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Record Information
Version3.6
Creation Date2012-09-06 15:16:51 UTC
Update Date2016-02-11 01:32:02 UTC
HMDB IDHMDB15242
Secondary Accession NumbersNone
Metabolite Identification
Common NameMiconazole
DescriptionMiconazole is only found in individuals that have used or taken this drug. It is an imidazole antifungal agent that is used topically and by intravenous infusion. [PubChem]Miconazole interacts with 14-α demethylase, a cytochrome P-450 enzyme necessary to convert lanosterol to ergosterol. As ergosterol is an essential component of the fungal cell membrane, inhibition of its synthesis results in increased cellular permeability causing leakage of cellular contents. Miconazole may also inhibit endogenous respiration, interact with membrane phospholipids, inhibit the transformation of yeasts to mycelial forms, inhibit purine uptake, and impair triglyceride and/or phospholipid biosynthesis.
Structure
Thumb
Synonyms
ValueSource
MonistatKegg
MCZHMDB
Chemical FormulaC18H14Cl4N2O
Average Molecular Weight416.129
Monoisotopic Molecular Weight413.986023908
IUPAC Name1-[2-(2,4-dichlorophenyl)-2-[(2,4-dichlorophenyl)methoxy]ethyl]-1H-imidazole
Traditional Namemiconazole
CAS Registry Number22916-47-8
SMILES
ClC1=CC(Cl)=C(COC(CN2C=CN=C2)C2=C(Cl)C=C(Cl)C=C2)C=C1
InChI Identifier
InChI=1S/C18H14Cl4N2O/c19-13-2-1-12(16(21)7-13)10-25-18(9-24-6-5-23-11-24)15-4-3-14(20)8-17(15)22/h1-8,11,18H,9-10H2
InChI KeyInChIKey=BYBLEWFAAKGYCD-UHFFFAOYSA-N
Chemical Taxonomy
DescriptionThis compound belongs to the class of organic compounds known as benzylethers. These are aromatic ethers with the general formula ROCR' (R = alkyl, aryl; R'=benzene).
KingdomOrganic compounds
Super ClassBenzenoids
ClassBenzene and substituted derivatives
Sub ClassBenzylethers
Direct ParentBenzylethers
Alternative Parents
Substituents
  • Benzylether
  • 1,3-dichlorobenzene
  • Halobenzene
  • Chlorobenzene
  • N-substituted imidazole
  • Aryl halide
  • Aryl chloride
  • Heteroaromatic compound
  • Imidazole
  • Azole
  • Azacycle
  • Organoheterocyclic compound
  • Ether
  • Dialkyl ether
  • Hydrocarbon derivative
  • Organooxygen compound
  • Organonitrogen compound
  • Organochloride
  • Organohalogen compound
  • Aromatic heteromonocyclic compound
Molecular FrameworkAromatic heteromonocyclic compounds
External Descriptors
Ontology
StatusExpected but not Quantified
Origin
  • Drug
Biofunction
  • Antifungal Agents
Application
  • Pharmaceutical
Cellular locations
  • Cytoplasm
  • Membrane
Physical Properties
StateSolid
Experimental Properties
PropertyValueReference
Melting Point159 - 163 °CNot Available
Boiling PointNot AvailableNot Available
Water Solubility7.63e-04 g/LNot Available
LogP6.1Not Available
Predicted Properties
PropertyValueSource
Water Solubility0.000763 mg/mLALOGPS
logP5.86ALOGPS
logP5.96ChemAxon
logS-5.7ALOGPS
pKa (Strongest Basic)6.77ChemAxon
Physiological Charge0ChemAxon
Hydrogen Acceptor Count2ChemAxon
Hydrogen Donor Count0ChemAxon
Polar Surface Area27.05 Å2ChemAxon
Rotatable Bond Count6ChemAxon
