Enzymes
| UniProtKB help_outline | 1,707 proteins |
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- Name help_outline (5S,12S)-dihydroxy-(6E,10E,12E,14Z)-eicosatetraenoate Identifier CHEBI:133975 Charge -1 Formula C20H31O4 InChIKeyhelp_outline VNYSSYRCGWBHLG-CTOJTRLNSA-M SMILEShelp_outline C([C@@H](/C=C/C=C/C=C/[C@H](CCCC([O-])=O)O)O)/C=C\CCCCC 2D coordinates Mol file for the small molecule Search links Involved in 1 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 1,253 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline 12-oxo-(5S)-hydroxy-(6E,8E,10E,14Z)-eicosatetraenoate Identifier CHEBI:133974 Charge -1 Formula C20H29O4 InChIKeyhelp_outline SJVWVCVZWMJXOK-TWMXWPQVSA-M SMILEShelp_outline C(C(/C=C/C=C/C=C/[C@H](CCCC([O-])=O)O)=O)/C=C\CCCCC 2D coordinates Mol file for the small molecule Search links Involved in 2 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 9,176 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 1,247 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:51212 | RHEA:51213 | RHEA:51214 | RHEA:51215 | |
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| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Publications
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Enzymatic inactivation of leukotriene B4 by a novel enzyme found in the porcine kidney. Purification and properties of leukotriene B4 12-hydroxydehydrogenase.
Yokomizo T., Izumi T., Takahashi T., Kasama T., Kobayashi Y., Sato F., Taketani Y., Shimizu T.
Leukotriene B4 (LTB4) 12-hydroxydehydrogenase was purified to apparent homogeneity from the cytosol fraction of the porcine kidney. The N-terminal amino acid sequence analysis revealed that this enzyme is a novel protein with a molecular weight of 35,000. Although the enzyme is ubiquitously distri ... >> More
Leukotriene B4 (LTB4) 12-hydroxydehydrogenase was purified to apparent homogeneity from the cytosol fraction of the porcine kidney. The N-terminal amino acid sequence analysis revealed that this enzyme is a novel protein with a molecular weight of 35,000. Although the enzyme is ubiquitously distributed in various tissues and leukocytes of porcine, the kidney and liver had the highest enzyme activities. In the presence of NADP+ as a cofactor, the enzyme catalyzes the conversion of LTB4 to 12-oxo-LTB4, the structure identified by gas chromatography/mass spectrometry. 12-Oxo-LTB4 was further converted by other enzymes to 10,11,14,15-tetrahydro-12-oxo-LTB4, which was determined by proton NMR and gas chromatography/mass spectrometry. 12-Oxo-LTB4 was 100-fold less potent than LTB4 in increasing intracellular calcium concentrations of human leukocytes. 6-trans-LTB4 and LTB4 proved to be the best substrates of the enzyme, whereas various types of monohydroxyeicosatetraenoic acids, 5(S),12(S)-dihydroxyeicosatetraenoic acid, prostaglandins, cortisol, or pregnenolone could not serve as a substrate. These results suggest that the enzyme acts specifically on the 12(R)-hydroxy group of leukotriene B4 and is involved in the metabolic inactivation of LTB4 in the porcine kidney. << Less
J. Biol. Chem. 268:18128-18135(1993) [PubMed] [EuropePMC]
This publication is cited by 3 other entries.