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UniProt functional annotation for P11766 | ||
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| UniProt code: P11766. |
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| Organism: | |
Homo sapiens (Human). |
| Taxonomy: | |
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo. |
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| Function: | |
Catalyzes the oxidation of long-chain primary alcohols and the oxidation of S-(hydroxymethyl) glutathione (PubMed:8460164). Also oxidizes long chain omega-hydroxy fatty acids, such as 20-HETE, producing both the intermediate aldehyde, 20-oxoarachidonate and the end product, a dicarboxylic acid, (5Z,8Z,11Z,14Z)-eicosatetraenedioate (PubMed:16081420). Class-III ADH is remarkably ineffective in oxidizing ethanol (PubMed:8460164). {ECO:0000269|PubMed:16081420, ECO:0000269|PubMed:8460164}. |
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| Catalytic activity: | |
Reaction=a primary alcohol + NAD(+) = an aldehyde + H(+) + NADH; Xref=Rhea:RHEA:10736, ChEBI:CHEBI:15378, ChEBI:CHEBI:15734, ChEBI:CHEBI:17478, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.1; Evidence={ECO:0000269|PubMed:8460164}; |
| Catalytic activity: | |
Reaction=a secondary alcohol + NAD(+) = a ketone + H(+) + NADH; Xref=Rhea:RHEA:10740, ChEBI:CHEBI:15378, ChEBI:CHEBI:17087, ChEBI:CHEBI:35681, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.1; Evidence={ECO:0000269|PubMed:8460164}; |
| Catalytic activity: | |
Reaction=NADP(+) + S-(hydroxymethyl)glutathione = H(+) + NADPH + S- formylglutathione; Xref=Rhea:RHEA:19981, ChEBI:CHEBI:15378, ChEBI:CHEBI:57688, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:58758; EC=1.1.1.284; Evidence={ECO:0000269|PubMed:8460164}; |
| Catalytic activity: | |
Reaction=NAD(+) + S-(hydroxymethyl)glutathione = H(+) + NADH + S- formylglutathione; Xref=Rhea:RHEA:19985, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57688, ChEBI:CHEBI:57945, ChEBI:CHEBI:58758; EC=1.1.1.284; Evidence={ECO:0000269|PubMed:8460164}; |
| Catalytic activity: | |
Reaction=20-oxo-(5Z,8Z,11Z,14Z)-eicosatetraenoate + H2O + NAD(+) = (5Z,8Z,11Z,14Z)-eicosatetraenedioate + 2 H(+) + NADH; Xref=Rhea:RHEA:39803, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:76645, ChEBI:CHEBI:76647; Evidence={ECO:0000269|PubMed:16081420}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39804; Evidence={ECO:0000305|PubMed:16081420}; |
| Catalytic activity: | |
Reaction=20-hydroxy-(5Z,8Z,11Z,14Z)-eicosatetraenoate + NAD(+) = 20- oxo-(5Z,8Z,11Z,14Z)-eicosatetraenoate + H(+) + NADH; Xref=Rhea:RHEA:39799, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:76624, ChEBI:CHEBI:76645; Evidence={ECO:0000269|PubMed:16081420}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39800; Evidence={ECO:0000305|PubMed:16081420}; |
| Cofactor: | |
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:3365377}; Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000269|PubMed:3365377}; |
| Biophysicochemical properties: | |
Kinetic parameters: KM=21 uM for 20-HETE {ECO:0000269|PubMed:16081420}; |
| Subunit: | |
Homodimer. {ECO:0000269|PubMed:9018047}. |
| Subcellular location: | |
Cytoplasm {ECO:0000305}. |
| Miscellaneous: | |
There are 7 different ADH's isozymes in human: three belongs to class-I: alpha, beta, and gamma, one to class-II: pi, one to class-III: chi, one to class-IV: ADH7 and one to class-V: ADH6. |
| Similarity: | |
Belongs to the zinc-containing alcohol dehydrogenase family. Class-III subfamily. {ECO:0000305}. |
Annotations taken from UniProtKB at the EBI.