Local view for "http://wifo5-04.informatik.uni-mannheim.de/drugbank/resource/drugs/DB06770"
| Predicate | Value (sorted: default) |
|---|---|
| rdfs:label |
"Benzyl alcohol"
|
| rdf:type | |
| ns1:description |
"
100-51-6
approved
# Taylor PM, Chengelis CP, Miller WR, Parker GA, Gleason TR, Cozzi E: Evaluation of propofol containing 2% benzyl alcohol preservative in cats. J Feline Med Surg. 2012 Aug;14(8):516-26. doi: 10.1177/1098612X12440354. Epub 2012 Feb 24. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/22366290
# Novak E, Stubbs SS, Sanborn EC, Eustice RM: The tolerance and safety of intravenously administered benzyl alcohol in methylprednisolone sodium succinate formulations in normal human subjects. Toxicol Appl Pharmacol. 1972 Sep;23(1):54-61. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/4560999
# Meinking TL, Villar ME, Vicaria M, Eyerdam DH, Paquet D, Mertz-Rivera K, Rivera HF, Hiriart J, Reyna S: The clinical trials supporting benzyl alcohol lotion 5% (Ulesfia): a safe and effective topical treatment for head lice (pediculosis humanus capitis). Pediatr Dermatol. 2010 Jan-Feb;27(1):19-24. doi: 10.1111/j.1525-1470.2009.01059.x. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/ 20199404
Cornelis Jongsma, Leon H. B. Frijns, Paula A. M. Raven-Donners, "Method for the preparation of a pure alkali metal benzoate and benzyl alcohol." U.S. Patent US4296245, issued June, 1940.
Ulesfia (benzyl alcohol) lotion is indicated for the topical treatment of head lice infestation in patients 6 months of age and older. Ulesfia Lotion does not have ovicidal activity.
Benzyl alcohol inhibits lice from closing their respiratory spiracles, allowing the vehicle to obstruct the spiracles and causing the lice to asphyxiate.
1250 mg/kg (rat, oral) LD50
400 mg/kg IPR-RAT LD50
2000 mg/kg SKN-RBT LD50
53 mg/kg IVN-RAT LD50
2500 mg/kg ORL-GPG LD50
This compound belongs to the benzene and substituted derivatives. These are aromatic compounds containing at least one benzene ring.
Benzene and Substituted Derivatives
Organic Compounds
Benzenoids
Benzene and Substituted Derivatives
Primary Alcohols
Polyamines
polyamine
primary alcohol
alcohol
(Hydroxymethyl)benzene
Alcoholum benzylicum
Alcool benzylique
Alcoolbenzylique
alpha-Hydroxytoluene
alpha-Toluenol
Aromatic alcohol
Bentalol
Benzalalcohol
Benzalcohol
Benzenecarbinol
Benzenemethanol
Benzoyl alcohol
Benzyl alcohol
Benzylalkohol
Benzylic alcohol
Hydroxymethylbenzene
Phenylcarbinol
Phenylmethanol
Phenylmethyl alcohol
Ulesfia
Anesthetics, Local
Pediculicides
Head lice
Lotion
Topical
5%
7294342
United States
2007-11-13
2024-05-19
6793931
United States
2004-09-21
2022-07-11
6139859
United States
2000-10-31
2017-08-11
5858383
United States
1999-01-12
2017-08-11
logP
1.07
ALOGPS
logS
-0.61
ALOGPS
Water Solubility
2.68e+01 g/l
ALOGPS
logP
1.21
ChemAxon
IUPAC Name
phenylmethanol
ChemAxon
Traditional IUPAC Name
benzyl alcohol
ChemAxon
Molecular Weight
108.1378
ChemAxon
Monoisotopic Weight
108.057514878
ChemAxon
SMILES
OCC1=CC=CC=C1
ChemAxon
Molecular Formula
C7H8O
ChemAxon
InChI
InChI=1S/C7H8O/c8-6-7-4-2-1-3-5-7/h1-5,8H,6H2
ChemAxon
InChIKey
InChIKey=WVDDGKGOMKODPV-UHFFFAOYSA-N
ChemAxon
Polar Surface Area (PSA)
20.23
ChemAxon
Refractivity
32.87
ChemAxon
Polarizability
11.89
ChemAxon
Rotatable Bond Count
1
ChemAxon
H Bond Acceptor Count
1
ChemAxon
H Bond Donor Count
1
ChemAxon
pKa (strongest acidic)
15.02
ChemAxon
pKa (strongest basic)
