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Information on EC 1.14.14.73 - albendazole monooxygenase (sulfoxide-forming) for references in articles please use BRENDA:EC1.14.14.73
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EC Tree
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
cyp2j2,
more
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albendazole hydroxylase
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ambiguous
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albendazole sulfoxidase
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ambiguous
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CYP2J2
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gene name
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CYP3A4
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gene name
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albendazole + [reduced NADPH-hemoprotein reductase] + O2 = albendazole S-oxide + [oxidized NADPH-hemoprotein reductase] + H2O
(1)
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fenbendazole + [reduced NADPH-hemoprotein reductase] + O2 = fenbendazole S-oxide + [oxidized NADPH-hemoprotein reductase] + H2O
(2)
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albendazole,[reduced NADPH-hemoprotein reductase]:oxygen oxidoreductase (sulfoxide-forming)
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albendazole + [reduced NADPH-hemoprotein reductase] + O2
albendazole S-oxide + [oxidized NADPH-hemoprotein reductase] + H2O
amiodarone + [reduced NADPH-hemoprotein reductase] + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
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?
astemizole + [reduced NADPH-hemoprotein reductase] + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
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?
cyclosporin + [reduced NADPH-hemoprotein reductase] + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
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?
danazol + [reduced NADPH-hemoprotein reductase] + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
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?
fenbendazole + [reduced NADPH-hemoprotein reductase] + O2
fenbendazole S-oxide + [oxidized NADPH-hemoprotein reductase] + H2O
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?
mesoridazine + [reduced NADPH-hemoprotein reductase] + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
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?
thioridazine + [reduced NADPH-hemoprotein reductase] + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
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?
additional information
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enzyme is able to modify antihistamine drugs such as albendazole, amiodarone, astemizole, thioridazine, mesoridazine, and danazol. The substrates vary in size and overall topology from relatively rigid structures (amiodarone) to larger complex structures (cyclosporine). CYP2J2 metabolism is more restrictive than that of YP3A4 and limited, in general, to a single site for large compounds
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albendazole + [reduced NADPH-hemoprotein reductase] + O2
albendazole S-oxide + [oxidized NADPH-hemoprotein reductase] + H2O
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?
albendazole + [reduced NADPH-hemoprotein reductase] + O2
albendazole S-oxide + [oxidized NADPH-hemoprotein reductase] + H2O
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?
albendazole + [reduced NADPH-hemoprotein reductase] + O2
albendazole S-oxide + [oxidized NADPH-hemoprotein reductase] + H2O
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?
albendazole + [reduced NADPH-hemoprotein reductase] + O2
albendazole S-oxide + [oxidized NADPH-hemoprotein reductase] + H2O
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?
albendazole + [reduced NADPH-hemoprotein reductase] + O2
albendazole S-oxide + [oxidized NADPH-hemoprotein reductase] + H2O
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?
albendazole + [reduced NADPH-hemoprotein reductase] + O2
albendazole S-oxide + [oxidized NADPH-hemoprotein reductase] + H2O
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?
albendazole + [reduced NADPH-hemoprotein reductase] + O2
albendazole S-oxide + [oxidized NADPH-hemoprotein reductase] + H2O
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?
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albendazole + [reduced NADPH-hemoprotein reductase] + O2
albendazole S-oxide + [oxidized NADPH-hemoprotein reductase] + H2O
P51589
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?
fenbendazole + [reduced NADPH-hemoprotein reductase] + O2
fenbendazole S-oxide + [oxidized NADPH-hemoprotein reductase] + H2O
P51589
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?
