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Information on EC 1.1.1.80 - isopropanol dehydrogenase (NADP+) and Organism(s) Thermoanaerobacter brockii and UniProt Accession P14941

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IUBMB Comments
Also acts on other short-chain secondary alcohols and, slowly, on primary alcohols.
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Thermoanaerobacter brockii
UNIPROT: P14941
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The taxonomic range for the selected organisms is: Thermoanaerobacter brockii
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
Synonyms
s-adh, isopropanol dehydrogenase, nadph-dependent primary-secondary alcohol dehydrogenase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
NADP-dependent isopropanol dehydrogenase
UniProt
isopropanol dehydrogenase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
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oxidation
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reduction
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PATHWAY SOURCE
PATHWAYS
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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.
CAS REGISTRY NUMBER
COMMENTARY hide
37250-18-3
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-butanone + NADPH + H+
2-butanol + NADP+
show the reaction diagram
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r
4-phenyl-2-butanone + NADPH + H+
4-phenyl-2-butanol + NADP+
show the reaction diagram
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r
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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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADPH
additional information
no cofactor: NADH
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
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
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
ADH_THEBR
352
0
37647
Swiss-Prot
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
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
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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)
Manually annotated by BRENDA team
Morra, S.; Pordea, A.
Biocatalyst-artificial metalloenzyme cascade based on alcohol dehydrogenase
Chem. Sci.
9
7447-7454
2018
Thermoanaerobacter brockii (P14941)
Manually annotated by BRENDA team