Enzyme

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EC Tree
     1. Oxidoreductases
        1.1 Acting on the CH-OH group of donors
            1.1.1 With NAD+ or NADP+ as acceptor
ID:1.1.1.80
Description:Isopropanol dehydrogenase (NADP(+)).
Cath: 3.40.50.720; 3.90.180.10;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 1.1.1.80
BRENDA Enzyme Link: BRENDA 1.1.1.80
KEGG Enzyme Link: KEGG1.1.1.80
BioCyc Enzyme Link: BioCyc 1.1.1.80
ExPASy Enzyme Link: ExPASy1.1.1.80
EC2PDB Enzyme Link: EC2PDB 1.1.1.80
ExplorEnz Enzyme Link: ExplorEnz 1.1.1.80
PRIAM enzyme-specific profiles Link: PRIAM 1.1.1.80
IntEnz Enzyme Link: IntEnz 1.1.1.80
MEDLINE Enzyme Link: MEDLINE 1.1.1.80
MSA:

1.1.1.80;

Phylogenetic Tree:

1.1.1.80;

Uniprot:
M-CSA:
RHEA:21792 NADP(+) + propan-2-ol = acetone + H(+) + NADPH
RULE(radius=1) [*:1]-[CH;+0:2](-[*:3])-[OH;+0:4].[*:5]-[n+;H0:6]1:[cH;+0:7]:[cH;+0:8]:[cH;+0:9]:[c;H0;+0:10](-[*:11]):[cH;+0:12]:1>>[*:1]-[C;H0;+0:2](-[*:3])=[O;H0;+0:4].[*:5]-[N;H0;+0:6]1-[CH;+0:7]=[CH;+0:8]-[CH2;+0:9]-[C;H0;+0:10](-[*:11])=[CH;+0:12]-1
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References

TitleAuthorsDatePubMed ID
Purification and characterization of a primary-secondary alcohol dehydrogenase from two strains of Clostridium beijerinckii.Ismaiel AA, Zhu CX, Colby GD, Chen JS1993 Aug8349550
Biochemical and structural properties of chimeras constructed by exchange of cofactor-binding domains in alcohol dehydrogenases from thermophilic and mesophilic microorganisms.Goihberg E, Peretz M, Tel-Or S, Dym O, Shimon L, Frolow F, Burstein Y2010 Mar 920102159