Refractivity103.07 m3·mol-1ChemAxon
Polarizability39.54 Å3ChemAxon
Number of Rings3ChemAxon
Bioavailability1ChemAxon
Rule of FiveYesChemAxon
Ghose FilterYesChemAxon
Veber's RuleYesChemAxon
MDDR-like RuleYesChemAxon
Spectra
Spectra
Spectrum TypeDescriptionSplash Key
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, PositiveNot Available
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, PositiveNot Available
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, PositiveNot Available
MSMass Spectrum (Electron Ionization)splash10-0bt9-4900000000-3f143064c2acde7e15a4View in MoNA
Biological Properties
Cellular Locations
  • Cytoplasm
  • Membrane
Biofluid Locations
  • Blood
  • Urine
Tissue LocationNot Available
PathwaysNot Available
Normal Concentrations
BiofluidStatusValueAgeSexConditionReferenceDetails
BloodExpected but not QuantifiedNot ApplicableNot AvailableNot AvailableTaking drug identified by DrugBank entry DB01110
  • Not Applicable
details
UrineExpected but not QuantifiedNot ApplicableNot AvailableNot AvailableTaking drug identified by DrugBank entry DB01110
  • Not Applicable
details
Abnormal Concentrations
Not Available
Predicted Concentrations
BiofluidValueOriginal ageOriginal sexOriginal conditionComments
Blood0-2 uMAdult (>18 years old)BothNormalPredicted based on drug qualities
Blood0-1 umol/mmol creatinineAdult (>18 years old)BothNormalPredicted based on drug qualities
Associated Disorders and Diseases
Disease ReferencesNone
Associated OMIM IDsNone
DrugBank IDDB01110
DrugBank Metabolite IDNot Available
Phenol Explorer Compound IDNot Available
Phenol Explorer Metabolite IDNot Available
FoodDB IDNot Available
KNApSAcK IDNot Available
Chemspider ID4044
KEGG Compound IDC08070
BioCyc IDNot Available
BiGG IDNot Available
Wikipedia LinkMiconazole
NuGOwiki LinkHMDB15242
Metagene LinkHMDB15242
METLIN IDNot Available
PubChem Compound4189
PDB IDNot Available
ChEBI ID6923
References
Synthesis ReferenceNot Available
Material Safety Data Sheet (MSDS)Download (PDF)
General ReferencesNot Available

Enzymes

General function:
Involved in monooxygenase activity
Specific function:
Has steroid 11-beta-hydroxylase activity. In addition to this activity, the 18 or 19-hydroxylation of steroids and the aromatization of androstendione to estrone have also been ascribed to cytochrome P450 XIB.
Gene Name:
CYP11B1
Uniprot ID:
P15538
Molecular weight:
57572.44
References
  1. Preissner S, Kroll K, Dunkel M, Senger C, Goldsobel G, Kuzman D, Guenther S, Winnenburg R, Schroeder M, Preissner R: SuperCYP: a comprehensive database on Cytochrome P450 enzymes including a tool for analysis of CYP-drug interactions. Nucleic Acids Res. 2010 Jan;38(Database issue):D237-43. Epub 2009 Nov 24. [19934256 ]
General function:
Involved in oxidoreductase activity
Specific function:
Produces nitric oxide (NO) which is a messenger molecule with diverse functions throughout the body. In macrophages, NO mediates tumoricidal and bactericidal actions. Also has nitrosylase activity and mediates cysteine S-nitrosylation of cytoplasmic target proteins such COX2.
