Enzymes
| UniProtKB help_outline | 2,131 proteins |
Reaction participants Show >> << Hide
- Name help_outline a secondary alcohol Identifier CHEBI:35681 Charge 0 Formula CH2OR2 SMILEShelp_outline *C(*)O 2D coordinates Mol file for the small molecule Search links Involved in 672 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline NADP+ Identifier CHEBI:58349 Charge -3 Formula C21H25N7O17P3 InChIKeyhelp_outline XJLXINKUBYWONI-NNYOXOHSSA-K SMILEShelp_outline NC(=O)c1ccc[n+](c1)[C@@H]1O[C@H](COP([O-])(=O)OP([O-])(=O)OC[C@H]2O[C@H]([C@H](OP([O-])([O-])=O)[C@@H]2O)n2cnc3c(N)ncnc23)[C@@H](O)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 1,294 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline a ketone Identifier CHEBI:17087 Charge 0 Formula COR2 SMILEShelp_outline [*]C([*])=O 2D coordinates Mol file for the small molecule Search links Involved in 1,156 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline NADPH Identifier CHEBI:57783 (Beilstein: 10411862) help_outline Charge -4 Formula C21H26N7O17P3 InChIKeyhelp_outline ACFIXJIJDZMPPO-NNYOXOHSSA-J SMILEShelp_outline NC(=O)C1=CN(C=CC1)[C@@H]1O[C@H](COP([O-])(=O)OP([O-])(=O)OC[C@H]2O[C@H]([C@H](OP([O-])([O-])=O)[C@@H]2O)n2cnc3c(N)ncnc23)[C@@H](O)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 1,288 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H+ Identifier CHEBI:15378 Charge 1 Formula H InChIKeyhelp_outline GPRLSGONYQIRFK-UHFFFAOYSA-N SMILEShelp_outline [H+] 2D coordinates Mol file for the small molecule Search links Involved in 9,521 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:19257 | RHEA:19258 | RHEA:19259 | RHEA:19260 | |
|---|---|---|---|---|
| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
| UniProtKB help_outline |
|
|||
| EC numbers help_outline | ||||
| Gene Ontology help_outline | ||||
| KEGG help_outline | ||||
| MetaCyc help_outline |
Related reactions help_outline
Specific form(s) of this reaction
- RHEA:70221
- RHEA:70217
- RHEA:68149
- RHEA:68145
- RHEA:68141
- RHEA:68137
- RHEA:65497
- RHEA:65062
- RHEA:65058
- RHEA:64418
- RHEA:63505
- RHEA:63482
- RHEA:63478
- RHEA:62270
- RHEA:62218
- RHEA:62070
- RHEA:53822
- RHEA:47541
- RHEA:45317
- RHEA:42770
- RHEA:36589
- RHEA:24510
- RHEA:20746
- RHEA:20235
- RHEA:18943
- RHEA:18427
- RHEA:17739
- RHEA:17027
- RHEA:16819
- RHEA:15859
- RHEA:13831
- RHEA:10726
- RHEA:10142
Publications
-
Purification and properties of an NADPH-dependent carbonyl reductase from human brain. Relationship to prostaglandin 9-ketoreductase and xenobiotic ketone reductase.
Wermuth B.
A nonspecific NADPH-dependent carbonyl reductase from human brain (formerly designated as aldehyde reductase 1; Ris, M. M., and von Wartburg, J. P. (1973) Eur. J. Biochem. 37, 69-77) has been purified to homogeneity. The enzyme reduces a number of biologically and pharmacologically active carbonyl ... >> More
A nonspecific NADPH-dependent carbonyl reductase from human brain (formerly designated as aldehyde reductase 1; Ris, M. M., and von Wartburg, J. P. (1973) Eur. J. Biochem. 37, 69-77) has been purified to homogeneity. The enzyme reduces a number of biologically and pharmacologically active carbonyl compounds. Quinones, e.g. menadione, ubiquinone, and tocopherolquinone are the best substrates, followed by aldehydes containing an activated carbonyl moiety, e.g. 4-nitrobenzaldehyde or methylglyoxal. The enzyme also reduces ketones, e.g. prostaglandins of the E and A class, the anthracycline antibiotic daunorubicin and 3-ketosteroids. During catalysis the pro 4S hydrogen atom of the nicotinamide ring of NADPH is transferred to the substrate. Flavonoids, e.g. quercetin and rutin, indomethacin, ethacrynic acid, and dicoumarol inhibit the enzyme activity. 4-Hydroxymercuribenzoate and iodoacetate inactivate the enzyme. NADPH and substrate do not protect against the loss of activity. Carbonyl reductase consists of a single polypeptide chain with a molecular weight of 30,000. The native enzyme occurs in three molecular forms with similar substrate specificity and inhibitor sensitivity. The isoelectric points of the three enzyme species are 6.95, 7.85, and 8.5. In the presence of coenzyme the isoelectric points are shifted to 5.2 to 5.9. The comparison of structural and enzymic features of carbonyl reductase with other monomeric oxidoreductases suggests a close relationship of carbonyl reductase with prostaglandin 9-keto-reductase and xenobiotic ketone reductase. << Less
J. Biol. Chem. 256:1206-1213(1981) [PubMed] [EuropePMC]
This publication is cited by 3 other entries.
-
Heterogeneity of anthracycline antibiotic carbonyl reductases in mammalian livers.
Ahmed N.K., Felsted R.L., Bachur N.R.