-2.8
ChemAxon
Physiological Charge
0
ChemAxon
Number of Rings
1
ChemAxon
Bioavailability
1
ChemAxon
Rule of Five
true
ChemAxon
Water Solubility
33 mg/mL, clear, colorless
# http://www.chemicalbook.com/ProductChemicalPropertiesCB3852587_EN.htm
Melting Point
-15..2 °C, 258 K, 5 °F
# http://sitem.herts.ac.uk/aeru/footprint/en/Reports/953.htm.
Boiling Point
205.3 °C, 478 K, 402 °F
# http://sitem.herts.ac.uk/aeru/footprint/en/Reports/953.htm.
logP
1.1
# http://sitem.herts.ac.uk/aeru/footprint/en/Reports/953.htm.
pKa
15.4
# http://sitem.herts.ac.uk/aeru/footprint/en/Reports/953.htm.
ChEBI
17987
KEGG Drug
D00077
National Drug Code Directory
59630-780-08
Wikipedia
Benzyl_alcohol
RxList
http://www.rxlist.com/ulesfia-drug.htm
BE0002887
Cytochrome P450 2C8
Human
substrate
# Nakajima T, Wang RS, Elovaara E, Gonzalez FJ, Gelboin HV, Raunio H, Pelkonen O, Vainio H, Aoyama T: Toluene metabolism by cDNA-expressed human hepatic cytochrome P450. Biochem Pharmacol. 1997 Feb 7;53(3):271-7. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/9065730
# Kim H, Wang RS, Elovaara E, Raunio H, Pelkonen O, Aoyama T, Vainio H, Nakajima T: Cytochrome P450 isozymes responsible for the metabolism of toluene and styrene in human liver microsomes. Xenobiotica. 1997 Jul;27(7):657-65. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/9253143
unknown
Cytochrome P450 2C8
Involved in monooxygenase activity
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. In the epoxidation of arachidonic acid it generates only 14,15- and 11,12-cis-epoxyeicosatrienoic acids. It is the principal enzyme responsible for the metabolism the anti- cancer drug paclitaxel (taxol)
CYP2C8
10q23.33
Endoplasmic reticulum
None
8.62
55825.0
Human
HUGO Gene Nomenclature Committee (HGNC)
HGNC:2622
GenAtlas
CYP2C8
GenBank Gene Database
M17397
UniProtKB
P10632
UniProt Accession
CP2C8_HUMAN
CYPIIC8
EC 1.14.14.1
P450 form 1
P450 IIC2
P450 MP- 12/MP-20
S-mephenytoin 4-hydroxylase
>Cytochrome P450 2C8
MEPFVVLVLCLSFMLLFSLWRQSCRRRKLPPGPTPLPIIGNMLQIDVKDICKSFTNFSKV
YGPVFTVYFGMNPIVVFHGYEAVKEALIDNGEEFSGRGNSPISQRITKGLGIISSNGKRW
KEIRRFSLTTLRNFGMGKRSIEDRVQEEAHCLVEELRKTKASPCDPTFILGCAPCNVICS
VVFQKRFDYKDQNFLTLMKRFNENFRILNSPWIQVCNNFPLLIDCFPGTHNKVLKNVALT
RSYIREKVKEHQASLDVNNPRDFIDCFLIKMEQEKDNQKSEFNIENLVGTVADLFVAGTE
TTSTTLRYGLLLLLKHPEVTAKVQEEIDHVIGRHRSPCMQDRSHMPYTDAVVHEIQRYSD
LVPTGVPHAVTTDTKFRNYLIPKGTTIMALLTSVLHDDKEFPNPNIFDPGHFLDKNGNFK
KSDYFMPFSAGKRICAGEGLARMELFLFLTTILQNFNLKSVDDLKNLNTTAVTKGIVSLP
PSYQICFIPV
>1473 bp
ATGGAACCTTTTGTGGTCCTGGTGCTGTGTCTCTCTTTTATGCTTCTCTTTTCACTCTGG
AGACAGAGCTGTAGGAGAAGGAAGCTCCCTCCTGGCCCCACTCCTCTTCCTATTATTGGA
AATATGCTACAGATAGATGTTAAGGACATCTGCAAATCTTTCACCAATTTCTCAAAAGTC
TATGGTCCTGTGTTCACCGTGTATTTTGGCATGAATCCCATAGTGGTGTTTCATGGATAT
GAGGCAGTGAAGGAAGCCCTGATTGATAATGGAGAGGAGTTTTCTGGAAGAGGCAATTCC
CCAATATCTCAAAGAATTACTAAAGGACTTGGAATCATTTCCAGCAATGGAAAGAGATGG
AAGGAGATCCGGCGTTTCTCCCTCACAAACTTGCGGAATTTTGGGATGGGGAAGAGGAGC
ATTGAGGACCGTGTTCAAGAGGAAGCTCACTGCCTTGTGGAGGAGTTGAGAAAAACCAAG
GCTTCACCCTGTGATCCCACTTTCATCCTGGGCTGTGCTCCCTGCAATGTGATCTGCTCC
GTTGTTTTCCAGAAACGATTTGATTATAAAGATCAGAATTTTCTCACCCTGATGAAAAGA
TTCAATGAAAACTTCAGGATTCTGAACTCCCCATGGATCCAGGTCTGCAATAATTTCCCT
CTACTCATTGATTGTTTCCCAGGAACTCACAACAAAGTGCTTAAAAATGTTGCTCTTACA
CGAAGTTACATTAGGGAGAAAGTAAAAGAACACCAAGCATCACTGGATGTTAACAATCCT
CGGGACTTTATGGATTGCTTCCTGATCAAAATGGAGCAGGAAAAGGACAACCAAAAGTCA
GAATTCAATATTGAAAACTTGGTTGGCACTGTAGCTGATCTATTTGTTGCTGGAACAGAG
ACAACAAGCACCACTCTGAGATATGGACTCCTGCTCCTGCTGAAGCACCCAGAGGTCACA
GCTAAAGTCCAGGAAGAGATTGATCATGTAATTGGCAGACACAGGAGCCCCTGCATGCAG
GATAGGAGCCACATGCCTTACACTGATGCTGTAGTGCACGAGATCCAGAGATACAGTGAC
CTTGTCCCCACCGGTGTGCCCCATGCAGTGACCACTGATACTAAGTTCAGAAACTACCTC
ATCCCCAAGGGCACAACCATAATGGCATTACTGACTTCCGTGCTACATGATGACAAAGAA
TTTCCTAATCCAAATATCTTTGACCCTGGCCACTTTCTAGATAAGAATGGCAACTTTAAG
AAAAGTGACTACTTCATGCCTTTCTCAGCAGGAAAACGAATTTGTGCAGGAGAAGGACTT
GCCCGCATGGAGCTATTTTTATTTCTAACCACAATTTTACAGAACTTTAACCTGAAATCT
GTTGATGATTTAAAGAACCTCAATACTACTGCAGTTACCAAAGGGATTGTTTCTCTGCCA
CCCTCATACCAGATCTGCTTCATCCCTGTCTGA
PF00067
p450
function
catalytic activity
function
heme binding
function
monooxygenase activity
function
oxidoreductase activity
function
ion binding
function
cation binding
function
transition metal ion binding
function
iron ion binding
function
binding
function
tetrapyrrole binding
process
metabolism
process