Gene Name:
NOS2
Uniprot ID:
P35228
Molecular weight:
131116.3
References
  1. Wolff DJ, Datto GA, Samatovicz RA: The dual mode of inhibition of calmodulin-dependent nitric-oxide synthase by antifungal imidazole agents. J Biol Chem. 1993 May 5;268(13):9430-6. [7683652 ]
  2. Bogle RG, Whitley GS, Soo SC, Johnstone AP, Vallance P: Effect of anti-fungal imidazoles on mRNA levels and enzyme activity of inducible nitric oxide synthase. Br J Pharmacol. 1994 Apr;111(4):1257-61. [7518297 ]
  3. Sennequier N, Wolan D, Stuehr DJ: Antifungal imidazoles block assembly of inducible NO synthase into an active dimer. J Biol Chem. 1999 Jan 8;274(2):930-8. [9873034 ]
  4. Dudek RR, Conforto A, Pinto V, Wildhirt S, Suzuki H: Inhibition of endothelial nitric oxide synthase by cytochrome P-450 reductase inhibitors. Proc Soc Exp Biol Med. 1995 May;209(1):60-4. [7536941 ]
General function:
Involved in oxidoreductase activity
Specific function:
Produces nitric oxide (NO) which is implicated in vascular smooth muscle relaxation through a cGMP-mediated signal transduction pathway. NO mediates vascular endothelial growth factor (VEGF)-induced angiogenesis in coronary vessels and promotes blood clotting through the activation of platelets. Isoform eNOS13C: Lacks eNOS activity, dominant-negative form that may down-regulate eNOS activity by forming heterodimers with isoform 1.
Gene Name:
NOS3
Uniprot ID:
P29474
Molecular weight:
133273.59
References
  1. Wolff DJ, Datto GA, Samatovicz RA: The dual mode of inhibition of calmodulin-dependent nitric-oxide synthase by antifungal imidazole agents. J Biol Chem. 1993 May 5;268(13):9430-6. [7683652 ]
  2. Bogle RG, Whitley GS, Soo SC, Johnstone AP, Vallance P: Effect of anti-fungal imidazoles on mRNA levels and enzyme activity of inducible nitric oxide synthase. Br J Pharmacol. 1994 Apr;111(4):1257-61. [7518297 ]
  3. Sennequier N, Wolan D, Stuehr DJ: Antifungal imidazoles block assembly of inducible NO synthase into an active dimer. J Biol Chem. 1999 Jan 8;274(2):930-8. [9873034 ]
  4. Dudek RR, Conforto A, Pinto V, Wildhirt S, Suzuki H: Inhibition of endothelial nitric oxide synthase by cytochrome P-450 reductase inhibitors. Proc Soc Exp Biol Med. 1995 May;209(1):60-4. [7536941 ]
General function:
Involved in monooxygenase activity
Specific function:
Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It performs a variety of oxidation reactions (e.g. caffeine 8-oxidation, omeprazole sulphoxidation, midazolam 1'-hydroxylation and midazolam 4-hydroxylation) of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics. Acts as a 1,8-cineole 2-exo-monooxygenase. The enzyme also hydroxylates etoposide.
Gene Name:
CYP3A4
Uniprot ID:
P08684
Molecular weight:
57255.585
References
  1. Sakaeda T, Iwaki K, Kakumoto M, Nishikawa M, Niwa T, Jin JS, Nakamura T, Nishiguchi K, Okamura N, Okumura K: Effect of micafungin on cytochrome P450 3A4 and multidrug resistance protein 1 activities, and its comparison with azole antifungal drugs. J Pharm Pharmacol. 2005 Jun;57(6):759-64. [15969931 ]
  2. Preissner S, Kroll K, Dunkel M, Senger C, Goldsobel G, Kuzman D, Guenther S, Winnenburg R, Schroeder M, Preissner R: SuperCYP: a comprehensive database on Cytochrome P450 enzymes including a tool for analysis of CYP-drug interactions. Nucleic Acids Res. 2010 Jan;38(Database issue):D237-43. Epub 2009 Nov 24. [19934256 ]
General function:
Involved in monooxygenase activity
Specific function:
Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics. This enzyme contributes to the wide pharmacokinetics variability of the metabolism of drugs such as S-warfarin, diclofenac, phenytoin, tolbutamide and losartan.
Gene Name:
CYP2C9
Uniprot ID:
P11712
Molecular weight:
55627.365
References
  1. Preissner S, Kroll K, Dunkel M, Senger C, Goldsobel G, Kuzman D, Guenther S, Winnenburg R, Schroeder M, Preissner R: SuperCYP: a comprehensive database on Cytochrome P450 enzymes including a tool for analysis of CYP-drug interactions. Nucleic Acids Res. 2010 Jan;38(Database issue):D237-43. Epub 2009 Nov 24. [19934256 ]
General function:
Involved in monooxygenase activity
Specific function:
Responsible for the metabolism of a number of therapeutic agents such as the anticonvulsant drug S-mephenytoin, omeprazole, proguanil, certain barbiturates, diazepam, propranolol, citalopram and imipramine.
