Acetylcholinesterase

Details

Name
Acetylcholinesterase
Synonyms
  • 3.1.1.7
  • AChE
Gene Name
ACHE
Organism
Humans
Amino acid sequence
>lcl|BSEQ0000849|Acetylcholinesterase
MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPV
SAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPN
RELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSM
NYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASV
GMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTEL
VACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVG
VVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPE
DPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGY
EIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQ
YVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKN
QFDHYSKQDRCSDL
Number of residues
614
Molecular Weight
67795.525
Theoretical pI
6.24
GO Classification
Functions
acetylcholine binding / acetylcholinesterase activity / beta-amyloid binding / cholinesterase activity / collagen binding / hydrolase activity / laminin binding / protein homodimerization activity / serine hydrolase activity
Processes
acetylcholine catabolic process / acetylcholine catabolic process in synaptic cleft / amyloid precursor protein metabolic process / cell adhesion / cell proliferation / DNA replication / glycerophospholipid biosynthetic process / muscle organ development / negative regulation of synaptic transmission, cholinergic / nervous system development / neurotransmitter biosynthetic process / neurotransmitter receptor biosynthetic process / osteoblast development / phosphatidylcholine biosynthetic process / phospholipid metabolic process / positive regulation of protein secretion / protein tetramerization / receptor internalization / regulation of receptor recycling / response to wounding / retina development in camera-type eye / small molecule metabolic process / synapse assembly / synaptic transmission
Components
anchored component of membrane / basal lamina / cell junction / cell surface / extracellular region / extracellular space / Golgi apparatus / membrane / neuromuscular junction / nucleus / perinuclear region of cytoplasm / plasma membrane / synapse / synaptic cleft
General Function
Serine hydrolase activity
Specific Function
Terminates signal transduction at the neuromuscular junction by rapid hydrolysis of the acetylcholine released into the synaptic cleft. Role in neuronal apoptosis.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Cell junction
Gene sequence
>lcl|BSEQ0010296|Acetylcholinesterase (ACHE)
ATGAGGCCCCCGCAGTGTCTGCTGCACACGCCTTCCCTGGCTTCCCCACTCCTTCTCCTC
CTCCTCTGGCTCCTGGGTGGAGGAGTGGGGGCTGAGGGCCGGGAGGATGCAGAGCTGCTG
GTGACGGTGCGTGGGGGCCGGCTGCGGGGCATTCGCCTGAAGACCCCCGGGGGCCCTGTC
TCTGCTTTCCTGGGCATCCCCTTTGCGGAGCCACCCATGGGACCCCGTCGCTTTCTGCCA
CCGGAGCCCAAGCAGCCTTGGTCAGGGGTGGTAGACGCTACAACCTTCCAGAGTGTCTGC