cellular metabolism
process
generation of precursor metabolites and energy
process
electron transport
process
physiological process
unknown
unknown
BE0003543
Cytochrome P450 1A1
Human
# Furman GM, Silverman DM, Schatz RA: Inhibition of rat lung mixed-function oxidase activity following repeated low-level toluene inhalation: possible role of toluene metabolites. J Toxicol Environ Health A. 1998 Aug 21;54(8):633-45. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/9726784
# Nakajima T, Wang RS, Elovaara E, Gonzalez FJ, Gelboin HV, Raunio H, Pelkonen O, Vainio H, Aoyama T: Toluene metabolism by cDNA-expressed human hepatic cytochrome P450. Biochem Pharmacol. 1997 Feb 7;53(3):271-7. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/9065730
# Nakajima T, Wang RS, Elovaara E, Gonzalez FJ, Gelboin HV, Raunio H, Pelkonen O, Vainio H, Aoyama T: Toluene metabolism by cDNA-expressed human hepatic cytochrome P450. Biochem Pharmacol. 1997 Feb 7;53(3):271-7. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/9065730
unknown
Cytochrome P450 1A1
Secondary metabolites biosynthesis, transport and catabolism
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
CYP1A1
15q24.1
Endoplasmic reticulum membrane
None
8.47
58164.8
Human
HUGO Gene Nomenclature Committee (HGNC)
GNC:2595
GeneCards
CYP1A1
GenBank Gene Database
K03191
GenBank Protein Database
181276
UniProtKB
P04798
UniProt Accession
CP1A1_HUMAN
CYPIA1
P450 form 6
P450-C
P450-P1
>Cytochrome P450 1A1
MLFPISMSATEFLLASVIFCLVFWVIRASRPQVPKGLKNPPGPWGWPLIGHMLTLGKNPH
LALSRMSQQYGDVLQIRIGSTPVVVLSGLDTIRQALVRQGDDFKGRPDLYTFTLISNGQS
MSFSPDSGPVWAARRRLAQNGLKSFSIASDPASSTSCYLEEHVSKEAEVLISTLQELMAG
PGHFNPYRYVVVSVTNVICAICFGRRYDHNHQELLSLVNLNNNFGEVVGSGNPADFIPIL
RYLPNPSLNAFKDLNEKFYSFMQKMVKEHYKTFEKGHIRDITDSLIEHCQEKQLDENANV
QLSDEKIINIVLDLFGAGFDTVTTAISWSLMYLVMNPRVQRKIQEELDTVIGRSRRPRLS
DRSHLPYMEAFILETFRHSSFVPFTIPHSTTRDTSLKGFYIPKGRCVFVNQWQINHDQKL
WVNPSEFLPERFLTPDGAIDKVLSEKVIIFGMGKRKCIGETIARWEVFLFLAILLQRVEF
SVPLGVKVDMTPIYGLTMKHACCEHFQMQLRS
>1539 bp
TCCCTACACTGATCATGCTTTTCCCAATCTCCATGTCGGCCACGGAGTTTCTTCTGGCCT
CTGTCATCTTCTGTCTGGTATTCTGGGTAATGAGGGCCTCAAGACCTCAGGTCCCCAAAG
GCCTGAAGAATCCACCAGGGCCATGGGGCTGGCCTCTGATTGGGCACATGCTGACCCTGG
GAAAGAACCCGCACCTGGCACTGTCAAGGATGAGCCAGCAGTATGGGGACGTGCTGCAGA
TCCGAATTGGCTCCACACCCGTGGTGGTGCTGAGCGGCCTGGACACCATCCGGCAGGCCC
TGGTGCGGCAGGGCGATGATTTCAAGGGCCGGCCCGACCTCTACACCTTCACCCTCATCA
GTAATGGTCAGAGCATGTCCTTCAGCCCAGACTCTGGACCAGTGTGGGCTGCCCGCCGGC
GCCTGGCCCAGAATGGCCTGAAAAGTTTCTCCATTGCCTCTGACCCAGCCTCCTCAACCT
CCTGCTACCTGGAAGAGCATGTGAGCAAGGAGGCTGAGGTCCTGATAAGCACGTTGCAGG
AGCTGATGGCAGGGCCTGGGCACTTTAACCCCTACAGGTATGTGGTGGTATCAGTGACCA
ATGTCATCTGTGCCATTTGCTTTGGCCGGCGCTATGACCACAACCACCAAGAACTGCTTA
GCCTAGTCAACCTGAATAATAATTTCGGGGAGGTGGTTGGCTCTGGAAACCCAGCTGAGT
TCATCCCTATTCTTCGCTACCTACCCAACCCTTCCCTGAATGCCTTCAAGGACCTGAATG
AGAAGTTCTACAGCTTCATGCAGAAGATGGTCAAGGAGCACTACAAAACCTTTGAGAAGG
GCCACATCCGGGACATCACAGACAGCCTGATTGAGCACTGTCAGGAGAAGCAGCTGGATG
AGAACGCCAATGTCCAGCTGTCAGATGAGAAGATCATTAACATCGTCTTGGACCTCTTTG
GAGCTGGGTTTGACACAGTCACAACTGCTATCTCCTGGAGCCTCATGTATTTGGTGATGA
ACCCCAGGGTACAGAGAAAGATCCAAGAGGAGCTAGACACAGTGATTGGCAGGTCACGGC
GGCCCCGGCTCTCTGACAGATCCCATCTGCCCTATATGGAGGCCTTCATCCTGGAGACCT
TCCGACACTCTTCCTTCGTCCCCTTCACCATCCCCCACAGCACAACAAGAGACACAAGTT
TGAAAGGCTTTTACATCCCCAAGGGGCGTTGTGTCTTTGTAAACCAGTGGCAGATCAACC
ATGACCAGAAGCTATGGGTCAACCCATCTGAGTTCCTACCTGAACGGTTTCTCACCCCTG
ATGGTGCTATCGACAAGGTGTTAAGTGAGAAGGTGATTATCTTTGGCATGGGCAAGCGGA
AGTGTATCGGTGAGACCGTTGCCCGCTGGGAGGTCTTTCTCTTCCTGGCTATCCTGCTGC
AACGGGTGGAATTCAGCGTGCCACTGGGCGTGAAGGTGGACATGACCCCCATCTATGGGC
TAACCATGAAGCATGCCTGCTGTGAGCACTTCCAAATGC
PF00067
p450
function
oxidoreductase activity
function
ion binding
function
cation binding
function
transition metal ion binding
function
iron ion binding
function
binding
function
tetrapyrrole binding
function
catalytic activity
function
heme binding
function
monooxygenase activity
function
oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen
process
generation of precursor metabolites and energy
process
electron transport
process
physiological process
process
metabolism
process
cellular metabolism
unknown
unknown
BE0000133
Aldehyde dehydrogenase, mitochondrial
Human
substrate
# Kawamoto T, Koga M, Murata K, Matsuda S, Kodama Y: Effects of ALDH2, CYP1A1, and CYP2E1 genetic polymorphisms and smoking and drinking habits on toluene metabolism in humans. Toxicol Appl Pharmacol. 1995 Aug;133(2):295-304. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/7645026
unknown