Gene Name:
CYP2C19
Uniprot ID:
P33261
Molecular weight:
55944.565
References
  1. Preissner S, Kroll K, Dunkel M, Senger C, Goldsobel G, Kuzman D, Guenther S, Winnenburg R, Schroeder M, Preissner R: SuperCYP: a comprehensive database on Cytochrome P450 enzymes including a tool for analysis of CYP-drug interactions. Nucleic Acids Res. 2010 Jan;38(Database issue):D237-43. Epub 2009 Nov 24. [19934256 ]
General function:
Involved in monooxygenase activity
Specific function:
Metabolizes several precarcinogens, drugs, and solvents to reactive metabolites. Inactivates a number of drugs and xenobiotics and also bioactivates many xenobiotic substrates to their hepatotoxic or carcinogenic forms.
Gene Name:
CYP2E1
Uniprot ID:
P05181
Molecular weight:
56848.42
References
  1. Preissner S, Kroll K, Dunkel M, Senger C, Goldsobel G, Kuzman D, Guenther S, Winnenburg R, Schroeder M, Preissner R: SuperCYP: a comprehensive database on Cytochrome P450 enzymes including a tool for analysis of CYP-drug interactions. Nucleic Acids Res. 2010 Jan;38(Database issue):D237-43. Epub 2009 Nov 24. [19934256 ]
General function:
Involved in monooxygenase activity
Specific function:
Responsible for the metabolism of many drugs and environmental chemicals that it oxidizes. It is involved in the metabolism of drugs such as antiarrhythmics, adrenoceptor antagonists, and tricyclic antidepressants.
Gene Name:
CYP2D6
Uniprot ID:
P10635
Molecular weight:
55768.94
References
  1. Preissner S, Kroll K, Dunkel M, Senger C, Goldsobel G, Kuzman D, Guenther S, Winnenburg R, Schroeder M, Preissner R: SuperCYP: a comprehensive database on Cytochrome P450 enzymes including a tool for analysis of CYP-drug interactions. Nucleic Acids Res. 2010 Jan;38(Database issue):D237-43. Epub 2009 Nov 24. [19934256 ]
General function:
Involved in monooxygenase activity
Specific function:
Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics. Acts as a 1,4-cineole 2-exo-monooxygenase.
Gene Name:
CYP2B6
Uniprot ID:
P20813
Molecular weight:
56277.81
References
  1. Preissner S, Kroll K, Dunkel M, Senger C, Goldsobel G, Kuzman D, Guenther S, Winnenburg R, Schroeder M, Preissner R: SuperCYP: a comprehensive database on Cytochrome P450 enzymes including a tool for analysis of CYP-drug interactions. Nucleic Acids Res. 2010 Jan;38(Database issue):D237-43. Epub 2009 Nov 24. [19934256 ]
General function:
Involved in monooxygenase activity
Specific function:
Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics. Most active in catalyzing 2-hydroxylation. Caffeine is metabolized primarily by cytochrome CYP1A2 in the liver through an initial N3-demethylation. Also acts in the metabolism of aflatoxin B1 and acetaminophen. Participates in the bioactivation of carcinogenic aromatic and heterocyclic amines. Catalizes the N-hydroxylation of heterocyclic amines and the O-deethylation of phenacetin.
Gene Name:
CYP1A2
Uniprot ID:
P05177
Molecular weight:
58406.915
References
  1. Preissner S, Kroll K, Dunkel M, Senger C, Goldsobel G, Kuzman D, Guenther S, Winnenburg R, Schroeder M, Preissner R: SuperCYP: a comprehensive database on Cytochrome P450 enzymes including a tool for analysis of CYP-drug interactions. Nucleic Acids Res. 2010 Jan;38(Database issue):D237-43. Epub 2009 Nov 24. [19934256 ]
General function:
Involved in monooxygenase activity
Specific function:
Catalyzes the formation of aromatic C18 estrogens from C19 androgens.
