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EC Number
BRENDA No.
Title
Journal
Volume
Pages
Year
Organism
PubMed ID
1.1.1.2
760724
Computational design of highly stable and soluble alcohol dehydrogenase for NADPH regeneration
Bioresour. Bioprocess.
8
12
2021
Clostridium beijerinckii
-
1.1.1.2
760278
Engineering an alcohol dehydrogenase for balancing kinetics in NADPH regeneration with 1,4-butanediol as a cosubstrate
ACS Sust. Chem. Eng.
7
15706-15714
2019
Vanderwaltozyma polyspora
-
1.1.1.2
746361
Engineering the cofactor specificity of an alcohol dehydrogenase via single mutations or insertions distal to the 2'-phosphate group of NADP(H)
Protein Eng. Des. Sel.
30
373-380
2017
Pyrococcus furiosus
28201792
1.1.1.2
744084
Stabilization of enzymes against thermal stress and freeze-drying by mannosylglycerate
Appl. Environ. Microbiol.
63
4020-4025
1997
Pyrococcus furiosus
16535713
1.1.1.2
760299
The structure of an iron-containing alcohol dehydrogenase from a hyperthermophilic archaeon in two chemical states
Acta Crystallogr. Sect. F
75
217-226
2019
Thermococcus thioreducens
30950821
1.1.1.2
763448
Two novel metal-independent long-chain alkyl alcohol dehydrogenases from Geobacillus thermodenitrificans NG80-2
Microbiology
155
2078-2085
2009
Geobacillus thermodenitrificans
19383697
1.1.1.2
763448
Two novel metal-independent long-chain alkyl alcohol dehydrogenases from Geobacillus thermodenitrificans NG80-2
Microbiology
155
2078-2085
2009
Geobacillus thermodenitrificans NG80-2
19383697
1.1.1.2
698097
A novel NADPH-dependent aldehyde reductase gene from Saccharomyces cerevisiae NRRL Y-12632 involved in the detoxification of aldehyde inhibitors derived from lignocellulosic biomass conversion
Gene
446
1-10
2009
Saccharomyces cerevisiae
19577617
1.1.1.2
698097
A novel NADPH-dependent aldehyde reductase gene from Saccharomyces cerevisiae NRRL Y-12632 involved in the detoxification of aldehyde inhibitors derived from lignocellulosic biomass conversion
Gene
446
1-10
2009
Saccharomyces cerevisiae NRRL Y-12632
19577617
1.1.1.2
286194
A novel NADPH-dependent aldehyde reductase, catalyzing asymmetric reduction of beta-keto acid esters, from Sporobolomyces salmonicolor: purification and characterization
FEMS Microbiol. Lett.
70
45-48
1990
Sporidiobolus salmonicolor
-
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