Aldehyde dehydrogenase, mitochondrial
Energy production and conversion
ALDH2
12q24.2
Mitochondrion; mitochondrial matrix
None
7.05
56382.0
Human
HUGO Gene Nomenclature Committee (HGNC)
HGNC:404
GenAtlas
ALDH2
GeneCards
ALDH2
GenBank Gene Database
X05409
GenBank Protein Database
28606
UniProtKB
P05091
UniProt Accession
ALDH2_HUMAN
Aldehyde dehydrogenase, mitochondrial precursor
ALDH class 2
ALDH-E2
ALDHI
EC 1.2.1.3
>Aldehyde dehydrogenase, mitochondrial precursor
MLRAAARFGPRLGRRLLSAAATQAVPAPNQQPEVFCNQIFINNEWHDAVSRKTFPTVNPS
TGEVICQVAEGDKEDVDKAVKAARAAFQLGSPWRRMDASHRGRLLNRLADLIERDRTYLA
ALETLDNGKPYVISYLVDLDMVLKCLRYYAGWADKYHGKTIPIDGDFFSYTRHEPVGVCG
QIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLTALYVANLIKEAGFPPGVVNIVPG
FGPTAGAAIASHEDVDKVAFTGSTEIGRVIQVAAGSSNLKRVTLELGGKSPNIIMSDADM
DWAVEQAHFALFFNQGQCCCAGSRTFVQEDIYDEFVERSVARAKSRVVGNPFDSKTEQGP
QVDETQFKKILGYINTGKQEGAKLLCGGGIAADRGYFIQPTVFGDVQDGMTIAKEEIFGP
VMQILKFKTIEEVVGRANNSTYGLAAAVFTKDLDKANYLSQALQAGTVWVNCYDVFGAQS
PFGGYKMSGSGRELGEYGLQAYTEVKTVTVKVPQKNS
>1551 bp
ATGTTGCGCGCTGCCGCCGCTCGGGCCCCGCCTGGCCGCCGCCTCTTGTCAGCCGCCGCC
ACCCAGGCCGTGCCTGCCCCCAACCAGCAGCCCGAGGTCTTCTGCAACCAGATTTTCATA
AACAATGAATGGCACGATGCCGTCAGCAGGAAAACATTCCCCACCGTCAATCCGTCCACT
GGAGAGGTCATCTGTCAGGTAGCTGAAGGGGACAAGGAAGATGTGGACAAGGCACGTGAA
GGCCGCCCGGGCGCCTTCCAGCTGGGCTCACCTTGGCGCCGCATGGACGCATCACACAGC
GGCCGGCTGCTGAACCGCCTGGCCGATCTGATCGAGCGGGACCGGACCTACCTGGCGGCC
TTGGAGACCCTGGACAATGGCAAGCCCTATGTCATCTCCTACCTGGTGGATTTGGACATG
GTCCTCAAATGTCTCCGGTATTATGCCGGCTGGGCTGATAAGTACCACGGGAAAACCATC
CCCATTGACGGAGACTTCTTCAGCTACACACGCCATGAACCTGTGGGGGTGTGCGGGCAG
ATCATTCCGTGGAATTTCCCGCTCCTGATGCAAGCATGGAAGCTGGGCCCAGCCTTGGCA
ACTGGAAACGTGGTTGTGATGAAGGTAGCTGAGCAGACACCCCTCACCGCCCTCTATGTG
GCCAACCTGATCAAGGAGGCTGGCTTTCCCCCTGGTGTGGTCAACATTGTGCCTGGATTT
GGCCCCACGGCTGGGGCCGCCATTGCCTCCCATGAGGATGTGGACAAAGTGGCATTCACA
GGCTCCACTGAGATTGGCCGCGTAATCCAGGTTGCTGCTGGGAGCAGCAACCTCAAGAGA
GTGACCTTGGAGCTGGGGGGGAAGAGCCCCAACATCATCATGTCAGATGCCGATATGGAT
TGGGCCGTGGAACAGGCCCACTTCGCCCTGTTCTTCAACCAGGGCCAGTGCTGCTGTGCC
GGCTCCCGGACCTTCGTGCAGGAGGACATCTATGATGAGTTTGTGGTGCGGAGCGTTGCC
CGGGCCAAGTCTCGGGTGGTCGGGAACCCCTTTGATAGCAAGACCGAGCAGGGGCCGCAG
GTGGATGAAACTCAGTTTAAGAAGATCCTCGGCTACATCAACACGGGGAAGCAAGAGGGG
GCGAAGCTGCTGTGTGGTGGGGGCATTGCTGCTGACCGTGGTTACTTCATCCAGCCCACT
GTGTTTGGAGATGTGCAGGATGGCATGACCATCGCCAAGGAGGAGATCTTCGGGCCAGTG
ATGCAGATCCTGAAGTTCAAGACCATAGAGGAGGTTGTTGGGAGAGCCAACAATTCCACG
TACGGGCTGGCCGCAGCTGTCTTCACAAAGGATTTGGACAAGGCCAATTACCTGTCCCAG
GCCCTCCAGGCGGGCACTGTGTGGGTCAACTGCTATGATGTGTTTGGAGCCCAGTCACCC
TTTGGTGGCTACAAGATGTCGGGGAGTGGCCGGGAGTTGGGCGAGTACGGGCTGCAGGCA
TACACTGAAGTGAAAACTGTCACAGTCAAAGTGCCTCAGAAGAACTCATAA
PF00171
Aldedh
function
catalytic activity
function
oxidoreductase activity
process
physiological process
process
metabolism
unknown
unknown
BE0003549
Cytochrome P450 2B6
Human
substrate
# Nakajima T, Wang RS, Elovaara E, Gonzalez FJ, Gelboin HV, Raunio H, Pelkonen O, Vainio H, Aoyama T: Toluene metabolism by cDNA-expressed human hepatic cytochrome P450. Biochem Pharmacol. 1997 Feb 7;53(3):271-7. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/9065730
unknown
Cytochrome P450 2B6
Secondary metabolites biosynthesis, transport and catabolism
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
CYP2B6
19q13.2
Endoplasmic reticulum membrane
None
8.44
56277.8
Human
HUGO Gene Nomenclature Committee (HGNC)
GNC:2615
GeneCards
CYP2B6
GenBank Gene Database
M29874
GenBank Protein Database
181296
UniProtKB
P20813
UniProt Accession
CP2B6_HUMAN
CYPIIB6
P450 IIB1
>Cytochrome P450 2B6
MELSVLLFLALLTGLLLLLVQRHPNTHDRLPPGPRPLPLLGNLLQMDRRGLLKSFLRFRE
KYGDVFTVHLGPRPVVMLCGVEAIREALVDKAEAFSGRGKIAMVDPFFRGYGVIFANGNR
WKVLRRFSVTTMRDFGMGKRSVEERIQEEAQCLIEELRKSKGALMDPTFLFQSITANIIC
SIVFGKRFHYQDQEFLKMLNLFYQTFSLISSVFGQLFELFSGFLKYFPGAHRQVYKNLQE
INAYIGHSVEKHRETLDPSAPKDLIDTYLLHMEKEKSNAHSEFSHQNLNLNTLSLFFAGT
ETTSTTLRYGFLLMLKYPHVAERVYREIEQVIGPHRPPELHDRAKMPYTEAVIYEIQRFS
DLLPMGVPHIVTQHTSFRGYIIPKDTEVFLILSTALHDPHYFEKPDAFNPDHFLDANGAL
KKTEAFIPFSLGKRICLGEGIARAELFLFFTTILQNFSMASPVAPEDIDLTPQECGVGKI
PPTYQIRFLPR
>1476 bp
ATGGAACTCAGCGTCCTCCTCTTCCTTGCACTCCTCACAGGACTCTTGCTACTCCTGGTT
CAGCGCCACCCTAACACCCATGACCGCCTCCCACCAGGGCCCCGCCCTCTGCCCCTTTTG
GGAAACCTTCTGCAGATGGATAGAAGAGGCCTACTCAAATCCTTTCTGAGGTTCCGAGAG