TACCAATATGTGGACACCCTATACCCAGGTTTTGAGGGCACCGAGATGTGGAACCCCAAC
CGTGAGCTGAGCGAGGACTGCCTGTACCTCAACGTGTGGACACCATACCCCCGGCCTACA
TCCCCCACCCCTGTCCTCGTCTGGATCTATGGGGGTGGCTTCTACAGTGGGGCCTCCTCC
TTGGACGTGTACGATGGCCGCTTCTTGGTACAGGCCGAGAGGACTGTGCTGGTGTCCATG
AACTACCGGGTGGGAGCCTTTGGCTTCCTGGCCCTGCCGGGGAGCCGAGAGGCCCCGGGC
AATGTGGGTCTCCTGGATCAGAGGCTGGCCCTGCAGTGGGTGCAGGAGAACGTGGCAGCC
TTCGGGGGTGACCCGACATCAGTGACGCTGTTTGGGGAGAGCGCGGGAGCCGCCTCGGTG
GGCATGCACCTGCTGTCCCCGCCCAGCCGGGGCCTGTTCCACAGGGCCGTGCTGCAGAGC
GGTGCCCCCAATGGACCCTGGGCCACGGTGGGCATGGGAGAGGCCCGTCGCAGGGCCACG
CAGCTGGCCCACCTTGTGGGCTGTCCTCCAGGCGGCACTGGTGGGAATGACACAGAGCTG
GTAGCCTGCCTTCGGACACGACCAGCGCAGGTCCTGGTGAACCACGAATGGCACGTGCTG
CCTCAAGAAAGCGTCTTCCGGTTCTCCTTCGTGCCTGTGGTAGATGGAGACTTCCTCAGT
GACACCCCAGAGGCCCTCATCAACGCGGGAGACTTCCACGGCCTGCAGGTGCTGGTGGGT
GTGGTGAAGGATGAGGGCTCGTATTTTCTGGTTTACGGGGCCCCAGGCTTCAGCAAAGAC
AACGAGTCTCTCATCAGCCGGGCCGAGTTCCTGGCCGGGGTGCGGGTCGGGGTTCCCCAG
GTAAGTGACCTGGCAGCCGAGGCTGTGGTCCTGCATTACACAGACTGGCTGCATCCCGAG
GACCCGGCACGCCTGAGGGAGGCCCTGAGCGATGTGGTGGGCGACCACAATGTCGTGTGC
CCCGTGGCCCAGCTGGCTGGGCGACTGGCTGCCCAGGGTGCCCGGGTCTACGCCTACGTC
TTTGAACACCGTGCTTCCACGCTCTCCTGGCCCCTGTGGATGGGGGTGCCCCACGGCTAC
GAGATCGAGTTCATCTTTGGGATCCCCCTGGACCCCTCTCGAAACTACACGGCAGAGGAG
AAAATCTTCGCCCAGCGACTGATGCGATACTGGGCCAACTTTGCCCGCACAGGGGATCCC
AATGAGCCCCGAGACCCCAAGGCCCCACAATGGCCCCCGTACACGGCGGGGGCTCAGCAG
TACGTTAGTCTGGACCTGCGGCCGCTGGAGGTGCGGCGGGGGCTGCGCGCCCAGGCCTGC
GCCTTCTGGAACCGCTTCCTCCCCAAATTGCTCAGCGCCACCGACACGCTCGACGAGGCG
GAGCGCCAGTGGAAGGCCGAGTTCCACCGCTGGAGCTCCTACATGGTGCACTGGAAGAAC
CAGTTCGACCACTACAGCAAGCAGGATCGCTGCTCAGACCTGTGA
Chromosome Location
7
Locus
7q22
External Identifiers
ResourceLink
UniProtKB IDP22303
UniProtKB Entry NameACES_HUMAN
GenBank Protein ID177975
GenBank Gene IDM55040
GenAtlas IDACHE
HGNC IDHGNC:108
General References
  1. Soreq H, Ben-Aziz R, Prody CA, Seidman S, Gnatt A, Neville L, Lieman-Hurwitz J, Lev-Lehman E, Ginzberg D, Lipidot-Lifson Y, et al.: Molecular cloning and construction of the coding region for human acetylcholinesterase reveals a G + C-rich attenuating structure. Proc Natl Acad Sci U S A. 1990 Dec;87(24):9688-92. [PubMed:2263619]
  2. Karpel R, Ben Aziz-Aloya R, Sternfeld M, Ehrlich G, Ginzberg D, Tarroni P, Clementi F, Zakut H, Soreq H: Expression of three alternative acetylcholinesterase messenger RNAs in human tumor cell lines of different tissue origins. Exp Cell Res. 1994 Feb;210(2):268-77. [PubMed:8299725]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed:14702039]