Gene Name:
CYP19A1
Uniprot ID:
P11511
Molecular weight:
57882.48
References
  1. Preissner S, Kroll K, Dunkel M, Senger C, Goldsobel G, Kuzman D, Guenther S, Winnenburg R, Schroeder M, Preissner R: SuperCYP: a comprehensive database on Cytochrome P450 enzymes including a tool for analysis of CYP-drug interactions. Nucleic Acids Res. 2010 Jan;38(Database issue):D237-43. Epub 2009 Nov 24. [19934256 ]
General function:
Involved in monooxygenase activity
Specific function:
Exhibits a high coumarin 7-hydroxylase activity. Can act in the hydroxylation of the anti-cancer drugs cyclophosphamide and ifosphamide. Competent in the metabolic activation of aflatoxin B1. Constitutes the major nicotine C-oxidase. Acts as a 1,4-cineole 2-exo-monooxygenase. Possesses low phenacetin O-deethylation activity.
Gene Name:
CYP2A6
Uniprot ID:
P11509
Molecular weight:
56517.005
References
  1. Preissner S, Kroll K, Dunkel M, Senger C, Goldsobel G, Kuzman D, Guenther S, Winnenburg R, Schroeder M, Preissner R: SuperCYP: a comprehensive database on Cytochrome P450 enzymes including a tool for analysis of CYP-drug interactions. Nucleic Acids Res. 2010 Jan;38(Database issue):D237-43. Epub 2009 Nov 24. [19934256 ]
General function:
Involved in ion channel activity
Specific function:
Potassium channel activated by both membrane depolarization or increase in cytosolic Ca(2+) that mediates export of K(+). It is also activated by the concentration of cytosolic Mg(2+). Its activation dampens the excitatory events that elevate the cytosolic Ca(2+) concentration and/or depolarize the cell membrane. It therefore contributes to repolarization of the membrane potential. Plays a key role in controlling excitability in a number of systems, such as regulation of the contraction of smooth muscle, the tuning of hair cells in the cochlea, regulation of transmitter release, and innate immunity. In smooth muscles, its activation by high level of Ca(2+), caused by ryanodine receptors in the sarcoplasmic reticulum, regulates the membrane potential. In cochlea cells, its number and kinetic properties partly determine the characteristic frequency of each hair cell and thereby helps to establish a tonotopic map. Kinetics of KCNMA1 channels are determined by alternative splicing, phosphorylation status and its combination with modulating beta subunits. Highly sensitive to both iberiotoxin (IbTx) and charybdotoxin (CTX)
Gene Name:
KCNMA1
Uniprot ID:
Q12791
Molecular weight:
137558.1
References
  1. Hatton CJ, Peers C: Effects of cytochrome P-450 inhibitors on ionic currents in isolated rat type I carotid body cells. Am J Physiol. 1996 Jul;271(1 Pt 1):C85-92. [8760033 ]
  2. Alvarez J, Montero M, Garcia-Sancho J: High affinity inhibition of Ca(2+)-dependent K+ channels by cytochrome P-450 inhibitors. J Biol Chem. 1992 Jun 15;267(17):11789-93. [1376313 ]
General function:
Involved in ion channel activity
Specific function:
Pore-forming (alpha) subunit of voltage-gated inwardly rectifying potassium channel. Channel properties are modulated by cAMP and subunit assembly. Mediates the rapidly activating component of the delayed rectifying potassium current in heart (IKr). Isoform 3 has no channel activity by itself, but modulates channel characteristics when associated with isoform 1
Gene Name:
KCNH2
Uniprot ID:
Q12809
Molecular weight:
126653.5
References
  1. Hatton CJ, Peers C: Effects of cytochrome P-450 inhibitors on ionic currents in isolated rat type I carotid body cells. Am J Physiol. 1996 Jul;271(1 Pt 1):C85-92. [8760033 ]
