1.1.1.80: isopropanol dehydrogenase (NADP+)

This is an abbreviated version!
For detailed information about isopropanol dehydrogenase (NADP+), go to the full flat file.

Word Map on EC 1.1.1.80

1.1.1.80

acetone

biocatalyst

diode

biofuels

autoethanogenum

2-propanol

2,3-butanediol

acetogenic

biocatalytic

emitted

nadh-dependent

n-butanol

diagnostics

Reaction

Synonyms

ADH, IDH, isopropanol dehydrogenase, NADP-dependent isopropanol dehydrogenase, NADPH-dependent primary-secondary alcohol dehydrogenase, S-ADH, TBADH, TVAG_228780

ECTree

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+)

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Results	in table
158	AA Sequence
3	Application
1	CAS Registry Number
2	Cloned(Commentary)
8	Cofactor
1	Expression
3	General Information
1	General Stability
6	Inhibitors
2	kcat/KM [mM/s]
19	KM Value [mM]
3	Localization
2	Metals/Ions
4	Molecular Weight [Da]
3	Natural Substrates/ Products (Substrates)
11	Organic Solvent Stability
18	Organism
8	Pathway
24	PDB ID
8	pH Optimum
1	pH Range
2	pH Stability
1	Protein Variants
2	Purification (Commentary)
1	Reaction
3	Reaction Type
8	Reference
1	Source Tissue
38	Substrates and Products (Substrate)
1	Subunits
13	Synonyms
1	Systematic Name
3	Temperature Optimum [°C]
1	Temperature Range [°C]
2	Temperature Stability [°C]
2	Turnover Number [1/s]

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General Information on EC 1.1.1.80 - isopropanol dehydrogenase (NADP+)

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evolution

2 entries

additional information

Thermoanaerobacter brockii

P14941

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

760881