  4. Hillier LW, Fulton RS, Fulton LA, Graves TA, Pepin KH, Wagner-McPherson C, Layman D, Maas J, Jaeger S, Walker R, Wylie K, Sekhon M, Becker MC, O'Laughlin MD, Schaller ME, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Cordes M, Du H, Sun H, Edwards J, Bradshaw-Cordum H, Ali J, Andrews S, Isak A, Vanbrunt A, Nguyen C, Du F, Lamar B, Courtney L, Kalicki J, Ozersky P, Bielicki L, Scott K, Holmes A, Harkins R, Harris A, Strong CM, Hou S, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Leonard S, Rohlfing T, Rock SM, Tin-Wollam AM, Abbott A, Minx P, Maupin R, Strowmatt C, Latreille P, Miller N, Johnson D, Murray J, Woessner JP, Wendl MC, Yang SP, Schultz BR, Wallis JW, Spieth J, Bieri TA, Nelson JO, Berkowicz N, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Bedell JA, Mardis ER, Clifton SW, Chissoe SL, Marra MA, Raymond C, Haugen E, Gillett W, Zhou Y, James R, Phelps K, Iadanoto S, Bubb K, Simms E, Levy R, Clendenning J, Kaul R, Kent WJ, Furey TS, Baertsch RA, Brent MR, Keibler E, Flicek P, Bork P, Suyama M, Bailey JA, Portnoy ME, Torrents D, Chinwalla AT, Gish WR, Eddy SR, McPherson JD, Olson MV, Eichler EE, Green ED, Waterston RH, Wilson RK: The DNA sequence of human chromosome 7. Nature. 2003 Jul 10;424(6945):157-64. [PubMed:12853948]
  5. 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. [PubMed:15489334]
  6. Wilson MD, Riemer C, Martindale DW, Schnupf P, Boright AP, Cheung TL, Hardy DM, Schwartz S, Scherer SW, Tsui LC, Miller W, Koop BF: Comparative analysis of the gene-dense ACHE/TFR2 region on human chromosome 7q22 with the orthologous region on mouse chromosome 5. Nucleic Acids Res. 2001 Mar 15;29(6):1352-65. [PubMed:11239002]
  7. Chhajlani V, Derr D, Earles B, Schmell E, August T: Purification and partial amino acid sequence analysis of human erythrocyte acetylcholinesterase. FEBS Lett. 1989 Apr 24;247(2):279-82. [PubMed:2714437]
  8. Velan B, Grosfeld H, Kronman C, Leitner M, Gozes Y, Lazar A, Flashner Y, Marcus D, Cohen S, Shafferman A: The effect of elimination of intersubunit disulfide bonds on the activity, assembly, and secretion of recombinant human acetylcholinesterase. Expression of acetylcholinesterase Cys-580----Ala mutant. J Biol Chem. 1991 Dec 15;266(35):23977-84. [PubMed:1748670]
  9. Shafferman A, Kronman C, Flashner Y, Leitner M, Grosfeld H, Ordentlich A, Gozes Y, Cohen S, Ariel N, Barak D, et al.: Mutagenesis of human acetylcholinesterase. Identification of residues involved in catalytic activity and in polypeptide folding. J Biol Chem. 1992 Sep 5;267(25):17640-8. [PubMed:1517212]
  10. Yang L, He HY, Zhang XJ: Increased expression of intranuclear AChE involved in apoptosis of SK-N-SH cells. Neurosci Res. 2002 Apr;42(4):261-8. [PubMed:11985878]
  11. Felder CE, Botti SA, Lifson S, Silman I, Sussman JL: External and internal electrostatic potentials of cholinesterase models. J Mol Graph Model. 1997 Oct;15(5):318-27, 335-7. [PubMed:9640563]
  12. Kryger G, Harel M, Giles K, Toker L, Velan B, Lazar A, Kronman C, Barak D, Ariel N, Shafferman A, Silman I, Sussman JL: Structures of recombinant native and E202Q mutant human acetylcholinesterase complexed with the snake-venom toxin fasciculin-II. Acta Crystallogr D Biol Crystallogr. 2000 Nov;56(Pt 11):1385-94. [PubMed:11053835]