  2. Kikuchi K, Nagatomo T, Abe H, Kawakami K, Duff HJ, Makielski JC, January CT, Nakashima Y: Blockade of HERG cardiac K+ current by antifungal drug miconazole. Br J Pharmacol. 2005 Mar;144(6):840-8. [15778703 ]
General function:
Involved in ion channel activity
Specific function:
Pore-forming (alpha) subunit of voltage-gated potassium channel. Elicits a slowly activating, rectifying current. Channel properties may be modulated by cAMP and subunit assembly
Gene Name:
KCNH6
Uniprot ID:
Q9H252
Molecular weight:
109923.7
References
  1. Hatton CJ, Peers C: Effects of cytochrome P-450 inhibitors on ionic currents in isolated rat type I carotid body cells. Am J Physiol. 1996 Jul;271(1 Pt 1):C85-92. [8760033 ]
  2. Kikuchi K, Nagatomo T, Abe H, Kawakami K, Duff HJ, Makielski JC, January CT, Nakashima Y: Blockade of HERG cardiac K+ current by antifungal drug miconazole. Br J Pharmacol. 2005 Mar;144(6):840-8. [15778703 ]
General function:
Involved in calcium-activated potassium channel activity
Specific function:
Regulatory subunit of the calcium activated potassium KCNMA1 (maxiK) channel. Modulates the calcium sensitivity and gating kinetics of KCNMA1, thereby contributing to KCNMA1 channel diversity. Increases the apparent Ca(2+)/voltage sensitivity of the KCNMA1 channel. It also modifies KCNMA1 channel kinetics and alters its pharmacological properties. It slows down the activation and the deactivation kinetics of the channel. Acts as a negative regulator of smooth muscle contraction by enhancing the calcium sensitivity to KCNMA1. Its presence is also a requirement for internal binding of the KCNMA1 channel opener dehydrosoyasaponin I (DHS-1) triterpene glycoside and for external binding of the agonist hormone 17-beta-estradiol (E2). Increases the binding activity of charybdotoxin (CTX) toxin to KCNMA1 peptide blocker by increasing the CTX association rate and decreasing the dissociation rate
Gene Name:
KCNMB1
Uniprot ID:
Q16558
Molecular weight:
21797.3
References
  1. Hatton CJ, Peers C: Effects of cytochrome P-450 inhibitors on ionic currents in isolated rat type I carotid body cells. Am J Physiol. 1996 Jul;271(1 Pt 1):C85-92. [8760033 ]
  2. Alvarez J, Montero M, Garcia-Sancho J: High affinity inhibition of Ca(2+)-dependent K+ channels by cytochrome P-450 inhibitors. J Biol Chem. 1992 Jun 15;267(17):11789-93. [1376313 ]
General function:
Involved in calcium-activated potassium channel activity
Specific function:
Regulatory subunit of the calcium activated potassium KCNMA1 (maxiK) channel. Modulates the calcium sensitivity and gating kinetics of KCNMA1, thereby contributing to KCNMA1 channel diversity. Acts as a negative regulator that confers rapid and complete inactivation of KCNMA1 channel complex. May participate in KCNMA1 inactivation in chromaffin cells of the adrenal gland or in hippocampal CA1 neurons
Gene Name:
KCNMB2
Uniprot ID:
Q9Y691
Molecular weight:
27129.4
References
  1. Hatton CJ, Peers C: Effects of cytochrome P-450 inhibitors on ionic currents in isolated rat type I carotid body cells. Am J Physiol. 1996 Jul;271(1 Pt 1):C85-92. [8760033 ]
  2. Alvarez J, Montero M, Garcia-Sancho J: High affinity inhibition of Ca(2+)-dependent K+ channels by cytochrome P-450 inhibitors. J Biol Chem. 1992 Jun 15;267(17):11789-93. [1376313 ]
General function:
Involved in calcium-activated potassium channel activity