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cytochrome P450
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ketoconazole
0.5-1 microM, 32% inhibition
ritonavir
0.5-1 microM, 34% inhibition
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brenda
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UniProt
brenda
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UniProt
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in bile of albendazole-treated animals, only albendazole S-oxide, but not the sulfone, is present
brenda
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brenda
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brenda
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brenda
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metabolism
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metabolism of albendazole to albendazole-sulfoxide by pig liver microsomes is dependent on both microsomal cytochrome P-450 and FAD-containing mono-oxygenase enzymes. the relative contributions of the two systems depend on the concentration of albendazole
physiological function
flavin monoxygenases and cytochrome P450 reductase contribute about 30% and 70%, respectively, to albendazole S-oxide production in vitro. CYP3A4 is the mainly contributing cytochrome component
physiological function
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two main enzymatic systems, cytochrome P450s and flavin-containing monooxygenase, are responsible for the sulfoxidation of albendazole. P450 inhibitors inhibit the production of (-)-albendazole S-oxide more than the production of (+)-albendazole S-oxide
physiological function
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in liver perfusion fluid of albendazole-treated animals, the concentration of albendazole-sulfoxide remains unchanged, as compared to control animals, whereas albendazole-sulfone is increased in treated animals
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CP3A4_HUMAN
503
2
57343
Swiss-Prot
FMO3_BOVIN
532
0
60093
Swiss-Prot
CP2J2_HUMAN
502
2
57611
Swiss-Prot
FMO3_CANLF
532
1
60070
Swiss-Prot
FMO3_HUMAN
532
1
60033
Swiss-Prot
FMO3_MACMU
532
1
60152
Swiss-Prot
FMO3_MOUSE
534
1
60516
Swiss-Prot
FMO3_PANTR
532
1
60052
Swiss-Prot
FMO3_RABIT
531
1
59815
Swiss-Prot
FMO3_RAT
531
0
59960
Swiss-Prot
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homology modeling of structure
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expression in Escherichia coli
expression in Escherichia coli
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expression in Escherichia coli
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cytochrome P-450c is induced potently in vivo by albendazole
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medicine
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enzyme is able to modify antihistamine drugs such as albendazole, amiodarone, astemizole, thioridazine, mesoridazine, and danazol with in vitro intrinsic clearance values ranging from 0.06 to 3.98 microl/min/pmol CYP2J2. Whereas isoform CYP3A4 commonly metabolizes compounds at multiple sites, CYP2J2 metabolism is more restrictive and limited, in general, to a single site for large compounds
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Wu, Z.; Lee, D.; Joo, J.; Shin, J.; Kang, W.; Oh, S.; Lee, D.; Lee, S.; Yea, S.; Lee, H.; Lee, T.; Liu, K.
CYP2J2 and CYP2C19 are the major enzymes responsible for metabolism of albendazole and fenbendazole in human liver microsomes and recombinant P450 assay systems
Antimicrob. Agents Chemother.
57
5448-5456
2013
Homo sapiens, Homo sapiens (P51589)
brenda
Rawden, H.; Kokwaro, G.; Ward, S.; Edwards, G.
Relative contribution of cytochromes P-450 and flavin-containing monoxygenases to the metabolism of albendazole by human liver microsomes
Br. J. Clin. Pharmacol.
49
313-322
2000
Homo sapiens (P08684)
brenda
Moroni, P.; Buronfosse, T.; Longin-Sauvageon, C.; Delatour, P.; Benoit, E.
Chiral sulfoxidation of albendazole by the flavin adenine dinucleotide-containing and cytochrome P450-dependent monooxygenases from rat liver microsomes
Drug Metab. Dispos.
23
160-165
1995
Rattus norvegicus
brenda
Lee, C.; Neul, D.; Clouser-Roche, A.; Dalvie, D.; Wester, M.; Jiang, Y.; Jones III, J.; Freiwald, S.; Zientek, M.; Totah, R.
Identification of novel substrates for human cytochrome P450 2J2
Drug Metab. Dispos.
38
347-356
2010
Homo sapiens, Homo sapiens (P51589)
brenda
Gul, T.; Krzek, M.; Permentier, H.; Fraaije, M.; Bischoff, R.
Microbial flavoprotein monooxygenases as mimics of mammalian flavin-containing monooxygenases for the enantioselective preparation of drug metabolites
Drug Metab. Dispos.
44
1270-1276
2016
Rhodococcus jostii, Thermothelomyces thermophilus
brenda
Souhaili-El Amri, H.; Mothe, O.; Totis, M.; Masson, C.; Batt, A.M.; Delatour, P.; Siest, G.
Albendazole sulfonation by rat liver cytochrome P-450c
J. Pharmacol. Exp. Ther.
246
758-764
1988
Rattus norvegicus
brenda
Souhaili El Amri, H.; Fargetton, X.; Delatour, P.; Batt, A.
Sulphoxidation of albendazole by the FAD-containing and cytochrome p-450 dependent mono-oxygenases from pig liver microsomes
Xenobiotica
17
1159-1174
1987
Sus scrofa
brenda
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