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- Name help_outline morphine Identifier CHEBI:58097 Charge 1 Formula C17H20NO3 InChIKeyhelp_outline BQJCRHHNABKAKU-KBQPJGBKSA-O SMILEShelp_outline [H][C@]12C=C[C@H](O)[C@@H]3Oc4c(O)ccc5C[C@H]1[NH+](C)CC[C@@]23c45 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 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 1,190 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline morphinone Identifier CHEBI:57728 Charge 1 Formula C17H18NO3 InChIKeyhelp_outline PFBSOANQDDTNGJ-YNHQPCIGSA-O SMILEShelp_outline C[NH+]1CC[C@@]23[C@H]4C=CC(=O)[C@@H]2Oc2c(O)ccc(C[C@@H]14)c32 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 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 1,120 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:14317 | RHEA:14318 | RHEA:14319 | RHEA:14320 | |
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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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Guinea-pig liver morphine 6-dehydrogenase as a naloxone reductase.
Yamano S., Nishida F., Toki S.
Elution profiles of guinea-pig liver naloxone reductase and morphine 6-dehydrogenase on Matrex green A, Sephadex G-100 and DEAE-cellulose (DE32) column chromatography used sequentially in the purification procedure were identical. The ratios of the two enzyme activities were almost constant throug ... >> More
Elution profiles of guinea-pig liver naloxone reductase and morphine 6-dehydrogenase on Matrex green A, Sephadex G-100 and DEAE-cellulose (DE32) column chromatography used sequentially in the purification procedure were identical. The ratios of the two enzyme activities were almost constant throughout all the purification steps. The two enzymes were similarly more stable at pH 6.0 than at pH 8.0 on storage at 4 degrees. The reversible inactivation of the two enzymes by the removal of 2-mercaptoethanol from the enzyme solution was the same. Inhibitory effects of lithocholic acid, CuSO4, quercitrin, phenylarsine oxide, and prostaglandin E1 on the two enzymes were almost the same. These results indicated that naloxone reductase is identical to morphine 6-dehydrogenase in the guinea-pig liver. For the reduction of naloxone, the enzyme utilized either NADPH or NADH as cofactor, and pH optima were 6.8 with NADPH and 6.2 with NADH. The Km values for NADPH and NADH were 6.5 and 2.2 microM respectively. The Vmax values for naloxone were 1.2 units/mg protein with NADPH and 0.5 unit/mg protein with NADH. The Km values for naloxone were 0.27 mM with NADPH and 0.44 mM with NADH. The reaction product formed by the enzyme was identified as 6 alpha-naloxol by thin-layer and gas-liquid chromatographic analyses. Accordingly, it is clear that the enzyme catalyzes the stereospecific reduction of naloxone to form the 6 alpha-hydroxyl congener. << Less
Biochem Pharmacol 35:4321-4326(1986) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.
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Purification and characterization of guinea pig liver morphine 6-dehydrogenase.
Yamano S., Kageura E., Ishida T., Toki S.
Morphine 6-dehydrogenase, which catalyzes the dehydrogenation of morphine to morphinone, has been purified about 440-fold from the soluble fraction of guinea pig liver with a yield of 38%. The purified enzyme was a homogeneous protein on polyacrylamide gel disc electrophoresis and isoelectric focu ... >> More
Morphine 6-dehydrogenase, which catalyzes the dehydrogenation of morphine to morphinone, has been purified about 440-fold from the soluble fraction of guinea pig liver with a yield of 38%. The purified enzyme was a homogeneous protein on polyacrylamide gel disc electrophoresis and isoelectric focusing. The molecular weight and isoelectric point of the enzyme were 29,000 and 7.6, respectively. The enzyme utilizes both NAD and NADP as a cofactor, and the Km values were 0.12 mM for NAD and 0.42 mM for NADP. The Vmax values for morphine were 588 milliunits/mg of protein (with NAD) and 1600 milliunits/mg of protein (with NADP). The Km values for morphine were 0.12 mM (with NAD) and 0.49 mM (with NADP). The enzyme also exhibited activity for morphine-related compounds: nalorphine, normorphine, codeine, and ethylmorphine; however, 7,8-saturated congeners such as dihydromorphine and dihydrocodeine were poor substrates. The enzyme was inactivated by removal of 2-mercaptoethanol from the enzyme solution. The inactivated enzyme was rapidly recovered by the addition of 2-mercaptoethanol. Phenylarsine oxide and CdCl2 (dithiol modifiers) inhibited competitively toward cofactor binding and noncompetitively toward morphine binding. These results suggest that the enzyme possesses the essential thiol groups, probably vicinal dithiol, at or near the cofactor-binding site. Using the partially purified enzyme, 8-(2-hydroxyethylthio)dihydromorphinone was isolated as the product and identified by UV, mass, and NMR spectra. It was confirmed that morphinone proposed as the dehydrogenation product was nonenzymatically and covalently bound to 2-mercaptoethanol. Accordingly, the isolated morphinone-2-mercaptoethanol conjugate must be formed by two steps: enzymatic production of morphinone from morphine and then nonenzymatic binding of 2-mercaptoethanol to morphinone. << Less
J Biol Chem 260:5259-5264(1985) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.