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Drug-Target Interaction

Drug

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PubChem ID:3033
Structure:
Synonyms:
(2,6-Dichlorophenyl)amino]benzeneacetic acid
15307-81-0
15307-81-0 (mono-potassium salt)
15307-86-5
2-((2,6-Dichlorophenyl)amino)benzeneacetic acid
2-(2,6-Dichloroanilino)phenylacetic Acid
2-(2,6-Dichlorophenylamino)phenylacetic acid
2-[(2,6-Dichlorophenyl)amino]benzeneacetic acid
2-[2,6-DICHLOROPHENYL)AMINO]BENZENEACETIC ACID
2-[2-(2,6-dichloroanilino)phenyl]acetic acid
2-[2-(2,6-Dichlorophenylamino)phenyl]acetic acid
2-[2-[(2,6-dichlorophenyl)amino]phenyl]acetic acid
2b17
AC1L1F0T
ACETIC ACID, (o-(2,6-DICHLOROANILINO)PHENYL)-
Acetic acid, [o-(2,6-dichloroanilino)phenyl]- (8CI)
AIDS-104206
AIDS104206
AKOS001579542
Apo-Diclo
Assaren
Benfofen
Benzeneacetic acid, 2-((2,6-dichlorophenyl)amino)-
Benzeneacetic acid, 2-((2,6-dichlorophenyl)amino)- (9CI)
Benzeneacetic acid, 2-[(2,6-dichlorophenyl)amino]-
BIDD:GT0380
BPBio1_000516
BRD-K08252256-236-05-6
BRN 2146636
BSPBio_000468
BSPBio_002169
C01690
C14H11Cl2NO2
CHEBI:47381
CHEMBL139
cMAP_000014
D07816
D30801
D3748
DB00586
Dichlofenac
Dichlofenal
Diclac
Diclo-Phlogont
Diclo-Puren
Diclobenin
Diclofenac
Diclofenac (INN)
Diclofenac acid
Diclofenac Potassium
Diclofenac Sodium
Diclofenac [INN:BAN]
Diclofenaco
Diclofenaco [INN-Spanish]
Diclofenacum
Diclofenacum [INN-Latin]
Diclofenamic acid
Diclomelan
Diclonate P
Diclophenac
Diclord
Dicloreum
Dicloreuma
Dicrofenac
DIF
DivK1c_000272
DivK1c_000402
Dolobasan
Duravolten
Dyloject
Ecofenac
Effekton
EINECS 239-348-5
Feloran
GP-45,840
henyl)-o-aminophenylacetic acid
HMS2090C10
HMS501E04
HSDB 7234
I14-7739
IDI1_000272
IDI1_000402
ISV-205
KBio1_000272
KBio1_000402
KBio2_001410
KBio2_002306
KBio2_003978
KBio2_004874
KBio2_006546
KBio2_007442
KBio3_001389
KBio3_002786
KBioGR_001051
KBioGR_002306
KBioSS_001410
KBioSS_002308
Lopac0_000441
LS-11575
N-(2,6-Dichlorop
NCGC00021125-01
NCGC00021125-02
NINDS_000272
NINDS_000402
Novapirina
Novo-Difenac
Novo-Difenac SR
Nu-Diclo
Oprea1_011155
Orthofen
Orthophen
Ortofen
Pennsaid
Prestwick0_000594
Prestwick1_000594
Prestwick2_000594
Prestwick3_000594
Primofenac
ProSorb-D
Rhumalgan
SBB068617
Sodium Diclofenac
Solaraze
Solaraze (TN)
Solaraze T
SPBio_001081
SPBio_002687
Spectrum2_000991
Spectrum3_000385
Spectrum4_000506
Spectrum5_000867
Spectrum_000930
SR-38
STK984493
Transfenac
UNII-144O8QL0L1
UNM000001216103
Voldal
Voltaflan
Voltaren
Voltaren Ophtha
Voltaren ophthalmic
Voltaren Rapide
Voltaren SR
Voltaren-XR
Voltarol
Xenid
[2-(2,6-dichloroanilino)phenyl]acetic acid
[o-(2,6-Dichloroanilino)phenyl]acetic acid
{2-[(2,6-dichlorophenyl)amino]phenyl}acetic acid
ATC-Codes:

Target

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Uniprot ID:CP1A1_HUMAN
Synonyms:
CYPIA1
Cytochrome P450 1A1
P450 form 6
P450-C
P450-P1
EC-Numbers:1.14.14.1
Organism:Homo sapiens
Human
PDB IDs:-

Binding Affinities:

Ki: Kd:Ic 50:Ec50/Ic50:
----
----
----
----

References:

