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Literature summary for 1.1.1.300 extracted from
- Generation and isolation of recombinant retinoid oxidoreductase complex (2020), Methods Enzymol., 637, 77-93 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| recombinant expression of the enzyme complex ROC formed by HA-tagged RDH10 and FLAT-tagged DHRS3, via a baculovirus expression system in Sopodoptera frugiperda Sf9 cells. Protein production method, overview | Homo sapiens |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| G43A/G47A/G49A | site-directed mutagenesis, the cofactor binding mutants, RDH10 G43A/G47A/G49A-HA and DHRS3 G49A/G51A-FLAG, retain the capacity to form complexes with wild-type protein partners | Homo sapiens |
| G49A/G51A | site-directed mutagenesis, the cofactor binding mutants, RDH10 G43A/G47A/G49A-HA and DHRS3 G49A/G51A-FLAG, retain the capacity to form complexes with wild-type protein partners | Homo sapiens |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| microsome | - |
Homo sapiens | - |
- |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| all-trans-retinol + NADP+ | Homo sapiens | - |
all-trans-retinal + NADPH + H+ | - |
r |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | O75911 | - |
- |
| Homo sapiens | Q8IZV5 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant enzyme complex ROC from Sopodoptera frugiperda Sf9 cells by anti-HA affinity chromatography | Homo sapiens |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| all-trans-retinol + NADP+ | - |
Homo sapiens | all-trans-retinal + NADPH + H+ | - |
r | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| all-trans-retinaldehyde reductase | - |
Homo sapiens |
| DHRS3 | - |
Homo sapiens |
| RDH10 | - |
Homo sapiens |
| retinoid oxidoreductase complex | - |
Homo sapiens |
| ROC | - |
Homo sapiens |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| NADP+ | - |
Homo sapiens | |
| NADPH | - |
Homo sapiens | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | the enzyme belongs to the the short-chain dehydrogenase/reductase (SDR) superfamily, NAD(P)-dependent enzymes, and short-chain dehydrogenase/reductase 16C family (SDR16C) | Homo sapiens |
| malfunction | the cofactor binding mutants, RDH10 G43A/G47A/G49A-HA and DHRS3 G49A/G51A-FLAG, retain the capacity to form complexes with wild-type protein partners. Similarly, active site mutants, RDH10 Y210A-HA and DHRS3 Y188A-FLAG, retain the capacity to form complexes with wild-type protein partners. Thus, catalytically active proteins are not necessary for complex formation | Homo sapiens |
| metabolism | the oxidation of all-trans-retinol to all-trans-retinal represents the first and rate-limiting step of the all-trans-retinoic acid (RA) synthesis pathway and it is the target of mechanisms that fine-tune RA levels within the cell. RDH10 is one enzyme responsible for the oxidation of all-trans-retinol to all-trans-retinaldehyde, and together with the all-trans-retinaldehyde reductase DHRS3 forms an oligomeric protein complex. The resulting retinoid oxidoreductase complex (ROC) is bifunctional and has the capacity to regulate steady-state levels of the direct precursor of RA, all-trans-retinaldehyde. By coupling retinol dehydrogenase and retinaldehyde reductase activities, an elegant system is formed that can fine-tune steady-state levels of all-trans-retinaldehyde, and consequently RA, concentrations within the cell. DHRS3 is a critical regulator of RA synthesis. Formation of ROC influences the catalytic properties of both RDH10 and DHRS3 subunits | Homo sapiens |
| metabolism | the oxidation of all-trans-retinol to all-trans-retinal represents the first and rate-limiting step of the all-trans-retinoic acid (RA) synthesis pathway and it is the target of mechanisms that fine-tune RA levels within the cell. RDH10 is one enzyme responsible for the oxidation of all-trans-retinol to all-trans-retinaldehyde, and together with the all-trans-retinaldehyde reductase DHRS3 forms an oligomeric protein complex. The resulting retinoid oxidoreductase complex (ROC) is bifunctional and has the capacity to regulate steady-state levels of the direct precursor of RA, all-trans-retinaldehyde. By coupling retinol dehydrogenase and retinaldehyde reductase activities, an elegant system is formed that can fine-tune steady-state levels of all-trans-retinaldehyde, and consequently RA, concentrations within the cell. Formation of ROC influences the catalytic properties of both RDH10 and DHRS3 subunits | Homo sapiens |
| physiological function | the retinoid oxidoreductase complex (ROC) is bifunctional and has the capacity to regulate steady-state levels of the direct precursor of RA, all-trans-retinaldehyde. By coupling retinol dehydrogenase and retinaldehyde reductase activities, an elegant system is formed that can fine-tune steady-state levels of all-trans-retinaldehyde, and consequently RA, concentrations within the cell. Formation of ROC influences the catalytic properties of both RDH10 and DHRS3 subunits. Catalytically active enzymes are not necessary for complex formation. As the rate-limiting step of RA synthesis, the conversion of all-trans-retinol to all-trans-retinaldehyde is a target of mechanisms that regulate RA synthesis. ROC, consisting of the retinol dehydrogenase RDH10 and the retinaldehyde reductase DHRS3, is a critical component of RA synthesis regulation | Homo sapiens |
| physiological function | the retinoid oxidoreductase complex (ROC) is bifunctional and has the capacity to regulate steady-state levels of the direct precursor of RA, all-trans-retinaldehyde. By coupling retinol dehydrogenase and retinaldehyde reductase activities, an elegant system is formed that can fine-tune steady-state levels of all-trans-retinaldehyde, and consequently RA, concentrations within the cell. Formation of ROC influences the catalytic properties of both RDH10 and DHRS3 subunits. DHRS3 is a critical regulator of RA synthesis. Catalytically active enzymes are not necessary for complex formation. As the rate-limiting step of RA synthesis, the conversion of all-trans-retinol to all-trans-retinaldehyde is a target of mechanisms that regulate RA synthesis. ROC, consisting of the retinol dehydrogenase RDH10 and the retinaldehyde reductase DHRS3, is a critical component of RA synthesis regulation | Homo sapiens |
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