Aldehyde oxidase

Details

Name
Aldehyde oxidase
Kind
protein
Synonyms
  • 1.2.3.1
  • Aldehyde oxidase 1
  • AO
  • Azaheterocycle hydroxylase
Gene Name
AOX1
UniProtKB Entry
Q06278Swiss-Prot
Organism
Humans
NCBI Taxonomy ID
9606
Amino acid sequence
>lcl|BSEQ0006819|Aldehyde oxidase
MDRASELLFYVNGRKVIEKNVDPETMLLPYLRKKLRLTGTKYGCGGGGCGACTVMISRYN
PITKRIRHHPANACLIPICSLYGAAVTTVEGIGSTHTRIHPVQERIAKCHGTQCGFCTPG
MVMSIYTLLRNHPEPTLDQLTDALGGNLCRCTGYRPIIDACKTFCKTSGCCQSKENGVCC
LDQGINGLPEFEEGSKTSPKLFAEEEFLPLDPTQELIFPPELMIMAEKQSQRTRVFGSER
MMWFSPVTLKELLEFKFKYPQAPVIMGNTSVGPEVKFKGVFHPVIISPDRIEELSVVNHA
YNGLTLGAGLSLAQVKDILADVVQKLPEEKTQMYHALLKHLGTLAGSQIRNMASLGGHII
SRHPDSDLNPILAVGNCTLNLLSKEGKRQIPLNEQFLSKCPNADLKPQEILVSVNIPYSR
KWEFVSAFRQAQRQENALAIVNSGMRVFFGEGDGIIRELCISYGGVGPATICAKNSCQKL
IGRHWNEQMLDIACRLILNEVSLLGSAPGGKVEFKRTLIISFLFKFYLEVSQILKKMDPV
HYPSLADKYESALEDLHSKHHCSTLKYQNIGPKQHPEDPIGHPIMHLSGVKHATGEAIYC
DDMPLVDQELFLTFVTSSRAHAKIVSIDLSEALSMPGVVDIMTAEHLSDVNSFCFFTEAE
KFLATDKVFCVGQLVCAVLADSEVQAKRAAKRVKIVYQDLEPLILTIEESIQHNSSFKPE
RKLEYGNVDEAFKVVDQILEGEIHMGGQEHFYMETQSMLVVPKGEDQEMDVYVSTQFPKY
IQDIVASTLKLPANKVMCHVRRVGGAFGGKVLKTGIIAAVTAFAANKHGRAVRCVLERGE
DMLITGGRHPYLGKYKAGFMNDGRILALDMEHYSNAGASLDESLFVIEMGLLKMDNAYKF
PNLRCRGWACRTNLPSNTAFRGFGFPQAALITESCITEVAAKCGLSPEKVRIINMYKEID
QTPYKQEINAKNLIQCWRECMAMSSYSLRKVAVEKFNAENYWKKKGLAMVPLKFPVGLGS
RAAGQAAALVHIYLDGSVLVTHGGIEMGQGVHTKMIQVVSRELRMPMSNVHLRGTSTETV
PNANISGGSVVADLNGLAVKDACQTLLKRLEPIISKNPKGTWKDWAQTAFDESINLSAVG
YFRGYESDMNWEKGEGQPFEYFVYGAACSEVEIDCLTGDHKNIRTDIVMDVGCSINPAID
IGQIEGAFIQGMGLYTIEELNYSPQGILHTRGPDQYKIPAICDMPTELHIALLPPSQNSN
TLYSSKGLGESGVFLGCSVFFAIHDAVSAARQERGLHGPLTLNSPLTPEKIRMACEDKFT
KMIPRDEPGSYVPWNVPI
Number of residues
1338
Molecular Weight
147916.735
Theoretical pI
7.17
GO Classification
Functions
2 iron, 2 sulfur cluster binding / aldehyde oxidase activity / flavin adenine dinucleotide binding / iron ion binding / molybdopterin cofactor binding / NAD binding
Components
cytosol / extracellular exosome
General Function
Oxidase with broad substrate specificity, oxidizing aromatic azaheterocycles, such as N1-methylnicotinamide, N-methylphthalazinium and phthalazine, as well as aldehydes, such as benzaldehyde, retinal, pyridoxal, and vanillin. Plays a key role in the metabolism of xenobiotics and drugs containing aromatic azaheterocyclic substituents. Participates in the bioactivation of prodrugs such as famciclovir, catalyzing the oxidation step from 6-deoxypenciclovir to penciclovir, which is a potent antiviral agent. Is probably involved in the regulation of reactive oxygen species homeostasis. May be a prominent source of superoxide generation via the one-electron reduction of molecular oxygen. May also catalyze nitric oxide (NO) production via the reduction of nitrite to NO with NADH or aldehyde as electron donor. May play a role in adipogenesis