10572000
11124228
Interaction of delavirdine with human liver microsomal cytochrome P450: inhibition of CYP2C9, CYP2C19, and CYP2D6.. R L Voorman; N A Payne; L C Wienkers; M J Hauer; P E Sanders (2001) Drug metabolism and disposition: the biological fate of chemicals display abstract
Delavirdine, a non-nucleoside inhibitor of HIV-1 reverse transcriptase, is metabolized primarily through desalkylation catalyzed by CYP3A4 and CYP2D6 and by pyridine hydroxylation catalyzed by CYP3A4. It is also an irreversible inhibitor of CYP3A4. The interaction of delavirdine with CYP2C9 was examined with pooled human liver microsomes using diclofenac 4'-hydroxylation as a reporter of CYP2C9 catalytic activity. As delavirdine concentration was increased from 0 to 100 microM, the K(M) for diclofenac metabolism rose from 4.5+/-0.5 to 21+/-6 microM, and V(max) declined from 4.2+/-0.1 to 0.54+/-0.08 nmol/min/mg of protein, characteristic of mixed-type inhibition. Nonlinear regression analysis revealed an apparent K(i) of 2.6+/-0.4 microM. There was no evidence for bioactivation as prerequisite to inhibition of CYP2C9. Desalkyl delavirdine, the major circulating metabolite of delavirdine, had no apparent effect on microsomal CYP2C9 activity at concentrations up to 20 microM. Several analogs of delavirdine showed similar inhibition of CYP2C9. Delavirdine significantly inhibited cDNA-expressed CYP2C19-catalyzed (S)-mephenytoin 4'-hydroxylation in a noncompetitive manner, with an apparent K(i) of 24+/-3 microM. Delavirdine at concentrations up to 100 microM did not inhibit the activity of CYP1A2 or -2E1. Delavirdine competitively inhibited recombinant CYP2D6 activity with a K(i) of 12.8+/-1.8 microM, similar to the observed K(M) for delavirdine desalkylation. These results, along with previously reported experiments, indicate that delavirdine can partially inhibit CYP2C9, -2C19, -2D6, and -3A4, although the degree of inhibition in vivo would be subject to a variety of additional factors.
11502726
Mechanism-based inactivation of CYP2C11 by diclofenac.. Y Masubuchi; A Ose; T Horie (2001) Drug metabolism and disposition: the biological fate of chemicals display abstract
It has been known that diclofenac is biotransformed into chemically reactive metabolites, which bind covalently to liver microsomal proteins, including cytochrome P450 enzyme(s). We have investigated the ability and selectivity of diclofenac to inactivate P450 enzymes. Preincubation of microsomes of untreated rats with diclofenac in the presence of NADPH resulted in time-dependent loss of testosterone 2alpha- and 16alpha-hydroxylation activities. No effect of the preincubation was observed on ethoxyresorufin O-deethylase, pentoxyresorufin O-depentylase, or testosterone 6beta-hydroxylation activity. The time-dependent decreases in testosterone 2alpha- and 16alpha-hydroxylation activities followed the pseudo-first order kinetics and were saturable with increasing diclofenac concentrations. Reduced glutathione was not capable of protecting against the decrease in the enzyme activities. These data establish that a mechanism-based inactivation of CYP2C11 occurs during the oxidative metabolism of diclofenac. The diclofenac concentrations required to achieve the half-maximal rate of inactivation (K(I)) were 3 to 4 microM, which were close to K(m) for the low-K(m) components for diclofenac 4'- and 5-hydroxylation activities (7.29 and 4.43 microM, respectively). Anti-CYP2C11 IgG inhibited diclofenac 4'- and 5-hydroxylation activities, indicating that CYP2C11 is a major isozyme responsible for these aromatic oxidations. The preincubation of microsomes with 4'- or 5-hydroxydiclofenac did not cause a decrease in testosterone 2alpha- or 16alpha-hydroxylation activity, suggesting that neither of the primary metabolites is a precursor of the metabolite that inactivates CYP2C11. Therefore, a highly reactive intermediate(s) inactivating CYP2C11, probably arene-oxide, appears to be generated during the process of diclofenac 4'- and/or 5-hydroxylation. Diclofenac metabolism in human liver microsomes did not cause inactivation of CYP2C9, a major isozyme involved in diclofenac 4'-hydroxylation. Because the human microsomes have high diclofenac 4'-hydroxylation but not 5-hydroxylation activity, importance of the latter pathway in the inactivation is suggested.
11853173
Inhibition of human hepatic cytochrome P450s and steroidogenic CYP17 by nonylphenol.. Toshiro Niwa; Yumi Maekawa; Megumi Fujimoto; Kae Kishimoto; Yoshiyasu Yabusaki; Fumihide Ishibashi; Masanao Katagiri (2002) Biological & pharmaceutical bulletin display abstract
Effect of nonylphenol on aminopyrine N-demethylase activity, a typical drug-metabolizing enzyme activity, by ten kinds of human hepatic cytochrome P450s (CYP) and on progesterone 17alpha-hydroxylase activity by steroidogenic CYP17 was investigated. When determined at 2 mM substrate concentration, nonylphenol (1 mM) most efficiently inhibited aminopyrine N-demethylation by CYP2C9 and CYP2C19, by 61% and 59%, respectively, followed by CYP2D6, CYP1A2, CYP2C18 and CYP2C8 (46-51%), whereas inhibition of the activities by other CYPs was less than 27%. Additionally, nonylphenol competitively inhibited diclofenac 4'-hydroxylation by CYP2C9 and S-mephenytoin 4'-hydroxylation by CYP2C19 with Ki values of 5.3 and 37 microM, respectively. Furthermore, nonylphenol exhibited a competitive inhibition of progesterone 17alpha-hydroxylase activity by CYP17 with Ki value of 62 microM. These results suggest that nonylphenol inhibits human hepatic CYPs, especially CYP2C9 and CYP2C19, and steroidogenic CYP17 activities.