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Information on EC 1.1.1.80 - isopropanol dehydrogenase (NADP+)
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1.1.1.80 isopropanol dehydrogenase (NADP+)IUBMB Comments
Also acts on other short-chain secondary alcohols and, slowly, on primary alcohols.
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Word Map
- 1.1.1.80
- acetone
-
diode
- autoethanogenum
- 2,3-butanediol
-
emitted
-
nadh-dependent
-
biofuels
-
acetogenic
- 2-propanol
- diagnostics
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
s-adh, isopropanol dehydrogenase, nadph-dependent primary-secondary alcohol dehydrogenase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ADH
isopropanol dehydrogenase
-
-
-
-
NADPH-dependent primary-secondary alcohol dehydrogenase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
propan-2-ol + NADP+ = acetone + NADPH + H+
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-
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
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-
-
-
reduction
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-
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-
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
propan-2-ol:NADP+ oxidoreductase
Also acts on other short-chain secondary alcohols and, slowly, on primary alcohols.
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CAS REGISTRY NUMBER
COMMENTARY
37250-18-3
-
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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
butan-2-ol + NADP+
butanone + NADPH + H+
preferred direction of the reaction is reduction rather than oxidation
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-
r
propan-2-ol + NAD+
acetone + NADH
-
NAD+ effectively substitutes for NADP+
-
?
propan-2-ol + NADP+
acetone + NADPH + H+
preferred direction of the reaction is reduction rather than oxidation
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-
r
additional information
?
-
-
also acts on short-chain secondary alcohols and, slowly, on primary alcohols
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-
-
additional information
?
-
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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
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-
additional information
?
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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
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-
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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
butan-2-ol + NADP+
butanone + NADPH + H+
A2DJ40
preferred direction of the reaction is reduction rather than oxidation
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-
r
propan-2-ol + NADP+
acetone + NADPH + H+
A2DJ40
preferred direction of the reaction is reduction rather than oxidation
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-
r
additional information
?
-
-
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
-
-
-
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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)
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
Sequence
ADH_MYCPN
Mycoplasma pneumoniae (strain ATCC 29342 / M129)
351
0
37812
Swiss-Prot
A0A1U9NPW0_9BACT
354
0
37908
TrEMBL
A0A1V5VBR4_9BACT
338
0
37299
TrEMBL
A0A1V5V367_9BACT
352
0
37706
TrEMBL
A0A143XNX9_9FIRM
353
0
37730
TrEMBL
A0A1V5RL40_9CHLR
341
0
36780
TrEMBL
A0A1V6N2Z0_9EURY
355
0
37625
TrEMBL
A0A143XBG1_9ACTN
357
0
37852
TrEMBL
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PURIFICATION/commentary
ORGANISM
UNIPROT
LITERATURE
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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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
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