  13. Dvir H, Harel M, Bon S, Liu WQ, Vidal M, Garbay C, Sussman JL, Massoulie J, Silman I: The synaptic acetylcholinesterase tetramer assembles around a polyproline II helix. EMBO J. 2004 Nov 10;23(22):4394-405. Epub 2004 Nov 4. [PubMed:15526038]
  14. Carletti E, Colletier JP, Dupeux F, Trovaslet M, Masson P, Nachon F: Structural evidence that human acetylcholinesterase inhibited by tabun ages through O-dealkylation. J Med Chem. 2010 May 27;53(10):4002-8. doi: 10.1021/jm901853b. [PubMed:20408548]
  15. Cheung J, Rudolph MJ, Burshteyn F, Cassidy MS, Gary EN, Love J, Franklin MC, Height JJ: Structures of human acetylcholinesterase in complex with pharmacologically important ligands. J Med Chem. 2012 Nov 26;55(22):10282-6. doi: 10.1021/jm300871x. Epub 2012 Nov 12. [PubMed:23035744]
  16. Nachon F, Carletti E, Ronco C, Trovaslet M, Nicolet Y, Jean L, Renard PY: Crystal structures of human cholinesterases in complex with huprine W and tacrine: elements of specificity for anti-Alzheimer's drugs targeting acetyl- and butyryl-cholinesterase. Biochem J. 2013 Aug 1;453(3):393-9. doi: 10.1042/BJ20130013. [PubMed:23679855]
  17. Bartels CF, Zelinski T, Lockridge O: Mutation at codon 322 in the human acetylcholinesterase (ACHE) gene accounts for YT blood group polymorphism. Am J Hum Genet. 1993 May;52(5):928-36. [PubMed:8488842]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB00382Tacrineapproved, investigational, withdrawnyesinhibitorDetails
DB00545Pyridostigmineapproved, investigationalyesantagonistinhibitorDetails
DB00674GalantamineapprovedyesinhibitorDetails
DB00843DonepezilapprovedyesinhibitorDetails
DB00944DemecariumapprovedyesinhibitorDetails
DB01010EdrophoniumapprovedyesinhibitorDetails
DB01122AmbenoniumapprovedyesinhibitorDetails
DB00122Cholineapproved, nutraceuticalunknownproduct ofDetails
DB00483Gallamine TriethiodideapprovedyesinhibitorDetails
DB00981Physostigmineapproved, investigationalyesinhibitorDetails
DB00989Rivastigmineapproved, investigationalyesinhibitorDetails
DB01199TubocurarineapprovedunknowninhibitorDetails
DB01245DecamethoniumapprovedunknowninhibitorDetails
DB01364EphedrineapprovedunknownDetails
DB01400Neostigmineapproved, vet_approvedyesinhibitorDetails
DB01805MonoisopropylphosphorylserineexperimentalunknownDetails
DB02166PropidiumexperimentalunknownDetails
DB022263,8-Diamino-6-Phenyl-5-[6-[1-[2-[(1,2,3,4-Tetrahydro-9-Acridinyl)Amino]Ethyl]-1h-1,2,3-Triazol-4-Yl]Hexyl]-PhenanthridiniumexperimentalunknownDetails
DB02673(4ar,6s,8ar)-11-[8-(1,3-Dioxo-1,3-Dihydro-2h-Isoindol-2-Yl)Octyl]-6-Hydroxy-3-Methoxy-5,6,9,10-Tetrahydro-4ah-[1]Benzofuro[3a,3,2-Ef][2]Benzazepin-11-IumexperimentalunknownDetails
DB02825Methylphosphonic Acid Ester GroupexperimentalunknownDetails
