BRENDA - Enzyme Database show
show all sequences of 1.14.14.73

Chiral sulfoxidation of albendazole by the flavin adenine dinucleotide-containing and cytochrome P450-dependent monooxygenases from rat liver microsomes

Moroni, P.; Buronfosse, T.; Longin-Sauvageon, C.; Delatour, P.; Benoit, E.; Drug Metab. Dispos. 23, 160-165 (1995)

Data extracted from this reference:

Inhibitors
Inhibitors
Commentary
Organism
Structure
clotrimazole
-
Rattus norvegicus
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
microsome
-
Rattus norvegicus
-
-
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Rattus norvegicus
-
-
-
Source Tissue
Source Tissue
Commentary
Organism
Textmining
liver
-
Rattus norvegicus
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
albendazole + [reduced NADPH-hemoprotein reductase] + O2
-
744768
Rattus norvegicus
albendazole S-oxide + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
Cofactor
Cofactor
Commentary
Organism
Structure
cytochrome P450
-
Rattus norvegicus
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
cytochrome P450
-
Rattus norvegicus
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
clotrimazole
-
Rattus norvegicus
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
microsome
-
Rattus norvegicus
-
-
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
liver
-
Rattus norvegicus
-
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
albendazole + [reduced NADPH-hemoprotein reductase] + O2
-
744768
Rattus norvegicus
albendazole S-oxide + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
General Information
General Information
Commentary
Organism
physiological function
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
Rattus norvegicus
General Information (protein specific)
General Information
Commentary
Organism
physiological function
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
Rattus norvegicus
Other publictions for EC 1.14.14.73
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [C]
Temperature Range [C]
Temperature Stability [C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [C] (protein specific)
Temperature Range [C] (protein specific)
Temperature Stability [C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
744771
Gul
Microbial flavoprotein monoox ...
Rhodococcus jostii, Thermothelomyces thermophilus
Drug Metab. Dispos.
44
1270-1276
2016
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2
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2
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744049
Wu
CYP2J2 and CYP2C19 are the ma ...
Homo sapiens
Antimicrob. Agents Chemother.
57
5448-5456
2013
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1
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2
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744770
Lee
Identification of novel subst ...
Homo sapiens
Drug Metab. Dispos.
38
347-356
2010
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1
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1
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8
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744610
Rawden
Relative contribution of cyto ...
Homo sapiens
Br. J. Clin. Pharmacol.
49
313-322
2000
-
-
-
-
-
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2
-
1
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1
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1
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1
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1
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1
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1
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1
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1
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1
1
-
-
-
744768
Moroni
Chiral sulfoxidation of alben ...
Rattus norvegicus
Drug Metab. Dispos.
23
160-165
1995
-
-
-
-
-
-
1
-
1
-
-
-
-
1
-
-
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1
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1
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1
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1
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1
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1
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1
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1
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1
1
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-
745602
Souhaili-El Amri
Albendazole sulfonation by ra ...
Rattus norvegicus
J. Pharmacol. Exp. Ther.
246
758-764
1988
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1
1
1
1
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746557
Souhaili El Amri
Sulphoxidation of albendazole ...
Sus scrofa
Xenobiotica
17
1159-1174
1987
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