| Identification |
|---|
| HMDB Protein ID
| HMDBP12177 |
| Secondary Accession Numbers
| None |
| Name
| Carbonyl reductase [NADPH] 1 |
| Synonyms
|
- 15-hydroxyprostaglandin dehydrogenase [NADP(+)]
- 20-beta-hydroxysteroid dehydrogenase
- NADPH-dependent carbonyl reductase 1
- Prostaglandin 9-ketoreductase
- Prostaglandin-E(2) 9-reductase
- PG-9-KR
|
| Gene Name
| CBR1 |
| Protein Type
| Unknown |
| Biological Properties |
|---|
| General Function
| Not Available |
| Specific Function
| NADPH-dependent reductase with broad substrate specificity. Catalyzes the reduction of a wide variety of carbonyl compounds including quinones, prostaglandins, menadione, plus various xenobiotics. Catalyzes the reduction of the antitumor anthracyclines doxorubicin and daunorubicin to the cardiotoxic compounds doxorubicinol and daunorubicinol. Can convert prostaglandin E2 to prostaglandin F2-alpha (PubMed:1377683, PubMed:1597188). Can bind glutathione, which explains its higher affinity for glutathione-conjugated substrates. Catalyzes the reduction of S-nitrosoglutathione. |
| Pathways
|
- Arachidonic acid metabolism
- Chemical carcinogenesis - DNA adducts
- Chemical carcinogenesis - reactive oxygen species
- Folate biosynthesis
- Metabolism of xenobiotics by cytochrome P450
|
| Reactions
| Not Available |
| GO Classification
|
| Biological Process |
| drug metabolic process |
| vitamin K metabolic process |
| Cellular Component |
| cytoplasm |
| Molecular Function |
| 15-hydroxyprostaglandin-D dehydrogenase (NADP+) activity |
| 15-hydroxyprostaglandin dehydrogenase (NADP+) activity |
| carbonyl reductase (NADPH) activity |
| prostaglandin-E2 9-reductase activity |
|
| Cellular Location
|
Not Available
|
| Gene Properties |
|---|
| Chromosome Location
| Not Available |
| Locus
| Not Available |
| SNPs
| Not Available |
| Gene Sequence
|
Not Available
|
| Protein Properties |
|---|
| Number of Residues
| 289 |
| Molecular Weight
| 31693.1 |
| Theoretical pI
| 7.696 |
| Pfam Domain Function
|
|
| Signals
|
Not Available
|
|
Transmembrane Regions
|
Not Available
|
| Protein Sequence
|
Not Available
|
| External Links |
|---|
| GenBank ID Protein
| Not Available |
| UniProtKB/Swiss-Prot ID
| Q28960 |
| UniProtKB/Swiss-Prot Entry Name
| CBR1_PIG |
| PDB IDs
|
|
| GenBank Gene ID
| Not Available |
| GeneCard ID
| Not Available |
| GenAtlas ID
| Not Available |
| HGNC ID
| Not Available |
| References |
|---|
| General References
| - Tanaka M, Ohno S, Adachi S, Nakajin S, Shinoda M, Nagahama Y: Pig testicular 20 beta-hydroxysteroid dehydrogenase exhibits carbonyl reductase-like structure and activity. cDNA cloning of pig testicular 20 beta-hydroxysteroid dehydrogenase. J Biol Chem. 1992 Jul 5;267(19):13451-5. [PubMed:1377683 ]
- Schieber A, Frank RW, Ghisla S: Purification and properties of prostaglandin 9-ketoreductase from pig and human kidney. Identity with human carbonyl reductase. Eur J Biochem. 1992 Jun 1;206(2):491-502. doi: 10.1111/j.1432-1033.1992.tb16952.x. [PubMed:1597188 ]
- Ghosh D, Sawicki M, Pletnev V, Erman M, Ohno S, Nakajin S, Duax WL: Porcine carbonyl reductase. structural basis for a functional monomer in short chain dehydrogenases/reductases. J Biol Chem. 2001 May 25;276(21):18457-63. doi: 10.1074/jbc.M100538200. Epub 2001 Mar 8. [PubMed:11279087 ]
|
