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UniProt functional annotation for P00352 | ||
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| UniProt code: P00352. |
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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: | |
Can convert/oxidize retinaldehyde to retinoic acid. Binds free retinal and cellular retinol-binding protein-bound retinal (By similarity). May have a broader specificity and oxidize other aldehydes in vivo (PubMed:19296407, PubMed:26373694, PubMed:25450233). {ECO:0000250|UniProtKB:P51647, ECO:0000269|PubMed:19296407, ECO:0000269|PubMed:25450233, ECO:0000269|PubMed:26373694}. |
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| Catalytic activity: | |
Reaction=all-trans-retinal + H2O + NAD(+) = all-trans-retinoate + 2 H(+) + NADH; Xref=Rhea:RHEA:42080, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17898, ChEBI:CHEBI:35291, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.2.1.36; Evidence={ECO:0000250|UniProtKB:P51647}; |
| Catalytic activity: | |
Reaction=9-cis-retinal + H2O + NAD(+) = 9-cis-retinoate + 2 H(+) + NADH; Xref=Rhea:RHEA:42084, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:78273, ChEBI:CHEBI:78630; Evidence={ECO:0000250|UniProtKB:P51647}; |
| Catalytic activity: | |
Reaction=11-cis-retinal + H2O + NAD(+) = 11-cis-retinoate + 2 H(+) + NADH; Xref=Rhea:RHEA:47132, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16066, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:87435; Evidence={ECO:0000250|UniProtKB:P51647}; |
| Activity regulation: | |
Inhibited by citral, disulfiram, and cyanamide. Activated by diethylstilbestrol (PubMed:19296407). Inhibited by duocarmycin analogs (PubMed:26373694). {ECO:0000269|PubMed:19296407, ECO:0000269|PubMed:26373694}. |
| Biophysicochemical properties: | |
Kinetic parameters: KM=59.4 uM for NAD (at pH 8.0) {ECO:0000269|PubMed:19296407}; KM=238.2 uM for acetaldehyde (at pH 8.0) {ECO:0000269|PubMed:19296407}; KM=142.2 uM for benzaldehyde (at pH 8.0) {ECO:0000269|PubMed:19296407}; KM=4.8 uM for 4-hydroxynonenal (at pH 8.0) {ECO:0000269|PubMed:19296407}; KM=121.4 uM for propionaldehyde (at pH 8.0) {ECO:0000269|PubMed:19296407}; KM=15 uM for propionaldehyde (at pH 7.5) {ECO:0000269|PubMed:25450233}; KM=3.5 uM for malonaldehyde (at pH 8.0) {ECO:0000269|PubMed:19296407}; KM=177.1 uM for trans-2-heptenal (at pH 8.0) {ECO:0000269|PubMed:19296407}; Vmax=149.7 nmol/min/mg enzyme with NAD (at pH 8.0) {ECO:0000269|PubMed:19296407}; Vmax=631.4 nmol/min/mg enzyme with acetaldehyde (at pH 8.0) {ECO:0000269|PubMed:19296407}; Vmax=750.3 nmol/min/mg enzyme with benzaldehyde (at pH 8.0) {ECO:0000269|PubMed:19296407}; Vmax=135 nmol/min/mg enzyme with 4-hydroxynonenal (at pH 8.0) {ECO:0000269|PubMed:19296407}; Vmax=445.3 nmol/min/mg enzyme with propionaldehyde (at pH 8.0) {ECO:0000269|PubMed:19296407}; Vmax=381.6 nmol/min/mg enzyme with malonaldehyde (at pH 8.0) {ECO:0000269|PubMed:19296407}; Vmax=155.8 nmol/min/mg enzyme with trans-2-heptenal (at pH 8.0) {ECO:0000269|PubMed:19296407}; |
| Pathway: | |
Cofactor metabolism; retinol metabolism. {ECO:0000250|UniProtKB:P51647}. |
| Subunit: | |
Homotetramer. {ECO:0000250|UniProtKB:P51977}. |
| Subcellular location: | |
Cytoplasm, cytosol {ECO:0000250|UniProtKB:P48644}. |
| Ptm: | |
The N-terminus is blocked most probably by acetylation. {ECO:0000250|UniProtKB:P15437}. |
| Similarity: | |
Belongs to the aldehyde dehydrogenase family. {ECO:0000305}. |
Annotations taken from UniProtKB at the EBI.