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Information on EC 1.1.1.218 - morphine 6-dehydrogenase
for references in articles please use BRENDA:EC1.1.1.218
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EC Tree 1 Oxidoreductases
1.1 Acting on the CH-OH group of donors
1.1.1 With NAD+ or NADP+ as acceptor
1.1.1.218 morphine 6-dehydrogenase
IUBMB Comments
Also acts on some other alkaloids, including codeine, normorphine and ethylmorphine, but only very slowly on 7,8-saturated derivatives such as dihydromorphine and dihydrocodeine. In the reverse direction, also reduces naloxone to the 6α-hydroxy analogue. Activated by 2-sulfanylethan-1-ol (2-mercaptoethanol).
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
- 1.1.1.218
- morphinone
-
dehydrogenation
-
aldo-keto
-
alicyclic
- normorphine
- ethylmorphine
- codeine
- steroid
- nadp
- hamster
-
congener
- barbital
-
lithocholic
- indomethacin
- pyrazole
- 2-mercaptoethanol
- dihydrocodeine
-
diethyl
-
nonenzymatically
-
phenylarsine
- phe
- maleate
- ketones
- biliary
-
17beta-hydroxysteroids
- o-quinones
- dihydromorphine
-
analgesia
-
nad+-dependent
-
3alpha-hydroxysteroids
showSynonyms
morphine 6-dehydrogenase, naloxone reductase, akr1c34, morphine-6-dehydrogenase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
morphine 6-dehydrogenase
-
-
-
-
naloxone reductase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
morphine + NAD(P)+ = morphinone + NAD(P)H + H+
dehydrogenation of the 6-hydroxy group of morphine derivatives having a 7,8-unsaturated bond
-
morphine + NAD(P)+ = morphinone + NAD(P)H + H+
dehydrogenation of the 6-hydroxy group of morphine derivatives having a 7,8-unsaturated bond
-
-
morphine + NAD(P)+ = morphinone + NAD(P)H + H+
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dehydrogenation
-
-
-
-
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
morphine biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
morphine:NAD(P)+ 6-oxidoreductase
Also acts on some other alkaloids, including codeine, normorphine and ethylmorphine, but only very slowly on 7,8-saturated derivatives such as dihydromorphine and dihydrocodeine. In the reverse direction, also reduces naloxone to the 6alpha-hydroxy analogue. Activated by 2-sulfanylethan-1-ol (2-mercaptoethanol).
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CAS REGISTRY NUMBER
COMMENTARY
106640-77-1
deleted Reg.No.
97002-71-6
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
3-hydroxyhexobarbital + NADP+
?
-
Substrates: does not serve as a substrate for guinea pig enzyme
Products: -
Products: -
?
cyclohexene-2-ol + NADP+
cyclohexene-2-one + NADPH
-
Substrates: -
Products: -
Products: -
?
morphine + NAD+
morphinone + NADH + H+
J7M9D0
Substrates: -
Products: -
Products: -
?
nalorphine + NAD(P)+
(5alpha)-3-hydroxy-17-(prop-2-en-1-yl)-7,8-didehydro-4,5-epoxymorphinan-6-one + NAD(P)H + H+
trans-1,4-decalindiol + NADP+
?
-
Substrates: about 30% of the activity observed with morphine
Products: -
Products: -
?
trans-naphthalene dihydrodiol + NAD+
?
Substrates: -
Products: -
Products: -
?
trans-naphthalene dihydrodiol + NAD+
? + NADH + H+
J7M9D0
Substrates: -
Products: -
Products: -
?
codeine + NAD(P)+
codeinone + NAD(P)H
-
Substrates: oxidation at 80% the rate of morphine oxidation
Products: -
Products: -
?
codeine + NAD(P)+
codeinone + NAD(P)H
-
Substrates: oxidation at 80% the rate of morphine oxidation
Products: -
Products: -
?
codeine + NAD(P)+
codeinone + NAD(P)H
-
Substrates: only weak enzyme activity for codeine
Products: -
Products: -
?
codeine + NAD(P)+
codeinone + NAD(P)H
-
Substrates: codeine best substrate
Products: -
Products: -
?
