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- Name help_outline NAD+ Identifier CHEBI:57540 (Beilstein: 3868403) help_outline Charge -1 Formula C21H26N7O14P2 InChIKeyhelp_outline BAWFJGJZGIEFAR-NNYOXOHSSA-M 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](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 1,142 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline thromboxane B2 Identifier CHEBI:90696 Charge -1 Formula C20H33O6 InChIKeyhelp_outline XNRNNGPBEPRNAR-JQBLCGNGSA-M SMILEShelp_outline C1[C@@H]([C@@H]([C@H](OC1O)/C=C/[C@H](CCCCC)O)C/C=C\CCCC(=O)[O-])O 2D coordinates Mol file for the small molecule Search links Involved in 3 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline 11-dehydro-thromboxane B2 Identifier CHEBI:136539 Charge -1 Formula C20H31O6 InChIKeyhelp_outline KJYIVXDPWBUJBQ-UHHGALCXSA-M SMILEShelp_outline C1[C@@H]([C@@H]([C@H](OC1=O)/C=C/[C@H](CCCCC)O)C/C=C\CCCC(=O)[O-])O 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 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 NADH Identifier CHEBI:57945 (Beilstein: 3869564) help_outline Charge -2 Formula C21H27N7O14P2 InChIKeyhelp_outline BOPGDPNILDQYTO-NNYOXOHSSA-L 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](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 1,073 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:52312 | RHEA:52313 | RHEA:52314 | RHEA:52315 | |
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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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Purification and characterization of an NAD(+)-dependent dehydrogenase that catalyzes the oxidation of thromboxane B2 at C-11 from porcine liver. Development and application of 11-dehydro-thromboxane B2 radioimmunoassay to enzyme assay.
Wu P., Fritzo M., Tai H.H.
11-Dehydro-thromboxane B2 has been identified as a major metabolite of infused as well as endogenous thromboxane B2 in mammalian plasma and urine. This metabolite is derived from thromboxane B2 by enzymatic oxidation at C-11 catalyzed by 11-hydroxythromboxane B2 dehydrogenase. A radioimmunoassay f ... >> More
11-Dehydro-thromboxane B2 has been identified as a major metabolite of infused as well as endogenous thromboxane B2 in mammalian plasma and urine. This metabolite is derived from thromboxane B2 by enzymatic oxidation at C-11 catalyzed by 11-hydroxythromboxane B2 dehydrogenase. A radioimmunoassay for 11-dehydro-thromboxane B2 has been developed and used for enzyme assay, purification and characterization. Antibodies were generated against 11-dehydro-thromboxane B2 conjugated to bovine thyroglobulin. Labeled marker was prepared by radioiodinating 11-dehydro-thromboxane B2-tyrosine methyl ester conjugate. A sensitive radioimmunoassay capable of detecting 10 pg of 11-dehydro-thromboxane B2 per assay tube was developed. The antibodies showed minimal crossreaction with thromboxane B2 (0.03%), prostaglandin D2 (2.76%) and other eicosanoids (less than 0.03%). The enzyme activity was determined by assaying NAD(+)-dependent formation of immunoreactive 11-dehydro-thromboxane B2 from thromboxane B2. The enzyme was found to be enriched in liver although significant activity was also detected in gastrointestinal tract and kidney in pig. The enzyme was purified from porcine liver cytosol to apparent homogeneity using conventional and affinity chromatography. The purified enzyme exhibited coenzyme specificity for NAD+ and used thromboxane B2 as a substrate. The enzyme also catalyzes NADH-dependent reduction of 11-dehydro-thromboxane B2 to thromboxane B2 indicating the reversibility of the enzyme catalyzed reaction. The apparent Km values for thromboxane B2, 11-dehydro-thromboxane B2 and NAD+ are 8.1, 8.0 and 23 microM, respectively. Subunit Mr was shown to be 55,000, whereas the native enzyme Mr was found to be 110,000 indicating that the enzyme is a dimer. The enzyme is sensitive to sulfhydryl inhibitions suggesting cysteine residues are essential to enzyme activity. The availability of a homogeneous enzyme preparation should allow further studies on the substrate specificity and the structure and function of the enzyme. << Less
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11-Hydroxythromboxane B2 dehydrogenase is identical to cytosolic aldehyde dehydrogenase.
Westlund P., Fylling A.C., Cederlund E., Jornvall H.
11-Hydroxythromboxane B2 dehydrogenase purified from porcine kidney has been identified as cytosolic aldehyde dehydrogenase (EC 1.2.1.3). This identification is based on protein characteristics, sequence analysis of one proteolytic digest, blocked N-terminus, subunit molecular mass of 55 kDa, and ... >> More
11-Hydroxythromboxane B2 dehydrogenase purified from porcine kidney has been identified as cytosolic aldehyde dehydrogenase (EC 1.2.1.3). This identification is based on protein characteristics, sequence analysis of one proteolytic digest, blocked N-terminus, subunit molecular mass of 55 kDa, and enzymatic activities. The sequence difference with the human enzyme is 7.5% in the fragments analyzed (29 exchanges of 388 positions, corresponding to the expected species variability for cytosolic aldehyde dehydrogenase). The substrate thromboxane B2 contains a hemiacetal in its ring structure, but the reaction most likely proceeds via the aldehyde form of the substrate. This finding is in agreement with the proposed metabolism of 4-hydroxycyclophosphamide and highlights the possibility that molecules containing a hemiacetal structure can function as substrates for aldehyde dehydrogenase. << Less