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; |
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Note: Use your mouse to drag, rotate, and zoom in and out of the structure. Mouse-over to identify atoms and bonds. Mouse controls documentation.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 |
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 |
Reaction | ![]() |
Core-to-Core |
Title | Authors | Date | PubMed ID |
---|---|---|---|
Purification and characterization of a primary-secondary alcohol dehydrogenase from two strains of Clostridium beijerinckii. | Ismaiel AA, Zhu CX, Colby GD, Chen JS | 1993 Aug | 8349550 |
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 Y | 2010 Mar 9 | 20102159 |