codeine + NAD(P)+
codeinone + NAD(P)H
-
Substrates: oxidation at 120% the rate of morphine oxidation
Products: at pH 6.5, + NADPH, reduction of codeinone to codeine
Products: at pH 6.5, + NADPH, reduction of codeinone to codeine
r
codeine + NAD(P)+
codeinone + NAD(P)H
-
Substrates: non-Theorell-Chance sequential ordered mechanism for codeine oxidation at pH 9.5
Products: morphine dehydrogenase follows a Theorell-Chance mechanism for codeinone reduction at pH 7.0
Products: morphine dehydrogenase follows a Theorell-Chance mechanism for codeinone reduction at pH 7.0
?
codeine + NAD(P)+
codeinone + NAD(P)H
-
Substrates: oxidation at 120% the rate of morphine oxidation
Products: at pH 6.5, + NADPH, reduction of codeinone to codeine
Products: at pH 6.5, + NADPH, reduction of codeinone to codeine
r
codeine + NAD(P)+
codeinone + NAD(P)H
-
Substrates: non-Theorell-Chance sequential ordered mechanism for codeine oxidation at pH 9.5
Products: morphine dehydrogenase follows a Theorell-Chance mechanism for codeinone reduction at pH 7.0
Products: morphine dehydrogenase follows a Theorell-Chance mechanism for codeinone reduction at pH 7.0
?
codeine + NADP+
codeinone + NADPH
-
Substrates: codeine as the sole carbon and energy source
Products: -
Products: -
?
codeine + NADP+
codeinone + NADPH
-
Substrates: codeine as the sole carbon and energy source
Products: -
Products: -
?
dihydrocodeine + NADP+
dihydrocodeinone + NADPH
-
Substrates: -
Products: -
Products: -
?
dihydrocodeine + NADP+
dihydrocodeinone + NADPH
-
Substrates: -
Products: -
Products: -
?
dihydrocodeine + NADP+
dihydrocodeinone + NADPH
-
Substrates: -
Products: -
Products: -
?
dihydrocodeine + NADP+
dihydrocodeinone + NADPH
-
Substrates: -
Products: -
Products: -
?
ethylmorphine + NAD(P)+
?
-
Substrates: oxidation at 51% the rate of morphine oxidation
Products: -
Products: -
?
ethylmorphine + NAD(P)+
?
-
Substrates: oxidation at 51% the rate of morphine oxidation
Products: -
Products: -
?
morphine + NADP+
morphinone + NADPH
-
Substrates: highly specific alkaloid dehydrogenase, oxidizing only the C-6 hydroxy group of morphine and codeine, morphine as the sole carbon and energy source
Products: -
Products: -
?
morphine + NADP+
morphinone + NADPH
-
Substrates: highly specific alkaloid dehydrogenase, oxidizing only the C-6 hydroxy group of morphine and codeine, morphine as the sole carbon and energy source
Products: -
Products: -
?
morphine + NADP+
morphinone + NADPH + H+
-
Substrates: -
Products: production of morphinone demonstrated in vitro experiments
Products: production of morphinone demonstrated in vitro experiments
?
morphine + NADP+
morphinone + NADPH + H+
-
Substrates: -
Products: production of morphinone demonstrated in vitro experiments
Products: production of morphinone demonstrated in vitro experiments
?
morphine + NADP+
morphinone + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
morphine + NADP+
morphinone + NADPH + H+
-
Substrates: enzyme activity only with NAD+
Products: -
Products: -
?
morphine + NADP+
morphinone + NADPH + H+
-
Substrates: enzyme acitivity with NAD+ four times that with NADP+
Products: -
Products: -
?
morphine + NADP+
morphinone + NADPH + H+
-
Substrates: enzyme activity only with NADP+
Products: -
Products: -
?
morphine + NADP+
morphinone + NADPH + H+
-
Substrates: enzyme activity only with NADP+
Products: -
Products: -
?
morphine + NADP+
morphinone + NADPH + H+
-
Substrates: + NAD+: enzyme activity ten times that with NADP+
Products: -
Products: -
?
morphine + NADP+
morphinone + NADPH + H+
-
Substrates: + NAD+: enzyme activity ten times that with NADP+
Products: -
Products: -
?