AAATATGGGGACGTCTTCACGGTACACCTGGGACCGAGGCCCGTGGTCATGCTGTGTGGA
GTAGAGGCCATACGGGAGGCCCTTGTGGACAAGGCTGAGGCCTTCTCTGGCCGGGGAAAA
ATCGCCATGGTCGACCCATTCTTCCGGGGATATGGTGTGATCTTTGCCAATGGAAACCGC
TGGAAGGTGCTTCGGCGATTCTCTGTGACCACTATGAGGGACTTCGGGATGGGAAAGCGG
AGTGTGGAGGAGCGGATTCAGGAGGAGGCTCAGTGTCTGATAGAGGAGCTTCGGAAATCC
AAGGGGGCCCTCATGGACCCCACCTTCCTCTTCCAGTCCATTACCGCCAACATCATCTGC
TCCATCGTCTTTGGAAAACGATTCCACTACCAAGATCAAGAGTTCCTGAAGATGCTGAAC
TTGTTCTACCAGACTTTTTCACTCATCAGCTCTGTATTCGGCCAGCTGTTTGAGCTCTTC
TCTGGCTTCTTGAAATACTTTCCTGGGGCACACAGGCAAGTTTACAAAAACCTGCAGGAA
ATCAATGCTTACATTGGCCACAGTGTGGAGAAGCACCGTGAAACCCTGGACCCCAGCGCC
CCCAAGGACCTCATCGACACCTACCTGCTCCACATGGAAAAAGAGAAATCCAACGCACAC
AGTGAATTCAGCCACCAGAACCTCAACCTCAACACGCTCTCGCTCTTCTTTGCTGGCACT
GAGACCACCAGCACCACTCTCCGCTACGGCTTCCTGCTCATGCTCAAATACCCTCATGTT
GCAGAGAGAGTCTACAGGGAGATTGAACAGGTGATTGGCCCACATCGCCCTCCAGAGCTT
CATGACCGAGCCAAAATGCCATACACAGAGGCAGTCATCTATGAGATTCAGAGATTTTCC
GACCTTCTCCCCATGGGTGTGCCCCACATTGTCACCCAACACACCAGCTTCCGAGGGTAC
ATCATCCCCAAGGACACAGAAGTATTTCTCATCCTGAGCACTGCTCTCCATGACCCACAC
TACTTTGAAAAACCAGACGCCTTCAATCCTGACCACTTTCTGGATGCCAATGGGGCACTG
AAAAAGACTGAAGCTTTTATCCCCTTCTCCTTAGGGAAGCGGATTTGTCTTGGTGAAGGC
ATCGCCCGTGCGGAATTGTTCCTCTTCTTCACCACCATCCTCCAGAACTTCTCCATGGCC
AGCCCCGTGGCCCCAGAAGACATCGATCTGACACCCCAGGAGTGTGGTGTGGGCAAAATA
CCCCCAACATACCAGATCCGCTTCCTGCCCCGCTGA
PF00067
p450
function
oxidoreductase activity
function
ion binding
function
cation binding
function
transition metal ion binding
function
iron ion binding
function
binding
function
tetrapyrrole binding
function
catalytic activity
function
heme binding
function
monooxygenase activity
function
oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen
process
generation of precursor metabolites and energy
process
electron transport
process
physiological process
process
metabolism
process
cellular metabolism
unknown
unknown
BE0002433
Cytochrome P450 1A2
Human
substrate
# Nakajima T, Wang RS, Elovaara E, Gonzalez FJ, Gelboin HV, Raunio H, Pelkonen O, Vainio H, Aoyama T: Toluene metabolism by cDNA-expressed human hepatic cytochrome P450. Biochem Pharmacol. 1997 Feb 7;53(3):271-7. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/9065730
# Kim H, Wang RS, Elovaara E, Raunio H, Pelkonen O, Aoyama T, Vainio H, Nakajima T: Cytochrome P450 isozymes responsible for the metabolism of toluene and styrene in human liver microsomes. Xenobiotica. 1997 Jul;27(7):657-65. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/9253143
unknown
Cytochrome P450 1A2
Involved in monooxygenase activity
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
CYP1A2
15q24
Endoplasmic reticulum
None
9.43
58295.0
Human
HUGO Gene Nomenclature Committee (HGNC)
HGNC:2596
GenAtlas
CYP1A2
GenBank Gene Database
Z00036
UniProtKB
P05177
UniProt Accession
CP1A2_HUMAN
CYPIA2
EC 1.14.14.1
P(3)450
P450 4
P450-P3
>Cytochrome P450 1A2
MALSQSVPFSATELLLASAIFCLVFWVLKGLRPRVPKGLKSPPEPWGWPLLGHVLTLGKN
PHLALSRMSQRYGDVLQIRIGSTPVLVLSRLDTIRQALVRQGDDFKGRPDLYTSTLITDG
QSLTFSTDSGPVWAARRRLAQNALNTFSIASDPASSSSCYLEEHVSKEAKALISRLQELM
AGPGHFDPYNQVVVSVANVIGAMCFGQHFPESSDEMLSLVKNTHEFVETASSGNPLDFFP
ILRYLPNPALQRFKAFNQRFLWFLQKTVQEHYQDFDKNSVRDITGALFKHSKKGPRASGN
LIPQEKIVNLVNDIFGAGFDTVTTAISWSLMYLVTKPEIQRKIQKELDTVIGRERRPRLS
DRPQLPYLEAFILETFRHSSFLPFTIPHSTTRDTTLNGFYIPKKCCVFVNQWQVNHDPEL
WEDPSEFRPERFLTADGTAINKPLSEKMMLFGMGKRRCIGEVLAKWEIFLFLAILLQQLE
FSVPPGVKVDLTPIYGLTMKHARCEHVQARRFSIN
>1548 bp
ATGGCATTGTCCCAGTCTGTTCCCTTCTCGGCCACAGAGCTTCTCCTGGCCTCTGCCATC
TTCTGCCTGGTATTCTGGGTGCTCAAGGGTTTGAGGCCTCGGGTCCCCAAAGGCCTGAAA
AGTCCACCAGAGCCATGGGGCTGGCCCTTGCTCGGGCATGTGCTGACCCTGGGGAAGAAC
CCGCACCTGGCACTGTCAAGGATGAGCCAGCGCTACGGGGACGTCCTGCAGATCCGCATT
GGCTCCACGCCCGTGCTGGTGCTGAGCCGCCTGGACACCATCCGGCAGGCCCTGGTGCGG
CAGGGCGACGATTTCAAGGGCCGGCCTGACCTCTACACCTCCACCCTCATCACTGATGGC
CAGAGCTTGACCTTCAGCACAGACTCTGGACCGGTGTGGGCTGCCCGCCGGCGCCTGGCC
CAGAATGCCCTCAACACCTTCTCCATCGCCTCTGACCCAGCTTCCTCATCCTCCTGCTAC
CTGGAGGAGCATGTGAGCAAGGAGGCTAAGGCCCTGATCAGCAGGTTGCAGGAGCTGATG
GCAGGGCCTGGGCACTTCGACCCTTACAATCAGGTGGTGGTGTCAGTGGCCAACGTCATT
GGTGCCATGTGCTTCGGACAGCACTTCCCTGAGAGTAGCGATGAGATGCTCAGCCTCGTG
AAGAACACTCATGAGTTCGTGGAGACTGCCTCCTCCGGGAACCCCCTGGACTTCTTCCCC
ATCCTTCGCTACCTGCCTAACCCTGCCCTGCAGAGGTTCAAGGCCTTCAACCAGAGGTTC
CTGTGGTTCCTGCAGAAAACAGTCCAGGAGCACTATCAGGACTTTGACAAGAACAGTGTC
CGGGACATCACGGGTGCCCTGTTCAAGCACAGCAAGAAGGGGCCTAGAGCCAGCGGCAAC