Specific Function
2 iron, 2 sulfur cluster binding
Pfam Domain Function
Signal Regions
Not Available
Transmembrane Regions
Not Available
Cellular Location
Cytoplasm
Gene sequence
>lcl|BSEQ0017136|Aldehyde oxidase (AOX1)
ATGGACCGGGCGTCCGAGCTGCTCTTCTACGTGAACGGCCGCAAGGTGATAGAAAAAAAT
GTCGATCCTGAAACAATGCTGTTGCCTTATTTGAGGAAGAAGCTTCGACTCACAGGAACT
AAGTATGGCTGTGGAGGAGGAGGCTGTGGTGCTTGTACAGTGATGATATCACGATACAAC
CCCATCACCAAGAGGATAAGGCATCACCCAGCCAATGCCTGTCTGATTCCCATCTGTTCT
CTGTATGGTGCTGCCGTCACCACAGTAGAAGGCATAGGAAGCACCCACACCAGAATTCAT
CCTGTTCAGGAGAGGATTGCCAAGTGTCATGGCACCCAGTGTGGCTTCTGCACACCTGGG
ATGGTGATGTCCATCTACACGCTGCTCAGGAACCACCCAGAGCCCACTCTGGATCAGTTA
ACTGATGCCCTTGGTGGTAACCTGTGCCGTTGCACTGGATACAGGCCCATAATTGATGCA
TGCAAGACTTTCTGTAAAACTTCGGGCTGCTGTCAAAGTAAAGAAAATGGGGTTTGCTGT
TTGGATCAAGGAATCAATGGATTGCCAGAATTTGAGGAAGGAAGTAAGACAAGTCCAAAA
CTCTTCGCAGAAGAGGAGTTTCTGCCATTGGATCCAACCCAGGAACTGATATTTCCTCCT
GAGCTAATGATAATGGCTGAGAAACAGTCGCAAAGGACCAGGGTGTTTGGCAGTGAGAGA
ATGATGTGGTTTTCCCCCGTGACCCTGAAGGAACTGCTGGAATTTAAATTCAAGTATCCC
CAGGCTCCTGTTATCATGGGAAACACCTCTGTGGGGCCTGAAGTGAAATTTAAAGGCGTC
TTTCACCCAGTTATAATTTCTCCTGATAGAATTGAAGAACTGAGTGTTGTAAACCATGCA
TATAATGGACTCACCCTTGGTGCTGGTCTCAGCCTAGCCCAGGTGAAGGACATTTTGGCT
GATGTAGTCCAGAAGCTTCCAGAGGAGAAGACACAGATGTACCATGCTCTCCTGAAGCAT
TTGGGAACTCTGGCTGGGTCCCAGATCAGGAACATGGCTTCTTTAGGGGGACACATCATT
AGCAGGCATCCAGATTCAGATCTGAATCCCATCCTGGCTGTGGGTAACTGTACCCTCAAC
TTGCTATCAAAAGAAGGAAAACGACAGATTCCTTTAAATGAGCAATTCCTCAGCAAGTGC
CCTAATGCAGATCTTAAGCCTCAAGAAATCTTGGTCTCAGTGAACATCCCCTACTCAAGG
AAGTGGGAATTTGTGTCAGCCTTCCGACAAGCCCAGCGACAGGAGAATGCGCTAGCGATA
GTCAATTCAGGAATGAGAGTCTTTTTTGGAGAAGGGGATGGCATTATTAGAGAGTTATGC
ATCTCATATGGAGGCGTTGGTCCAGCCACCATCTGTGCCAAGAATTCCTGCCAGAAACTC
ATTGGAAGGCACTGGAACGAACAGATGCTGGATATAGCCTGCAGGCTTATTCTGAATGAA
GTCTCCCTTTTGGGCTCGGCGCCAGGTGGGAAAGTGGAGTTCAAGAGGACTCTCATCATC
AGCTTCCTCTTCAAGTTCTACCTGGAAGTGTCACAGATTTTGAAAAAGATGGATCCAGTT
CACTATCCTAGCCTTGCAGACAAGTATGAAAGTGCTTTAGAAGATCTTCATTCCAAACAT
CACTGCAGTACATTAAAGTACCAGAATATAGGCCCAAAGCAGCATCCTGAAGACCCAATT
GGCCACCCCATCATGCATCTGTCTGGTGTGAAGCATGCCACGGGGGAGGCCATCTACTGT
GATGACATGCCTCTGGTGGACCAGGAACTTTTCTTGACTTTTGTGACTAGTTCAAGAGCT
CATGCTAAGATTGTGTCTATTGATCTGTCAGAAGCTCTCAGCATGCCCGGTGTGGTGGAC
ATCATGACAGCAGAACATCTTAGTGACGTCAACTCCTTCTGCTTTTTTACTGAAGCTGAG
AAATTTCTGGCGACAGATAAGGTGTTCTGTGTGGGTCAGCTTGTCTGTGCTGTGCTTGCC