nalorphine + NAD(P)+
(5alpha)-3-hydroxy-17-(prop-2-en-1-yl)-7,8-didehydro-4,5-epoxymorphinan-6-one + NAD(P)H + H+
-
Substrates: best substrate, oxidation at 120% the rate of morphine oxidation
Products: -
Products: -
?
nalorphine + NAD(P)+
(5alpha)-3-hydroxy-17-(prop-2-en-1-yl)-7,8-didehydro-4,5-epoxymorphinan-6-one + NAD(P)H + H+
-
Substrates: best substrate, oxidation at 120% the rate of morphine oxidation
Products: -
Products: -
?
naloxone + NAD(P)H
6alpha-naloxol + NADP+
-
Substrates: -
Products: stereospecific reduction
Products: stereospecific reduction
?
naloxone + NAD(P)H
6alpha-naloxol + NADP+
-
Substrates: -
Products: stereospecific reduction
Products: stereospecific reduction
?
normorphine + NAD(P)+
?
-
Substrates: about 3 times better substrate than morphine
Products: -
Products: -
?
normorphine + NAD(P)+
?
-
Substrates: about 3 times better substrate than morphine
Products: -
Products: -
?
normorphine + NAD(P)+
?
-
Substrates: best substrate, oxidation at 139% the rate of morphine oxidation
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme AKR1C34 shows 3alpha/17beta/20alpha-hydroxysteroid dehydrogenase activities, EC 1.1.1.239, detailed overview. Ala54 plays a critical role in non-/recognition of the steroidal substrates. Reaction products identification by thin-layer chromatography (TLC) and liquid chromatography/mass spectrometry (LC/MS)
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme AKR1C34 shows 3alpha/17beta/20alpha-hydroxysteroid dehydrogenase activities, EC 1.1.1.239, detailed overview. Ala54 plays a critical role in non-/recognition of the steroidal substrates. Reaction products identification by thin-layer chromatography (TLC) and liquid chromatography/mass spectrometry (LC/MS)
Products: -
Products: -
?
additional information
?
-
J7M9D0
Substrates: the enzyme shows NAD+-dependent dehydrogenase activity towards other nonsteroidal alicyclic alcohols and 3alpha/17beta-hydroxy-C18/C19/C21-steroids, detailed overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme shows NAD+-dependent dehydrogenase activity towards other nonsteroidal alicyclic alcohols and 3alpha/17beta-hydroxy-C18/C19/C21-steroids, detailed overview
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
morphine + NAD+
morphinone + NADH + H+
J7M9D0
Substrates: -
Products: -
Products: -
?
codeine + NADP+
codeinone + NADPH
-
Substrates: codeine as the sole carbon and energy source
Products: -
Products: -
?
codeine + NADP+
codeinone + NADPH
-
Substrates: codeine as the sole carbon and energy source
Products: -
Products: -
?
morphine + NADP+
morphinone + NADPH
-
Substrates: highly specific alkaloid dehydrogenase, oxidizing only the C-6 hydroxy group of morphine and codeine, morphine as the sole carbon and energy source
Products: -
Products: -
?