DB030053,8-Diamino-6-Phenyl-5-[6-[1-[2-[(1,2,3,4-Tetrahydro-9-Acridinyl)Amino]Ethyl]-1h-1,2,3-Triazol-5-Yl]Hexyl]-PhenanthridiniumexperimentalunknownDetails
DB03128Acetylcholineapproved, investigationalunknownDetails
DB03283beta-L-fucoseexperimentalunknownDetails
DB03359M-(N,N,N-Trimethylammonio)-2,2,2-Trifluoro-1,1-DihydroxyethylbenzeneexperimentalunknownDetails
DB03740N-acetyl-alpha-D-glucosamineexperimentalunknownDetails
DB038142-(N-Morpholino)-Ethanesulfonic AcidexperimentalunknownDetails
DB00677Isoflurophateapproved, investigational, withdrawnyesinhibitorDetails
DB04859ZanapezilinvestigationalunknownDetails
DB04864Huperzine Aapproved, experimentalunknowninhibitorDetails
DB03348Huperzine BinvestigationalunknownDetails
DB04892PhenserineinvestigationalunknownDetails
DB04924ItoprideinvestigationalunknowninhibitorDetails
DB04614(R)-tacrine(10)-hupyridoneexperimentalunknownDetails
DB04615(S)-tacrine(10)-hupyridoneexperimentalunknownDetails
DB04616TACRINE(8)-4-AMINOQUINOLINEexperimentalunknownDetails
DB06525GanstigmineinvestigationalunknownDetails
DB04617(9S)-9-[(8-AMMONIOOCTYL)AMINO]-1,2,3,4,9,10-HEXAHYDROACRIDINIUMexperimentalunknownDetails
DB07555Hydroxy(oxo)(2-{(1S)-2,2,2-trifluoro-1-[2-(trimethylarsonio)ethoxy]ethyl}phenyl)ammoniumexperimentalunknownDetails
DB077011-BENZYL-4-[(5,6-DIMETHOXY-1-INDANON-2-YL)METHYL]PIPERIDINEexperimentalunknownDetails
DB077561-[3-({[(4-AMINO-5-FLUORO-2-METHYLQUINOLIN-3-YL)METHYL]THIO}METHYL)PHENYL]-2,2,2-TRIFLUOROETHANE-1,1-DIOLexperimentalunknownDetails
DB078461S,3AS,8AS-TRIMETHYL-1-OXIDO-1,2,3,3A,8,8A-HEXAHYDROPYRROLO[2,3-B]INDOL-5-YL 2-ETHYLPHENYLCARBAMATEexperimentalunknownDetails
DB041143-Chloro-9-Ethyl-6,7,8,9,10,11-Hexahydro-7,11-Methanocycloocta[B]Quinolin-12-AmineexperimentalunknownDetails
DB08167Methylthioniniumexperimental, investigationalunknownDetails
DB04021MF268experimentalunknownDetails
DB023433,6,9,12,15-PentaoxaheptadecaneexperimentalunknownDetails
DB083571-ETHOXY-2-(2-ETHOXYETHOXY)ETHANEexperimentalunknownDetails
DB024041-Deoxy-1-Thio-Heptaethylene GlycolexperimentalunknownDetails
DB045563-[(1s)-1-(Dimethylamino)Ethyl]PhenolexperimentalunknownDetails
DB086152-[4-(DIMETHYLAMINO)PHENYL]-6-HYDROXY-3-METHYL-1,3-BENZOTHIAZOL-3-IUMexperimentalunknownDetails
DB00805MinaprineapprovedyesinhibitorDetails
DB00733Pralidoximeapproved, vet_approvedyesactivatorDetails
DB02845Methylphosphinic AcidexperimentalunknownDetails
DB00358Mefloquineapproved, investigationalunknowninhibitorDetails
DB00449DipivefrinapprovedunknowninhibitorDetails
DB08996Dimetacrineexperimental, withdrawnyesantagonistDetails
DB01233Metoclopramideapproved, investigationalunknowninhibitorDetails
DB00863RanitidineapprovedunknowninhibitorDetails
DB00411CarbamoylcholineapprovedunknownDetails
DB14006Choline salicylateapproved, nutraceuticalunknownproduct ofDetails
DB13503TyrothricinapprovedunknowninhibitorDetails