CTCATCCCACAGGAGAAGATTGTCAACCTTGTCAATGACATCTTTGGAGCAGGATTTGAC
ACAGTCACCACAGCCATCTCCTGGAGCCTCATGTACCTTGTGACCAAGCCTGAGATACAG
AGGAAGATCCAGAAGGAGCTGGACACTGTGATTGGCAGGGAGCGGCGGCCCCGGCTCTCT
GACAGACCCCAGCTGCCCTACTTGGAGGCCTTCATCCTGGAGACCTTCCGACACTCCTCC
TTCTTGCCCTTCACCATCCCCCACAGCACAACAAGGGACACAACGCTGAATGGCTTCTAC
ATCCCCAAGAAATGCTGTGTCTTCGTAAACCAGTGGCAGGTCAACCATGACCCAGAGCTG
TGGGAGGACCCCTCTGAGTTCCGGCCTGAGCGGTTCCTCACCGCCGATGGCACTGCCATT
AACAAGCCCTTGAGTGAGAAGATGATGCTGTTTGGCATGGGCAAGCGCCGGTGTATCGGG
GAAGTCCTGGCCAAGTGGGAGATCTTCCTCTTCCTGGCCATCCTGCTACAGCAACTGGAG
TTCAGCGTGCCGCCGGGCGTGAAAGTCGACCTGACCCCCATCTACGGGCTGACCATGAAG
CACGCCCGCTGTGAACATGTCCAGGCGCGGCGCTTCTCCATCAATTGA
PF00067
p450
function
catalytic activity
function
heme binding
function
monooxygenase activity
function
oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen
function
oxidoreductase activity
function
ion binding
function
cation binding
function
transition metal ion binding
function
iron ion binding
function
binding
function
tetrapyrrole binding
process
metabolism
process
cellular metabolism
process
generation of precursor metabolites and energy
process
electron transport
process
physiological process
unknown
unknown
BE0003533
Cytochrome P450 2E1
Human
substrate
# Nakajima T, Wang RS, Elovaara E, Gonzalez FJ, Gelboin HV, Raunio H, Pelkonen O, Vainio H, Aoyama T: Toluene metabolism by cDNA-expressed human hepatic cytochrome P450. Biochem Pharmacol. 1997 Feb 7;53(3):271-7. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/9065730
# Lipscomb JC, Barton HA, Tornero-Velez R, Evans MV, Alcasey S, Snawder JE, Laskey J: The metabolic rate constants and specific activity of human and rat hepatic cytochrome P-450 2E1 toward toluene and chloroform. J Toxicol Environ Health A. 2004 Apr 9;67(7):537-53. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/15129551
# Kim H, Wang RS, Elovaara E, Raunio H, Pelkonen O, Aoyama T, Vainio H, Nakajima T: Cytochrome P450 isozymes responsible for the metabolism of toluene and styrene in human liver microsomes. Xenobiotica. 1997 Jul;27(7):657-65. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/9253143
# Wang RS, Nakajima T, Park SS, Gelboin HV, Murayama N: Monoclonal antibody-directed assessment of toluene induction of rat hepatic cytochrome P450 isozymes. Biochem Pharmacol. 1993 Aug 3;46(3):413-9. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/8347164
unknown
Cytochrome P450 2E1
Secondary metabolites biosynthesis, transport and catabolism
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
CYP2E1
10q24.3-qter
Endoplasmic reticulum membrane
None
8.22
56848.4
Human
HUGO Gene Nomenclature Committee (HGNC)
GNC:2631
GeneCards
CYP2E1
GenBank Gene Database
J02625
GenBank Protein Database
181360
UniProtKB
P05181
UniProt Accession
CP2E1_HUMAN
4-nitrophenol 2-hydroxylase
CYPIIE1
P450-J
>Cytochrome P450 2E1
MSALGVTVALLVWAAFLLLVSMWRQVHSSWNLPPGPFPLPIIGNLFQLELKNIPKSFTRL
AQRFGPVFTLYVGSQRMVVMHGYKAVKEALLDYKDEFSGRGDLPAFHAHRDRGIIFNNGP
TWKDIRRFSLTTLRNYGMGKQGNESRIQREAHFLLEALRKTQGQPFDPTFLIGCAPCNVI
ADILFRKHFDYNDEKFLRLMYLFNENFHLLSTPWLQLYNNFPSFLHYLPGSHRKVIKNVA
EVKEYVSERVKEHHQSLDPNCPRDLTDCLLVEMEKEKHSAERLYTMDGITVTVADLFFAG
TETTSTTLRYGLLILMKYPEIEEKLHEEIDRVIGPSRIPAIKDRQEMPYMDAVVHEIQRF
ITLVPSNLPHEATRDTIFRGYLIPKGTVVVPTLDSVLYDNQEFPDPEKFKPEHFLNENGK
FKYSDYFKPFSTGKRVCAGEGLARMELFLLLCAILQHFNLKPLVDPKDIDLSPIHIGFGC
IPPRYKLCVIPRS
>1482 bp
CCCAGCGCACCATGTCTGCCCTCGGAGTGACCGTGGCCCTGCTGGTGTGGGCGGCCTTCC
TCCTGCTGGTGTCCATGTGGAGGCAGGTGCACAGCAGCTGGAATCTGCCCCCAGGTCCTT
TCCCGCTTCCCATCATCGGGAACCTCTTCCAGTTGGAATTGAAGAATATTCCCAAGTCCT
TCACCCGGTTGGCCCAGCGCTTCGGGCCGGTGTTCACGCTGTACGTGGGCTCGCAGCGCA
TGGTGGTGATGCACGGCTACAAGGCGGTGAAGGAAGCGCTGCTGGACTACAAGGACGAGT
TCTCGGGCAGAGGCGACCTCCCCGCGTTCCATGCGCACAGGGACAGGGGAATCATTTTTA
ATAATGGACCTACCTGGAAGGACATCCGGCGGTTTTCCCTGACCACCCTCCGGAACTATG
GGATGGGGAAACAGGGCAATGAGAGCCGGATCCAGAGGGAGGCCCACTTCCTGCTGGAAG
CACTCAGGAAGACCCAAGGCCAGCCTTTCGACCCCACCTTCCTCATCGGCTGCGCGCCCT
GCAACGTCATAGCCGACATCCTCTTCCGCAAGCATTTTGACTACAATGATGAGAAGTTTC
TAAGGCTGATGTATTTGTTTAATGAGAACTTCCACCTACTCAGCACTCCCTGGCTCCAGC
TTTACAATAATTTTCCCAGCTTTCTACACTACTTGCCTGGAAGCCACAGAAAAGTCATAA
AAAATGTGGCTGAAGTAAAAGAGTATGTGTCTGAAAGGGTGAAGGAGCACCATCAATCTC
TGGACCCCAACTGTCCCCGGGACCTCACCGACTGCCTGCTCGTGGAAATGGAGAAGGAAA
AGCACAGTGCAGAGCGCTTGTACACAATGGACGGTATCACCGTGACTGTGGCCGACCTGT