GATTCTGAGGTTCAGGCAAAGCGAGCTGCTAAGCGAGTGAAGATTGTCTATCAAGACTTG
GAGCCGCTGATACTAACAATTGAGGAAAGTATACAACACAACTCCTCCTTCAAGCCAGAA
AGGAAACTGGAATATGGAAATGTTGACGAAGCATTTAAAGTGGTTGATCAAATTCTTGAA
GGTGAAATACATATGGGAGGTCAAGAACATTTTTATATGGAAACCCAAAGCATGCTTGTC
GTTCCCAAGGGAGAGGATCAAGAAATGGATGTCTACGTGTCCACACAGTTTCCCAAATAT
ATACAGGACATTGTTGCCTCAACCTTGAAGCTCCCAGCTAACAAGGTCATGTGCCATGTA
AGGCGTGTTGGTGGAGCGTTTGGAGGGAAGGTGTTAAAAACCGGAATCATTGCAGCCGTC
ACTGCATTTGCCGCAAACAAACATGGCCGTGCAGTTCGCTGTGTTCTGGAACGAGGAGAA
GACATGTTAATAACTGGAGGCCGCCATCCTTACCTTGGAAAGTACAAAGCTGGATTCATG
AACGATGGCAGAATCTTGGCCCTGGACATGGAGCATTACAGCAATGCAGGCGCCTCCTTG
GATGAATCATTATTCGTGATAGAAATGGGACTTCTGAAAATGGACAATGCTTACAAGTTT
CCCAATCTCCGCTGCCGGGGTTGGGCATGCAGAACCAACCTTCCATCCAACACAGCTTTT
CGTGGGTTTGGCTTTCCTCAGGCAGCGCTGATCACCGAATCTTGTATCACGGAAGTTGCA
GCCAAATGTGGACTATCCCCTGAGAAGGTGCGAATCATAAACATGTACAAGGAAATTGAT
CAAACACCCTACAAACAAGAGATCAATGCCAAGAACCTAATCCAGTGTTGGAGAGAATGT
ATGGCCATGTCTTCCTACTCCTTGAGGAAAGTTGCTGTGGAAAAGTTCAATGCAGAGAAT
TATTGGAAGAAGAAAGGACTGGCCATGGTCCCCCTGAAGTTTCCTGTTGGCCTTGGCTCA
CGTGCTGCTGGTCAGGCTGCTGCCTTGGTTCACATTTATCTTGATGGCTCTGTGCTGGTC
ACTCACGGTGGAATTGAAATGGGGCAGGGGGTCCACACTAAAATGATTCAGGTGGTCAGC
CGTGAATTAAGAATGCCAATGTCGAATGTCCACCTGCGTGGAACAAGCACAGAAACTGTC
CCTAATGCAAATATCTCTGGAGGTTCTGTGGTGGCAGATCTCAACGGTTTGGCAGTAAAG
GATGCCTGTCAAACTCTTCTAAAACGCCTCGAACCCATCATCAGCAAGAATCCTAAAGGA
ACTTGGAAAGACTGGGCACAGACTGCTTTTGATGAAAGCATTAACCTTTCAGCTGTTGGA
TACTTCAGAGGTTATGAGTCAGACATGAACTGGGAGAAAGGCGAAGGCCAGCCCTTCGAA
TACTTTGTTTATGGAGCTGCCTGTTCCGAGGTTGAAATAGACTGCCTGACGGGGGATCAT
AAGAACATCAGAACAGACATTGTCATGGATGTTGGCTGCAGTATAAATCCAGCCATTGAC
ATAGGCCAGATTGAAGGTGCATTTATTCAAGGCATGGGACTTTATACAATAGAGGAACTG
AATTATTCTCCCCAGGGCATTCTGCACACTCGTGGTCCAGACCAATATAAAATCCCTGCC
ATCTGTGACATGCCCACGGAGTTGCACATTGCTTTGTTGCCTCCTTCTCAAAACTCAAAT
ACTCTTTATTCATCTAAGGGTCTGGGAGAGTCGGGGGTGTTCCTGGGGTGTTCCGTGTTT
TTCGCTATCCATGACGCAGTGAGTGCAGCACGACAGGAGAGAGGCCTGCATGGACCCTTG
ACCCTTAATAGTCCACTGACCCCGGAGAAGATTAGGATGGCCTGTGAAGACAAGTTCACA
AAAATGATTCCGAGAGATGAACCTGGATCCTACGTTCCTTGGAATGTACCCATCTGA
Chromosome Location
2
Locus
2q33.1
External Identifiers
ResourceLink
UniProtKB IDQ06278
UniProtKB Entry NameAOXA_HUMAN
GenBank Protein ID438656
GenBank Gene IDL11005
GeneCard IDAOX1
HGNC IDHGNC:553
PDB ID(s)4UHW, 4UHX, 5EPG, 6Q6Q, 7OPN, 7ORC, 8EMT
KEGG IDhsa:316
IUPHAR/Guide To Pharmacology ID3186
NCBI Gene ID316
General References
  1. Wright RM, Vaitaitis GM, Wilson CM, Repine TB, Terada LS, Repine JE: cDNA cloning, characterization, and tissue-specific expression of human xanthine dehydrogenase/xanthine oxidase. Proc Natl Acad Sci U S A. 1993 Nov 15;90(22):10690-4. [Article]