morphine + NADP+
morphinone + NADPH
-
Substrates: highly specific alkaloid dehydrogenase, oxidizing only the C-6 hydroxy group of morphine and codeine, morphine as the sole carbon and energy source
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
J7M9D0
the rabbit enzyme shows high coenzyme preference for NAD+ over NADP+. Also in the reverse reaction, the enzymes reduces several alpha-dicarbonyl compounds including S-camphorquinone using NADH as the coenzyme, exhibiting low Km values of 0.004-0.006 mM. The reductase activity of the enzyme determined with NADPH as the coenzyme is less than 40% of their NADH-linked activity
-
additional information
-
the rabbit enzyme shows high coenzyme preference for NAD+ over NADP+. Also in the reverse reaction, the enzymes reduces several alpha-dicarbonyl compounds including S-camphorquinone using NADH as the coenzyme, exhibiting low Km values of 0.004-0.006 mM. The reductase activity of the enzyme determined with NADPH as the coenzyme is less than 40% of their NADH-linked activity
-
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Phenylarsine oxide
-
dithiol modifier, competitive inhibitor to cofactor binding and noncompetitively toward morphine binding
additional information
-
competitive inhibitors: testosterone, 5alpha-androstan-17beta-ol-3-one, 5beta-androsteran-17beta-ol-3-one; no inhibition by indomethacine; no or weak inhibition by pyrazole, barbital
-
additional information
no or poor inhibition by 7-hydroxyflavone, chrysin, quercetin, genistein, galangin, lithocholic acid, and zearalenone
-
additional information
-
no or poor inhibition by 7-hydroxyflavone, chrysin, quercetin, genistein, galangin, lithocholic acid, and zearalenone
-
additional information
-
5beta-dihydrotestosterone, lithocholic acid, androsterone and estradiol inhibit competitively toward morphine binding; little inhibitory effect: indomethacin, prostaglandins E2, D2; no or weak inhibition by pyrazole, barbital
-
additional information
-
competitive inhibition: NADP+ with respect to NADPH, codeine with respect to codeinone
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.002
5alpha-androstan-17beta-ol-3-one
-
similar values of other 17beta-hydroxysteroids
additional information
additional information
J7M9D0
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5
-
in presence of NADPH reduction of codeinone to codeine, in MOPS buffer
7.4
9.3
9.5
-
with NADP+ as cofactor, in glycine-NaOH buffer, oxidizing the C-6 hydroxy group of morphine and codeine
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
additional information
mRNA for AKR1C34 is expressed liver-specific in female hamsters and ubiquitously in male hamsters
brenda
additional information
-
mRNA for AKR1C34 is expressed liver-specific in female hamsters and ubiquitously in male hamsters
brenda
additional information
J7M9D0
ubiquitous expression in rabbit tissues
brenda
additional information
-
ubiquitous expression in rabbit tissues
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
physiological function
J7M9D0
mammalian morphine 6-dehydrogenase converts morphine into a reactive electrophile, morphinone. M6DH is involved in the toxic action of morphine including the development of tolerance to this drug
evolution
enzyme M6DH is a member of the aldoketo reductase (AKR) 1C subfamily in the AKR superfamily
evolution
J7M9D0
enzyme M6DH is a member of the aldoketo reductase (AKR) 1C subfamily in the AKR superfamily
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). Y2407_MYCS2
Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155)
283
0
29949
Swiss-Prot
-
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
31000
32000
38000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D47N
-
residue modified by site-directed mutagenesis, resulting in substantial loss of activity
K76M
-
residue modified by site-directed mutagenesis, resulting in substantial loss of activity
Y52F
D47N
-
residue modified by site-directed mutagenesis, resulting in substantial loss of activity
-
K76M
-
residue modified by site-directed mutagenesis, resulting in substantial loss of activity
-
Y52F
Y52F
-
F is incapable of acting as proton donor /aim: NAD+-dependent morphine dehydrogenase for biotransformation morphine-morphinone-hydromorphine, codeine-hydrocodone respectively (medically useful semisynthetic opiates)
Y52F
-
residue modified by site-directed mutagenesis, resulting in substantial loss of activity
Y52F
-
F is incapable of acting as proton donor /aim: NAD+-dependent morphine dehydrogenase for biotransformation morphine-morphinone-hydromorphine, codeine-hydrocodone respectively (medically useful semisynthetic opiates)
-
Y52F
-
residue modified by site-directed mutagenesis, resulting in substantial loss of activity
-
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8
-
in 50 mM sodium phosphate buffer + 100 mM 2-mercaptoethanol + NAD+ at least for a week stable at 2-4°C
6
-
in 50 mM sodium phosphate buffer + 100 mM 2-mercaptoethanol + NADP+ or NAD+ at least for a week stable at 2-4°C
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
2-mercaptoethanol stabilizes during purification and storage, removal inactivates, reversible
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80C, 20% glycerol, v/v, stable at least four months
2-4°C, 50 mM sodium phosphate buffer + 100 mM 2-mercaptoethanol, pH 6., 90% of the activity retained with both NAD+ and NADP+ for a week
-
4°C, 80% of the activity after a week in 50 mM sodium phosphate buffer, pH 6.0, 100 mM 2-mercaptoethanol, more stable at pH 6.0 than at pH 8.0
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
gel filtration, various chromatographic techniques
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3)pLysS by nickel affinity chromatography, ultrafiltration, and dialysis
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene AKR1C26, DNA and amino acid sequence determination and analysis, sequence comparisons, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)pLysS
J7M9D0
gene AKR1C34, cloned from liver, DNA and amino acid sequence determination and analysis, sequence comparisons, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)pLysS
gene encoding morphine dehydrogenase on natural plasmid, expressed in Escherichia coli
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Yamano, S; Kageura, E.; Ishida, T.; Toki, S.