TCTTTGCGGGGACAGAGACCACCAGCACAACTCTGAGATATGGGCTCCTGATTCTCATGA
AATACCCTGAGATCGAAGAGAAGCTCCATGAAGAAATTGACAGGGTGATTGGGCCAAGCC
GAATCCCTGCCATCAAGGATAGGCAAGAGATGCCCTACATGGATGCTGTGGTGCATGAGA
TTCAGCGGTTCATCACCCTCGTGCCCTCCAACCTGCCCCATGAAGCAACCCGAGACACCA
TTTTCAGAGGATACCTCATCCCCAAGGGCACAGTCGTAGTGCCAACTCTGGACTCTGTTT
TGTATGACAACCAAGAATTTCCTGATCCAGAAAAGTTTAAGCCAGAACACTTCCTGAATG
AAAATGGAAAGTTCAAGTACAGTGACTATTTCAAGCCATTTTCCACAGGAAAACGAGTGT
GTGCTGGAGAAGGCCTGGCTCGCATGGAGTTGTTTCTTTTGTTGTGTGCCATTTTGCAGC
ATTTTAATTTGAAGCCTCTCGTTGACCCAAAGGATATCGACCTCAGCCCTATACATATTG
GGTTTGGCTGTATCCCACCACGTTACAAACTCTGTGTCATTC
PF00067
p450
function
ion binding
function
cation binding
function
transition metal ion binding
function
iron ion binding
function
binding
function
tetrapyrrole binding
function
catalytic activity
function
heme binding
function
monooxygenase activity
function
oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen
function
oxidoreductase activity
process
generation of precursor metabolites and energy
process
electron transport
process
physiological process
process
metabolism
process
cellular metabolism
unknown
unknown
BE0002363
Cytochrome P450 2D6
Human
substrate
# Obach RS: Mechanism of cytochrome P4503A4- and 2D6-catalyzed dehydrogenation of ezlopitant as probed with isotope effects using five deuterated analogs. Drug Metab Dispos. 2001 Dec;29(12):1599-607. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/11717179
unknown
Cytochrome P450 2D6
Secondary metabolites biosynthesis, transport and catabolism
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
CYP2D6
22q13.1
Endoplasmic reticulum
None
7.26
55770.0
Human
HUGO Gene Nomenclature Committee (HGNC)
HGNC:2625
GenAtlas
CYP2D6
GeneCards
CYP2D6
GenBank Gene Database
M20403
GenBank Protein Database
181350
UniProtKB
P10635
UniProt Accession
CP2D6_HUMAN
CYPIID6
Debrisoquine 4-hydroxylase
EC 1.14.14.1
P450-DB1
>Cytochrome P450 2D6
MGLEALVPLAVIVAIFLLLVDLMHRRQRWAARYPPGPLPLPGLGNLLHVDFQNTPYCFDQ
LRRRFGDVFSLQLAWTPVVVLNGLAAVREALVTHGEDTADRPPVPITQILGFGPRSQGVF
LARYGPAWREQRRFSVSTLRNLGLGKKSLEQWVTEEAACLCAAFANHSGRPFRPNGLLDK
AVSNVIASLTCGRRFEYDDPRFLRLLDLAQEGLKEESGFLREVLNAVPVLLHIPALAGKV
LRFQKAFLTQLDELLTEHRMTWDPAQPPRDLTEAFLAEMEKAKGNPESSFNDENLRIVVA
DLFSAGMVTTSTTLAWGLLLMILHPDVQRRVQQEIDDVIGQVRRPEMGDQAHMPYTTAVI
HEVQRFGDIVPLGVTHMTSRDIEVQGFRIPKGTTLITNLSSVLKDEAVWEKPFRFHPEHF
LDAQGHFVKPEAFLPFSAGRRACLGEPLARMELFLFFTSLLQHFSFSVPTGQPRPSHHGV
FAFLVSPSPYELCAVPR
>1494 bp
ATGGGGCTAGAAGCACTGGTGCCCCTGGCCGTGATAGTGGCCATCTTCCTGCTCCTGGTG
GACCTGATGCACCGGCGCCAACGCTGGGCTGCACGCTACCCACCAGGCCCCCTGCCACTG
CCCGGGCTGGGCAACCTGCTGCATGTGGACTTCCAGAACACACCATACTGCTTCGACCAG
TTGCGGCGCCGCTTCGGGGACGTGTTCAGCCTGCAGCTGGCCTGGACGCCGGTGGTCGTG
CTCAATGGGCTGGCGGCCGTGCGCGAGGCGCTGGTGACCCACGGCGAGGACACCGCCGAC
CGCCCGCCTGTGCCCATCACCCAGATCCTGGGTTTCGGGCCGCGTTCCCAAGGGGTGTTC
CTGGCGCGCTATGGGCCCGCGTGGCGCGAGCAGAGGCGCTTCTCCGTGTCCACCTTGCGC
AACTTGGGCCTGGGCAAGAAGTCGCTGGAGCAGTGGGTGACCGAGGAGGCCGCCTGCCTT
TGTGCCGCCTTCGCCAACCACTCCGGACGCCCCTTTCGCCCCAACGGTCTCTTGGACAAA
GCCGTGAGCAACGTGATCGCCTCCCTCACCTGCGGGCGCCGCTTCGAGTACGACGACCCT
CGCTTCCTCAGGCTGCTGGACCTAGCTCAGGAGGGACTGAAGGAGGAGTCGGGCTTTCTG
CGCGAGGTGCTGAATGCTGTCCCCGTCCTCCTGCATATCCCAGCGCTGGCTGGCAAGGTC
CTACGCTTCCAAAAGGCTTTCCTGACCCAGCTGGATGAGCTGCTAACTGAGCACAGGATG
ACCTGGGACCCAGCCCAGCCCCCCCGAGACCTGACTGAGGCCTTCCTGGCAGAGATGGAG
AAGGCCAAGGGGAACCCTGAGAGCAGCTTCAATGATGAGAACCTGCGCATAGTGGTGGCT
GACCTGTTCTCTGCCGGGATGGTGACCACCTCGACCACGCTGGCCTGGGGCCTCCTGCTC
ATGATCCTACATCCGGATGTGCAGCGCCGTGTCCAACAGGAGATCGACGACGTGATAGGG
CAGGTGCGGCGACCAGAGATGGGTGACCAGGCTCACATGCCCTACACCACTGCCGTGATT
CATGAGGTGCAGCGCTTTGGGGACATCGTCCCCCTGGGTATGACCCATATGACATCCCGT
GACATCGAAGTACAGGGCTTCCGCATCCCTAAGGGAACGACACTCATCACCAACCTGTCA
TCGGTGCTGAAGGATGAGGCCGTCTGGGAGAAGCCCTTCCGCTTCCACCCCGAACACTTC
CTGGATGCCCAGGGCCACTTTGTGAAGCCGGAGGCCTTCCTGCCTTTCTCAGCAGGCCGC
CGTGCATGCCTCGGGGAGCCCCTGGCCCGCATGGAGCTCTTCCTCTTCTTCACCTCCCTG
CTGCAGCACTTCAGCTTCTCGGTGCCCACTGGACAGCCCCGGCCCAGCCACCATGGTGTC
TTTGCTTTCCTGGTGAGCCCATCCCCCTATGAGCTTTGTGCTGTGCCCCGCTAG
PF00067
p450
function
ion binding
function
cation binding
function
transition metal ion binding
function
iron ion binding
function
binding
function
tetrapyrrole binding
function
catalytic activity
function
heme binding
function
monooxygenase activity
function
oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen
function
oxidoreductase activity
process