Specific function:
Regulatory subunit of the calcium activated potassium KCNMA1 (maxiK) channel. Modulates the calcium sensitivity and gating kinetics of KCNMA1, thereby contributing to KCNMA1 channel diversity. Alters the functional properties of the current expressed by the KCNMA1 channel. Isoform 2, isoform 3 and isoform 4 partially inactivate the current of KCNBMA. Isoform 4 induces a fast and incomplete inactivation of KCNMA1 channel that is detectable only at large depolarizations. In contrast, isoform 1 does not induce detectable inactivation of KCNMA1. Two or more subunits of KCNMB3 are required to block the KCNMA1 tetramer
Gene Name:
KCNMB3
Uniprot ID:
Q9NPA1
Molecular weight:
31603.3
References
  1. Hatton CJ, Peers C: Effects of cytochrome P-450 inhibitors on ionic currents in isolated rat type I carotid body cells. Am J Physiol. 1996 Jul;271(1 Pt 1):C85-92. [8760033 ]
  2. Alvarez J, Montero M, Garcia-Sancho J: High affinity inhibition of Ca(2+)-dependent K+ channels by cytochrome P-450 inhibitors. J Biol Chem. 1992 Jun 15;267(17):11789-93. [1376313 ]
General function:
Involved in calcium-activated potassium channel activity
Specific function:
Regulatory subunit of the calcium activated potassium KCNMA1 (maxiK) channel. Modulates the calcium sensitivity and gating kinetics of KCNMA1, thereby contributing to KCNMA1 channel diversity. Decreases the gating kinetics and calcium sensitivity of the KCNMA1 channel, but with fast deactivation kinetics. May decrease KCNMA1 channel openings at low calcium concentrations but increases channel openings at high calcium concentrations. Makes KCNMA1 channel resistant to 100 nM charybdotoxin (CTX) toxin concentrations
Gene Name:
KCNMB4
Uniprot ID:
Q86W47
Molecular weight:
23948.5
References
  1. Hatton CJ, Peers C: Effects of cytochrome P-450 inhibitors on ionic currents in isolated rat type I carotid body cells. Am J Physiol. 1996 Jul;271(1 Pt 1):C85-92. [8760033 ]
  2. Alvarez J, Montero M, Garcia-Sancho J: High affinity inhibition of Ca(2+)-dependent K+ channels by cytochrome P-450 inhibitors. J Biol Chem. 1992 Jun 15;267(17):11789-93. [1376313 ]
General function:
Involved in calmodulin binding
Specific function:
Forms a voltage-independent potassium channel activated by intracellular calcium. Activation is followed by membrane hyperpolarization. Thought to regulate neuronal excitability by contributing to the slow component of synaptic afterhyperpolarization. The channel is blocked by apamin
Gene Name:
KCNN1
Uniprot ID:
Q92952
Molecular weight:
59986.9
References
  1. Hatton CJ, Peers C: Effects of cytochrome P-450 inhibitors on ionic currents in isolated rat type I carotid body cells. Am J Physiol. 1996 Jul;271(1 Pt 1):C85-92. [8760033 ]
  2. Alvarez J, Montero M, Garcia-Sancho J: High affinity inhibition of Ca(2+)-dependent K+ channels by cytochrome P-450 inhibitors. J Biol Chem. 1992 Jun 15;267(17):11789-93. [1376313 ]
General function:
Involved in calmodulin binding
Specific function:
Forms a voltage-independent potassium channel activated by intracellular calcium. Activation is followed by membrane hyperpolarization. Thought to regulate neuronal excitability by contributing to the slow component of synaptic afterhyperpolarization. The channel is blocked by apamin
Gene Name:
KCNN2
Uniprot ID:
Q9H2S1
Molecular weight:
63759.0
References
