TMTFA
Transition state analogue TMTFA is an equilibrium mixture of the free ketone and ketone hydrate NAF in aqueous solution, with a hydration equilibrium constant of 60 000
General
Type : Trifluoro, Trimethylammonium, Quaternary compound, Transition state analogue, Halo ketone
Chemical_Nomenclature : m-(N,N,N-Trimethylammonio)trifluoroacetophenone
Canonical SMILES : C[N+](C)(C)C1=CC=CC(=C1)C(=O)C(F)(F)F
InChI : InChI=1S\/C11H13F3NO\/c1-15(2,3)9-6-4-5-8(7-9)10(16)11(12,13)14\/h4-7H,1-3H3\/q+1
InChIKey : JIBZSTPMDKSJOX-UHFFFAOYSA-N
Other name(s) : m-(N,N,N-trimethylammonio)-2,2,2-trifluro-1,1-dihydroxyethylbenzene || CHEMBANK2333 || TFK
MW : 232.222
Formula : C11H13F3NO+
CAS_number :
PubChem : 5492
UniChem : JIBZSTPMDKSJOX-UHFFFAOYSA-N
Target
Families : TMTFA ligand of proteins in family
ACHE
Protein :
torca-ACHE
mouse-ACHE
References (10)
| Title : Drug and pro-drug substrates and pseudo-substrates of human butyrylcholinesterase - Masson_2023_Biochem.Pharmacol_218_115910 |
| Author(s) : Masson P , Shaihutdinova Z , Lockridge O |
| Ref : Biochemical Pharmacology , 218 :115910 , 2023 |
| Abstract : |
| PubMedSearch : Masson_2023_Biochem.Pharmacol_218_115910 |
| PubMedID: 37972875 |
| Title : 1-(3-Tert-Butylphenyl)-2,2,2-Trifluoroethanone as a Potent Transition-State Analogue Slow-Binding Inhibitor of Human Acetylcholinesterase: Kinetic, MD and QM\/MM Studies - Zueva_2020_Biomolecules_10_1608 |
| Author(s) : Zueva IV , Lushchekina SV , Pottie IR , Darvesh S , Masson P |
| Ref : Biomolecules , 10 : , 2020 |
| Abstract : |
| PubMedSearch : Zueva_2020_Biomolecules_10_1608 |
| PubMedID: 33260981 |
| Title : Substrate and product trafficking through the active center gorge of acetylcholinesterase analyzed by crystallography and equilibrium binding - Bourne_2006_J.Biol.Chem_281_29256 |
| Author(s) : Bourne Y , Radic Z , Sulzenbacher G , Kim E , Taylor P , Marchot P |
| Ref : Journal of Biological Chemistry , 281 :29256 , 2006 |
| Abstract : |
| PubMedSearch : Bourne_2006_J.Biol.Chem_281_29256 |
| PubMedID: 16837465 |
| Gene_locus related to this paper: mouse-ACHE |
| Title : A preliminary comparison of structural models for catalytic intermediates of acetylcholinesterase - Silman_1999_Chem.Biol.Interact_119-120_43 |
| Author(s) : Silman I , Millard CB , Ordentlich A , Greenblatt HM , Harel M , Barak D , Shafferman A , Sussman JL |
| Ref : Chemico-Biological Interactions , 119-120 :43 , 1999 |
| Abstract : |
| PubMedSearch : Silman_1999_Chem.Biol.Interact_119-120_43 |
| PubMedID: 10421437 |
| Gene_locus related to this paper: torca-ACHE |
| Title : Theoretical and experimental investigations of electrostatic effects on acetylcholinesterase catalysis and inhibition - Malany_1999_Chem.Biol.Interact_119-120_99 |
| Author(s) : Malany S , Baker NA , Verweyst M , Medhekar R , Quinn DM , Velan B , Kronman C , Shafferman A |
| Ref : Chemico-Biological Interactions , 119-120 :99 , 1999 |
| Abstract : |
| PubMedSearch : Malany_1999_Chem.Biol.Interact_119-120_99 |
| PubMedID: 10421443 |
| Title : Nonequilibrium analysis alters the mechanistic interpretation of inhibition of acetylcholinesterase by peripheral site ligands - Szegletes_1998_Biochemistry_37_4206 |
| Author(s) : Szegletes T , Mallender WD , Rosenberry TL |
| Ref : Biochemistry , 37 :4206 , 1998 |
| Abstract : |
| PubMedSearch : Szegletes_1998_Biochemistry_37_4206 |
| PubMedID: 9521743 |
| Title : Electrostatic influence on the kinetics of ligand binding to acetylcholinesterase. Distinctions between active center ligands and fasciculin - Radic_1997_J.Biol.Chem_272_23265 |
| Author(s) : Radic Z , Kirchhoff PD , Quinn DM , McCammon JA , Taylor P |
| Ref : Journal of Biological Chemistry , 272 :23265 , 1997 |
| Abstract : |
| PubMedSearch : Radic_1997_J.Biol.Chem_272_23265 |
| PubMedID: 9287336 |
| Title : The X-ray structure of a transition state analog complex reveals the molecular origins of the catalytic power and substrate specificity of acetylcholinesterase. - |
| Author(s) : Harel M , Quinn DM , Nair HK , Silman I , Sussman JL |
| Ref : Journal of the American Chemical Society , 118 :2340 , 1996 |
| PubMedID: |
| Gene_locus related to this paper: torca-ACHE |
| Title : Allosteric control of acetylcholinesterase catalysis by fasciculin - Radic_1995_J.Biol.Chem_270_20391 |
| Author(s) : Radic Z , Quinn DM , Vellom DC , Camp S , Taylor P |
| Ref : Journal of Biological Chemistry , 270 :20391 , 1995 |
| Abstract : |
| PubMedSearch : Radic_1995_J.Biol.Chem_270_20391 |
| PubMedID: 7657613 |
| Title : Molecular recognition in acetylcholinesterase catalysis: free-energy correlations for substrate turnover and inhibition by trifluoro ketone transition-state analogs - Nair_1994_Biochemistry_33_8566 |
| Author(s) : Nair HK , Seravalli J , Arbuckle T , Quinn DM |
| Ref : Biochemistry , 33 :8566 , 1994 |
| Abstract : |
| PubMedSearch : Nair_1994_Biochemistry_33_8566 |
| PubMedID: 8031791 |