  2. Ichida K, Matsumura T, Sakuma R, Hosoya T, Nishino T: Mutation of human molybdenum cofactor sulfurase gene is responsible for classical xanthinuria type II. Biochem Biophys Res Commun. 2001 Apr 20;282(5):1194-200. [Article]
  3. Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [Article]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [Article]
  5. Beedham C, Critchley DJ, Rance DJ: Substrate specificity of human liver aldehyde oxidase toward substituted quinazolines and phthalazines: a comparison with hepatic enzyme from guinea pig, rabbit, and baboon. Arch Biochem Biophys. 1995 Jun 1;319(2):481-90. [Article]
  6. Rashidi MR, Smith JA, Clarke SE, Beedham C: In vitro oxidation of famciclovir and 6-deoxypenciclovir by aldehyde oxidase from human, guinea pig, rabbit, and rat liver. Drug Metab Dispos. 1997 Jul;25(7):805-13. [Article]
  7. Neumeier M, Weigert J, Schaffler A, Weiss TS, Schmidl C, Buttner R, Bollheimer C, Aslanidis C, Scholmerich J, Buechler C: Aldehyde oxidase 1 is highly abundant in hepatic steatosis and is downregulated by adiponectin and fenofibric acid in hepatocytes in vitro. Biochem Biophys Res Commun. 2006 Nov 24;350(3):731-5. Epub 2006 Sep 27. [Article]
  8. Garattini E, Fratelli M, Terao M: Mammalian aldehyde oxidases: genetics, evolution and biochemistry. Cell Mol Life Sci. 2008 Apr;65(7-8):1019-48. [Article]
  9. Weigert J, Neumeier M, Bauer S, Mages W, Schnitzbauer AA, Obed A, Groschl B, Hartmann A, Schaffler A, Aslanidis C, Scholmerich J, Buechler C: Small-interference RNA-mediated knock-down of aldehyde oxidase 1 in 3T3-L1 cells impairs adipogenesis and adiponectin release. FEBS Lett. 2008 Aug 20;582(19):2965-72. doi: 10.1016/j.febslet.2008.07.034. Epub 2008 Jul 29. [Article]
  10. Zientek M, Jiang Y, Youdim K, Obach RS: In vitro-in vivo correlation for intrinsic clearance for drugs metabolized by human aldehyde oxidase. Drug Metab Dispos. 2010 Aug;38(8):1322-7. doi: 10.1124/dmd.110.033555. Epub 2010 May 5. [Article]
  11. Hutzler JM, Yang YS, Albaugh D, Fullenwider CL, Schmenk J, Fisher MB: Characterization of aldehyde oxidase enzyme activity in cryopreserved human hepatocytes. Drug Metab Dispos. 2012 Feb;40(2):267-75. doi: 10.1124/dmd.111.042861. Epub 2011 Oct 26. [Article]
  12. Strelevitz TJ, Orozco CC, Obach RS: Hydralazine as a selective probe inactivator of aldehyde oxidase in human hepatocytes: estimation of the contribution of aldehyde oxidase to metabolic clearance. Drug Metab Dispos. 2012 Jul;40(7):1441-8. doi: 10.1124/dmd.112.045195. Epub 2012 Apr 20. [Article]
