombinant enzyme. Stability studies reveal that the incorporation of the catalysts into the TbADH pocket provides a shielding environment for the metal catalyst, resulting in increased stability of both the recycling catalyst and the ADH. The reduction of a representative ketone using this modified alcohol dehydrogenase-artificial formate dehydrogenase cascade yields better conversions than in the presence of free metal catalyst. Active site residues are H59 and D150, engineering of TbADH for the covalent binding of small molecules into the active site. Reduction of a model ketone using a native-artificial enzyme cascade with the same alcohol dehydrogenase scaffold, modeling, overview
evolution
-
an evolutionary tree is constructed to analyze the evolution of the enzyme illustrates that the isopropanol dehydrogenase from Aspergillus fumigatus Af293 is far from to other dehydrogenases
evolution
-
an evolutionary tree is constructed to analyze the evolution of the enzyme illustrates that the isopropanol dehydrogenase from Aspergillus fumigatus Af293 is far from to other dehydrogenases
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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). ADH1_ENTH1
Entamoeba histolytica (strain ATCC 30459 / HM-1:IMSS / ABRM)
366
0
39215
Swiss-Prot
Secretory Pathway (Reliability: 1)
ADH_MYCPN
Mycoplasma pneumoniae (strain ATCC 29342 / M129 / Subtype 1)
351
0
37812
Swiss-Prot
-
A2DJ40_TRIV3
Trichomonas vaginalis (strain ATCC PRA-98 / G3)
365
0
39155
TrEMBL
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PDB
SCOP
CATH
UNIPROT
ORGANISM
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
replacement of the zinc from Thermoanaerobacter brockii alcohol dehydrogenase (TbADH) with Rh(III) catalysts possessing nitrogen donor ligands, by covalent conjugation to the active site cysteine, to create artificial metalloenzymes for NADP+ reduction. TbADH is used as protein scaffold for both alcohol synthesis and the recycling of the cofactor, by combination of the chemically modified species with the non-modified recombinant enzyme. Stability studies reveal that the incorporation of the catalysts into the TbADH pocket provides a shielding environment for the metal catalyst, resulting in increased stability of both the recycling catalyst and the ADH. The reduction of a representative ketone using this modified alcohol dehydrogenase-artificial formate dehydrogenase cascade yields better conversions than in the presence of free metal catalyst
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.6
-
without any stabilizer, the enzyme at pH 5.6 and 7.0 retains over 25% of its maximum activity after pre-treated in different buffers ranging from pH 5.6-10.0 for 27 h at 4°C
7
-
without any stabilizer, the enzyme at pH 5.6 and 7.0 retains over 25% of its maximum activity after pre-treated in different buffers ranging from pH 5.6-10.0 for 27 h at 4°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25 - 45
-
incubation for 1 h under pH 6.0, the enzyme shows over 43% of the maximal activity between 25°C and 30°C
40 - 45
-
incubation for 1 h under pH 6.0, the enzyme shows less than 10% of the maximal activity between 25°C and 30°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Acetone
acetonitrile
acetophenone
-
strong stability in the presence of acetophenone at concentrations of 10% (v/v)
Ethanol
isopropanol
Methanol
Acetone
-
in the presence of isopropanol, acetonitrile, and acetone at 10% (v/v) or 30% (v/v), the enzyme exhibits over 45% of its maximum activity
Acetone
-
in the presence of isopropanol, acetonitrile, and acetone at 10% (v/v) or 30% (v/v), the enzyme exhibits over 45% of its maximum activity
-
acetonitrile
-
in the presence of isopropanol, acetonitrile, and acetone at 10% (v/v) or 30% (v/v), the enzyme exhibits over 45% of its maximum activity
acetonitrile
-
in the presence of isopropanol, acetonitrile, and acetone at 10% (v/v) or 30% (v/v), the enzyme exhibits over 45% of its maximum activity
-
Ethanol
-
the enzyme remains less than 20% of its maximum activity in the presence of ethanol
Ethanol
-
the enzyme remains less than 20% of its maximum activity in the presence of ethanol
-
isopropanol
-
in the presence of isopropanol, acetonitrile, and acetone at 10% (v/v) or 30% (v/v), the enzyme exhibits over 45% of its maximum activity
isopropanol
-
in the presence of isopropanol, acetonitrile, and acetone at 10% (v/v) or 30% (v/v), the enzyme exhibits over 45% of its maximum activity
-
Methanol
-
the enzyme remains less than 20% of its maximum activity in the presence of methanol
Methanol
-
the enzyme remains less than 20% of its maximum activity in the presence of methanol
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
the enzyme is an ideal candidate biocatalyst in the construction of coenzyme regeneration system and the enzymatic bioconversion of high value alcohols or other compounds
additional information
-
the enzyme is an ideal candidate biocatalyst in the construction of coenzyme regeneration system and the enzymatic bioconversion of high value alcohols or other compounds
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ploc, I.; Starka, L.
Gas chromatographic study of the histochemical reaction for isopropanol dehydrogenase
J. Chromatogr.
172
374-378
1979
Rattus norvegicus
brenda
Sutak, R.; Hrdy, I.; Dolezal, P.; Cabala, R.; Sedinova, M.; Lewin, J.; Harant, K.; Mueller, M.; Tachezy, J.
Secondary alcohol dehydrogenase catalyzes the reduction of exogenous acetone to 2-propanol in Trichomonas vaginalis
FEBS J.
279
2768-2780
2012
Trichomonas vaginalis (A2DJ40)
brenda
Peretz, M.; Bogin, O.; Keinan, E.; Burstein, Y.
Stereospecificity of hydrogen transfer by the NADP-linked alcohol dehydrogenase from the thermophilic bacterium Thermoanaerobium brockii
Int. J. Pept. Protein Res.
42
490-495
1993
Thermoanaerobacter brockii (P14941)
brenda
Koepke, M.; Gerth, M.L.; Maddock, D.J.; Mueller, A.P.; Liew, F.; Simpson, S.D.; Patrick, W.M.
Reconstruction of an acetogenic 2,3-butanediol pathway involving a novel NADPH-dependent primary-secondary alcohol dehydrogenase
Appl. Environ. Microbiol.
80
3394-3403
2014
Clostridium autoethanogenum, Clostridium autoethanogenum DSM 10061
brenda
Morra, S.; Pordea, A.
Biocatalyst-artificial metalloenzyme cascade based on alcohol dehydrogenase
Chem. Sci.
9
7447-7454
2018
Thermoanaerobacter brockii (P14941)
brenda
Jiang, W.; Fang, B.S.
Coenzyme binding site analysis of an isopropanol dehydrogenase with wide substrate spectrum and excellent organic solvent tolerance
Appl. Biochem. Biotechnol.
190
18-29
2020
Aspergillus fumigatus, Aspergillus fumigatus Af293
brenda
EXTERNAL LINKS (specific for EC-Number 1.1.1.80)
html completed
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2026.1 (March 2026)
About BRENDA
Social media
Help
Survey
Download
Contribution
Legal
Curated at
Member of
![DSMZ Digital Diversity]()
![Global Core Biodata Resource]()
![ELIXIR Core Data Resource]()
![German Network for Bioinformatics Infrastructure]()