  1. Hatton CJ, Peers C: Effects of cytochrome P-450 inhibitors on ionic currents in isolated rat type I carotid body cells. Am J Physiol. 1996 Jul;271(1 Pt 1):C85-92. [8760033 ]
  2. Alvarez J, Montero M, Garcia-Sancho J: High affinity inhibition of Ca(2+)-dependent K+ channels by cytochrome P-450 inhibitors. J Biol Chem. 1992 Jun 15;267(17):11789-93. [1376313 ]
General function:
Involved in calmodulin binding
Specific function:
Forms a voltage-independent potassium channel activated by intracellular calcium. Activation is followed by membrane hyperpolarization. Thought to regulate neuronal excitability by contributing to the slow component of synaptic afterhyperpolarization. The channel is blocked by apamin
Gene Name:
KCNN3
Uniprot ID:
Q9UGI6
Molecular weight:
82025.3
References
  1. Hatton CJ, Peers C: Effects of cytochrome P-450 inhibitors on ionic currents in isolated rat type I carotid body cells. Am J Physiol. 1996 Jul;271(1 Pt 1):C85-92. [8760033 ]
  2. Alvarez J, Montero M, Garcia-Sancho J: High affinity inhibition of Ca(2+)-dependent K+ channels by cytochrome P-450 inhibitors. J Biol Chem. 1992 Jun 15;267(17):11789-93. [1376313 ]
General function:
Involved in calmodulin binding
Specific function:
Forms a voltage-independent potassium channel that is activated by intracellular calcium. Activation is followed by membrane hyperpolarization which promotes calcium influx. The channel is blocked by clotrimazole and charybdotoxin but is insensitive to apamin
Gene Name:
KCNN4
Uniprot ID:
O15554
Molecular weight:
47695.1
References
  1. Hatton CJ, Peers C: Effects of cytochrome P-450 inhibitors on ionic currents in isolated rat type I carotid body cells. Am J Physiol. 1996 Jul;271(1 Pt 1):C85-92. [8760033 ]
  2. Alvarez J, Montero M, Garcia-Sancho J: High affinity inhibition of Ca(2+)-dependent K+ channels by cytochrome P-450 inhibitors. J Biol Chem. 1992 Jun 15;267(17):11789-93. [1376313 ]
General function:
Involved in ion channel activity
Specific function:
Pore-forming (alpha) subunit of voltage-gated potassium channel. Channel properties may be modulated by cAMP and subunit assembly
Gene Name:
KCNH7
Uniprot ID:
Q9NS40
Molecular weight:
134998.5
References
  1. Hatton CJ, Peers C: Effects of cytochrome P-450 inhibitors on ionic currents in isolated rat type I carotid body cells. Am J Physiol. 1996 Jul;271(1 Pt 1):C85-92. [8760033 ]
  2. Kikuchi K, Nagatomo T, Abe H, Kawakami K, Duff HJ, Makielski JC, January CT, Nakashima Y: Blockade of HERG cardiac K+ current by antifungal drug miconazole. Br J Pharmacol. 2005 Mar;144(6):840-8. [15778703 ]

Transporters

General function:
Involved in ATP binding
Specific function:
Energy-dependent efflux pump responsible for decreased drug accumulation in multidrug-resistant cells
Gene Name:
ABCB1
Uniprot ID:
P08183
Molecular weight:
141477.3
References
  1. Ekins S, Kim RB, Leake BF, Dantzig AH, Schuetz EG, Lan LB, Yasuda K, Shepard RL, Winter MA, Schuetz JD, Wikel JH, Wrighton SA: Three-dimensional quantitative structure-activity relationships of inhibitors of P-glycoprotein. Mol Pharmacol. 2002 May;61(5):964-73. [11961113 ]
  2. Schwab D, Fischer H, Tabatabaei A, Poli S, Huwyler J: Comparison of in vitro P-glycoprotein screening assays: recommendations for their use in drug discovery. J Med Chem. 2003 Apr 24;46(9):1716-25. [12699389 ]
  3. Yasuda K, Lan LB, Sanglard D, Furuya K, Schuetz JD, Schuetz EG: Interaction of cytochrome P450 3A inhibitors with P-glycoprotein. J Pharmacol Exp Ther. 2002 Oct;303(1):323-32. [12235267 ]