Purification and characterization of guinea pig liver morphine 6-dehydrogenase
J. Biol. Chem.
260
5259-5264
1985
Cavia porcellus, Cavia porcellus Hartley
brenda
Yamano, S.; Nishida, F; Toki, S.
Guinea-pig liver morphine 6-dehydrogenase as a naloxone reductase
Biochem. Pharmacol.
35
4321-4326
1986
Cavia porcellus, Cavia porcellus Hartley
brenda
Bruce, N.C.; Wilmot, C.J.; Jordan, K.N.; Trebilcock, A.E.; Stephens, L.D.G.; Lowe, Ch.R.
Microbial degradation of the morphine alkaloids: identification of morphinone as an intermediate in the metabolism of morphine by Pseudomonas putida M10
Arch. Microbiol.
154
465-470
1990
Pseudomonas putida, Pseudomonas putida M10
brenda
Bruce, N.C.; Wilmot, C.J.; Jordan, K.N.; Stephens, L.D.G.; Lowe, Ch.R.
Microbial degradation of the morphine alkaloids
Biochem. J.
274
875-880
1991
Pseudomonas putida, Pseudomonas putida M10
-
brenda
Walker, E.H.; Bruce, N.C.
Towards engineering an improved morphine dehydrogenase
Ann. N. Y. Acad. Sci.
799
6-10
1996
Pseudomonas putida, Pseudomonas putida M10
brenda
Yamano, S.; Ito, K.; Ogata, S.; Toki, S.
Purification, characterization and partial primary structure of morphine 6-dehydrogenase from rabbit liver cytosol
Arch. Biochem. Biophys.
341
81-88
1997
Oryctolagus cuniculus
brenda
Yamano, S.; Takahashi, A.; Todaka, T.; Toki, S.
In vivo and in vitro formation of morphinone from morphine in rat
Xenobiotica
27
645-656
1997
Rattus norvegicus, Rattus norvegicus Wistar
brenda
Todaka, T.; Yamano, S.; Toki, S.
Purification and characterization of NAD-dependent morphine 6-dehydrogenase from hamster liver cytosol, a new member of the aldo-keto reductase superfamily
Arch. Biochem. Biophys.
374
189-197
2000
Mesocricetus auratus
brenda
Walker, E.H.; French, C.E.; Rathbone, D.A.; Bruce, N.C.
Mechanistic studies of morphine dehydrogenase and stabilization against covalent inactivation
Biochem. J.
345
687-692
2000
Pseudomonas putida, Pseudomonas putida M10
brenda
Todaka, T.; Ishida, T.; Kita, H.; Narimatsu, S.; Yamano, S.
Bioactivation of morphine in human liver: isolation and identification of morphinone, a toxic metabolite
Biol. Pharm. Bull.
28
1275-1280
2005
Homo sapiens
brenda
Endo, S.; Matsunaga, T.; Fujimoto, A.; Kumada, S.; Arai, Y.; Miura, Y.; Mikamo, H.; El-Kabbani, O.; Yamano, S.; Iinuma, M.; Hara, A.
Characterization of rabbit morphine 6-dehydrogenase and two NAD+-dependent 3alpha(17beta)-hydroxysteroid dehydrogenases
Arch. Biochem. Biophys.
529
131-139
2013
Oryctolagus cuniculus (J7M9D0), Oryctolagus cuniculus
brenda
Endo, S.; Noda, M.; Ikari, A.; Tatematsu, K.; El-Kabbani, O.; Hara, A.; Kitade, Y.; Matsunaga, T.
Characterization of hamster NAD+-dependent 3(17)beta-hydroxysteroid dehydrogenase belonging to the aldo-keto reductase 1C subfamily
J. Biochem.
158
425-434
2015
Mesocricetus auratus (A0A097ZMY7), Mesocricetus auratus
brenda
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Release 2026.1 (March 2026)
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