generation of precursor metabolites and energy
process
electron transport
process
physiological process
process
metabolism
process
cellular metabolism
unknown
unknown
BE0002638
Cytochrome P450 3A4
Human
substrate
# Obach RS: Mechanism of cytochrome P4503A4- and 2D6-catalyzed dehydrogenation of ezlopitant as probed with isotope effects using five deuterated analogs. Drug Metab Dispos. 2001 Dec;29(12):1599-607. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/11717179
# Obach RS: Mechanism of cytochrome P4503A4- and 2D6-catalyzed dehydrogenation of ezlopitant as probed with isotope effects using five deuterated analogs. Drug Metab Dispos. 2001 Dec;29(12):1599-607. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/11717179
# Obach RS: Mechanism of cytochrome P4503A4- and 2D6-catalyzed dehydrogenation of ezlopitant as probed with isotope effects using five deuterated analogs. Drug Metab Dispos. 2001 Dec;29(12):1599-607. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/11717179
unknown
Cytochrome P450 3A4
Involved in monooxygenase activity
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. The enzyme also hydroxylates etoposide
CYP3A4
7q21.1
Endoplasmic reticulum
2-22
8.25
57344.0
Human
HUGO Gene Nomenclature Committee (HGNC)
HGNC:2637
GenAtlas
CYP3A4
GenBank Gene Database
M18907
UniProtKB
P08684
UniProt Accession
CP3A4_HUMAN
CYPIIIA4
EC 1.14.13.67
EC 1.14.13.97
NF-25
Nifedipine oxidase
P450-PCN1
Quinine 3-monooxygenase
Taurochenodeoxycholate 6-alpha- hydroxylase
>Cytochrome P450 3A4
MALIPDLAMETWLLLAVSLVLLYLYGTHSHGLFKKLGIPGPTPLPFLGNILSYHKGFCMF
DMECHKKYGKVWGFYDGQQPVLAITDPDMIKTVLVKECYSVFTNRRPFGPVGFMKSAISI
AEDEEWKRLRSLLSPTFTSGKLKEMVPIIAQYGDVLVRNLRREAETGKPVTLKDVFGAYS
MDVITSTSFGVNIDSLNNPQDPFVENTKKLLRFDFLDPFFLSITVFPFLIPILEVLNICV
FPREVTNFLRKSVKRMKESRLEDTQKHRVDFLQLMIDSQNSKETESHKALSDLELVAQSI
IFIFAGYETTSSVLSFIMYELATHPDVQQKLQEEIDAVLPNKAPPTYDTVLQMEYLDMVV
NETLRLFPIAMRLERVCKKDVEINGMFIPKGVVVMIPSYALHRDPKYWTEPEKFLPERFS
KKNKDNIDPYIYTPFGSGPRNCIGMRFALMNMKLALIRVLQNFSFKPCKETQIPLKLSLG
GLLQPEKPVVLKVESRDGTVSGA
>1512 bp
ATGGCTCTCATCCCAGACTTGGCCATGGAAACCTGGCTTCTCCTGGCTGTCAGCCTGGTG
CTCCTCTATCTATATGGAACCCATTCACATGGACTTTTTAAGAAGCTTGGAATTCCAGGG
CCCACACCTCTGCCTTTTTTGGGAAATATTTTGTCCTACCATAAGGGCTTTTGTATGTTT
GACATGGAATGTCATAAAAAGTATGGAAAAGTGTGGGGCTTTTATGATGGTCAACAGCCT
GTGCTGGCTATCACAGATCCTGACATGATCAAAACAGTGCTAGTGAAAGAATGTTATTCT
GTCTTCACAAACCGGAGGCCTTTTGGTCCAGTGGGATTTATGAAAAGTGCCATCTCTATA
GCTGAGGATGAAGAATGGAAGAGATTACGATCATTGCTGTCTCCAACCTTCACCAGTGGA
AAACTCAAGGAGATGGTCCCTATCATTGCCCAGTATGGAGATGTGTTGGTGAGAAATCTG
AGGCGGGAAGCAGAGACAGGCAAGCCTGTCACCTTGAAAGACGTCTTTGGGGCCTACAGC
ATGGATGTGATCACTAGCACATCATTTGGAGTGAACATCGACTCTCTCAACAATCCACAA
GACCCCTTTGTGGAAAACACCAAGAAGCTTTTAAGATTTGATTTTTTGGATCCATTCTTT
CTCTCAATAACAGTCTTTCCATTCCTCATCCCAATTCTTGAAGTATTAAATATCTGTGTG
TTTCCAAGAGAAGTTACAAATTTTTTAAGAAAATCTGTAAAAAGGATGAAAGAAAGTCGC
CTCGAAGATACACAAAAGCACCGAGTGGATTTCCTTCAGCTGATGATTGACTCTCAGAAT
TCAAAAGAAACTGAGTCCCACAAAGCTCTGTCCGATCTGGAGCTCGTGGCCCAATCAATT
ATCTTTATTTTTGCTGGCTATGAAACCACGAGCAGTGTTCTCTCCTTCATTATGTATGAA
CTGGCCACTCACCCTGATGTCCAGCAGAAACTGCAGGAGGAAATTGATGCAGTTTTACCC
AATAAGGCACCACCCACCTATGATACTGTGCTACAGATGGAGTATCTTGACATGGTGGTG
AATGAAACGCTCAGATTATTCCCAATTGCTATGAGACTTGAGAGGGTCTGCAAAAAAGAT
GTTGAGATCAATGGGATGTTCATTCCCAAAGGGGTGGTGGTGATGATTCCAAGCTATGCT
CTTCACCGTGACCCAAAGTACTGGACAGAGCCTGAGAAGTTCCTCCCTGAAAGATTCAGC
AAGAAGAACAAGGACAACATAGATCCTTACATATACACACCCTTTGGAAGTGGACCCAGA
AACTGCATTGGCATGAGGTTTGCTCTCATGAACATGAAACTTGCTCTAATCAGAGTCCTT
CAGAACTTCTCCTTCAAACCTTGTAAAGAAACACAGATCCCCCTGAAATTAAGCTTAGGA
GGACTTCTTCAACCAGAAAAACCCGTTGTTCTAAAGGTTGAGTCAAGGGATGGCACCGTA
AGTGGAGCCTGA
PF00067
p450
function
oxidoreductase activity
function
ion binding
function
cation binding
function
transition metal ion binding
function
iron ion binding
function
binding
function
tetrapyrrole binding
function
catalytic activity
function
heme binding
function
monooxygenase activity
function
oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen
process
generation of precursor metabolites and energy
process
electron transport
process
physiological process
process
metabolism
process
cellular metabolism
unknown
unknown
"
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| ns1:drugCategory |
All properties reside in the graph file:///home/swish/src/ClioPatria/guidelines/drugbank_small.nt
The resource does not appear as an object