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Information on EC 1.14.14.73 - albendazole monooxygenase (sulfoxide-forming) and Organism(s) Homo sapiens and UniProt Accession P08684

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IUBMB Comments
This is one of the activities carried out by some microsomal cytochrome P-450 monooxygenases. A similar conversion is also carried out by a different microsomal enzyme (EC 1.14.13.32, albendazole monooxygenase (flavin-containing)), but it is estimated that cytochrome P-450s are responsible for 70% of the activity.
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This record set is specific for:
Homo sapiens
UNIPROT: P08684
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The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
cyp2j2, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CYP1A2
-
-
-
-
CYP2J2
CYP3A4
-
-
-
-
cytochrome P450 2J2
-
SYSTEMATIC NAME
IUBMB Comments
albendazole,[reduced NADPH-hemoprotein reductase]:oxygen oxidoreductase (sulfoxide-forming)
This is one of the activities carried out by some microsomal cytochrome P-450 monooxygenases. A similar conversion is also carried out by a different microsomal enzyme (EC 1.14.13.32, albendazole monooxygenase (flavin-containing)), but it is estimated that cytochrome P-450s are responsible for 70% of the activity.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
albendazole + [reduced NADPH-hemoprotein reductase] + O2
albendazole S-oxide + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
-
-
-
?
albendazole + [reduced NADPH-hemoprotein reductase] + O2
albendazole S-oxide + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
amiodarone + [reduced NADPH-hemoprotein reductase] + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
-
-
-
?
astemizole + [reduced NADPH-hemoprotein reductase] + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
-
-
-
?
cyclosporin + [reduced NADPH-hemoprotein reductase] + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
-
-
-
?
danazol + [reduced NADPH-hemoprotein reductase] + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
-
-
-
?
fenbendazole + [reduced NADPH-hemoprotein reductase] + O2
fenbendazole S-oxide + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
-
-
-
?
mesoridazine + [reduced NADPH-hemoprotein reductase] + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
-
-
-
?
thioridazine + [reduced NADPH-hemoprotein reductase] + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
albendazole + [reduced NADPH-hemoprotein reductase] + O2
albendazole S-oxide + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
-
-
-
?
fenbendazole + [reduced NADPH-hemoprotein reductase] + O2
fenbendazole S-oxide + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cytochrome P450
-
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ketoconazole
0.5-1 microM, 32% inhibition
ritonavir
0.5-1 microM, 34% inhibition
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
CP3A4_HUMAN
503
2
57343
Swiss-Prot
Secretory Pathway (Reliability: 1)
PDB
SCOP
CATH
UNIPROT
ORGANISM
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
homology modeling of structure
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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 (P51589), Homo sapiens
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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 (P51589), Homo sapiens
Manually annotated by BRENDA team