  13. Garattini E, Terao M: The role of aldehyde oxidase in drug metabolism. Expert Opin Drug Metab Toxicol. 2012 Apr;8(4):487-503. doi: 10.1517/17425255.2012.663352. Epub 2012 Feb 16. [Article]
  14. Barr JT, Jones JP: Evidence for substrate-dependent inhibition profiles for human liver aldehyde oxidase. Drug Metab Dispos. 2013 Jan;41(1):24-9. doi: 10.1124/dmd.112.048546. Epub 2012 Sep 20. [Article]
  15. Fu C, Di L, Han X, Soderstrom C, Snyder M, Troutman MD, Obach RS, Zhang H: Aldehyde oxidase 1 (AOX1) in human liver cytosols: quantitative characterization of AOX1 expression level and activity relationship. Drug Metab Dispos. 2013 Oct;41(10):1797-804. doi: 10.1124/dmd.113.053082. Epub 2013 Jul 15. [Article]
  16. Bian Y, Song C, Cheng K, Dong M, Wang F, Huang J, Sun D, Wang L, Ye M, Zou H: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. J Proteomics. 2014 Jan 16;96:253-62. doi: 10.1016/j.jprot.2013.11.014. Epub 2013 Nov 22. [Article]
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Associated Data

Drug Relations
DrugDrug groupPharmacological action?TypeActionsDetails
Famciclovirapproved, investigationalunknownenzymesubstrateDetails
BrimonidineapprovedunknownenzymesubstrateDetails
MethotrexateapprovedunknownenzymesubstrateDetails
NADHapproved, nutraceuticalunknownenzymesubstrateDetails
Menadioneapproved, nutraceuticalunknownenzymeinhibitorDetails
Raloxifeneapproved, investigationalunknownenzymeinhibitorDetails
Zonisamideapproved, investigationalunknownenzymesubstrateDetails
Zaleplonapproved, illicit, investigationalunknownenzymesubstrateDetails
AllopurinolapprovedunknownenzymesubstrateDetails
Pyrazinamideapproved, investigationalunknownenzymesubstrateDetails
EniluracilinvestigationalunknowntargetDetails
Urethaneapproved, withdrawnunknownenzymesubstrateDetails
Aminocaproic acidapproved, investigationalunknownenzymesubstrateDetails
MercaptopurineapprovedunknownenzymesubstrateDetails
N-methylnicotinamideexperimentalunknownenzymesubstrateDetails
Lenvatinibapproved, investigationalnoenzymesubstrateDetails
IdelalisibapprovednoenzymesubstrateDetails
ZiprasidoneapprovednoenzymesubstrateDetails
CyclobenzaprineapprovedunknowntargetinhibitorDetails
Favipiravirapproved, investigationalnoenzymesubstrateinhibitorDetails
Capmatinibapproved, investigationalunknownenzymesubstrateDetails
EscitalopramapprovednoenzymesubstrateDetails
CitalopramapprovednoenzymesubstrateDetails
Menadioneapproved, nutraceuticalyestargetinhibitorDetails