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UniProt functional annotation for P00325 | ||
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| UniProt code: P00325. |
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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 NAD-dependent oxidation of all-trans-retinol and its derivatives such as all-trans-4-hydroxyretinol and may participate in retinoid metabolism (PubMed:15369820, PubMed:16787387). In vitro can also catalyzes the NADH-dependent reduction of all-trans- retinal and its derivatives such as all-trans-4-oxoretinal (PubMed:15369820, PubMed:16787387). Catalyzes in the oxidative direction with higher efficiency (PubMed:16787387). Has the same affinity for all-trans-4-hydroxyretinol and all-trans-4-oxoretinal (PubMed:15369820). {ECO:0000269|PubMed:15369820, ECO:0000269|PubMed:16787387}. |
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| Catalytic activity: | |
Reaction=all-trans-retinol + NAD(+) = all-trans-retinal + H(+) + NADH; Xref=Rhea:RHEA:21284, ChEBI:CHEBI:15378, ChEBI:CHEBI:17336, ChEBI:CHEBI:17898, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.105; Evidence={ECO:0000269|PubMed:16787387}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21285; Evidence={ECO:0000305|PubMed:16787387}; |
| Catalytic activity: | |
Reaction=all-trans-4-hydroxyretinol + NAD(+) = all-trans-4- hydroxyretinal + H(+) + NADH; Xref=Rhea:RHEA:55936, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:132259, ChEBI:CHEBI:139346; Evidence={ECO:0000269|PubMed:15369820}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55937; Evidence={ECO:0000305|PubMed:15369820}; |
| Catalytic activity: | |
Reaction=all-trans-4-oxoretinol + NAD(+) = all-trans-4-oxoretinal + H(+) + NADH; Xref=Rhea:RHEA:60632, ChEBI:CHEBI:15378, ChEBI:CHEBI:44597, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:139347; Evidence={ECO:0000269|PubMed:15369820}; |
| Cofactor: | |
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 2 Zn(2+) ions per subunit.; |
| Biophysicochemical properties: | |
Kinetic parameters: KM=4 uM for all-trans-4-hydroxyretinol (in allele ADH1B*1) {ECO:0000269|PubMed:15369820}; KM=25 uM for all-trans-4-oxoretinal (in allele ADH1B*1) {ECO:0000269|PubMed:15369820}; KM=11 uM for all-trans-4-hydroxyretinol (in allele ADH1B*2) {ECO:0000269|PubMed:15369820}; KM=27 uM for all-trans-4-oxoretinal (in allele ADH1B*2) {ECO:0000269|PubMed:15369820}; KM=24 uM for all-trans-3,4-didehydroretinol(in allele ADH1B*2) {ECO:0000269|PubMed:15369820}; KM=25 uM for all-trans-3,4-didehydroretinal(in allele ADH1B*2) {ECO:0000269|PubMed:15369820}; KM=0.4 uM for all-trans-retinaldehyde (in allele ADH1B*2) {ECO:0000269|PubMed:16787387}; KM=0.3 uM for all-trans-retinol (in allele ADH1B*2) {ECO:0000269|PubMed:16787387}; |
| Subunit: | |
Dimer of identical or non-identical chains of three types; alpha, beta and gamma. |
| Subcellular location: | |
Cytoplasm. |
| Polymorphism: | |
Three alleles are known: ADH1B*1 (ADH2*1) corresponding to variant beta-1, ADH1B*2 (ADH2*2) corresponding to variant beta-2, ADH1B*3 (ADH2*3) corresponding to variant beta-3. The sequence shown is that of allele ADH1B*1. The ADH1B*2 allele frequency in orientals is approximately 75%, whereas it is less than 5% in most Caucasian populations. ADH1B variations have been associated with protection against alcohol dependence and alcohol-related aerodigestive tract cancer [MIM:103720]. {ECO:0000269|PubMed:10733556, ECO:0000269|PubMed:2547609, ECO:0000269|PubMed:2679216, ECO:0000269|PubMed:3619918, ECO:0000269|PubMed:6374651}. |
| 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. {ECO:0000305}. |
Annotations taken from UniProtKB at the EBI.