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Substrate Report for: Acetylthiocholine

Synthetic substrate for the Ellman reaction (the free thiol product of reaction is detected colorimetrically with the DTNB reagent). Entry of reference human-ACHE. Acetylthiocholine is an agent used as a substrate in assays for cholinesterases, especially to discriminate among enzyme types.


General
Type Acetate, Trimethylammonium, Choline ester, Chromogen
Chemical_Nomenclature 2-acetylsulfanylethyl(trimethyl)azanium
Canonical SMILES CC(=O)SCC[N+](C)(C)C
InChI InChI=1S/C7H16NOS/c1-7(9)10-6-5-8(2,3)4/h5-6H2,1-4H3/q+1
InChIKey GFFIJCYHQYHUHB-UHFFFAOYSA-N
Other name(s) 2-(Thioacetyloxy)-N,N,N,-trimethylethanaminium (bromide or chloride) ; S-Acetylthiocholine ; 2ha5 ; AC1L2GHM ; Lopac-A-5626
________________________________________________________________________________________________
MW|162.27
Formula|C7H16NOS
CAS_number|4468-05-7
PubChem|20544, 74629, 22411, 90691, 547124
UniChem|GFFIJCYHQYHUHB-UHFFFAOYSA-N
IUPHAR|
Wikipedia|

Target
Families | Acetylthiocholine ligand of proteins in family: ACHE, BCHE, Cholinesterase, Cholinesterase-like
Stucture | 4 structures (e.g. : 2HA5, 2C4H, 2C58... more)
Protein | bunfa-ACHE, eleel-ACHE, chick-ACHE, human-ACHE, human-BCHE, mouse-ACHE, mouse-BCHE, ratno-ACHE, torca-ACHE, torma-ACHE

References:
Search PubMed for references concerning: Acetylthiocholine

10 more
    Title: Cloning and expression of acetylcholinesterase from Bungarus fasciatus venom. A new type of cooh-terminal domain; involvement of a positively charged residue in the peripheral site
    Cousin X, Bon S, Duval N, Massoulie J, Bon C
    Ref: Journal of Biological Chemistry, 271:15099, 1996 : PubMed

            

    Title: Acetylcholinesterase peripheral anionic site degeneracy conferred by amino acid arrays sharing a common core
    Barak D, Kronman C, Ordentlich A, Ariel N, Bromberg A, Marcus D, Lazar A, Velan B, Shafferman A
    Ref: Journal of Biological Chemistry, 269:6296, 1994 : PubMed

            

    Title: Hydrolysis of electronically and sterically defined substrates of acetylcholinesterase
    Hillman GR, Mautner HG
    Ref: Biochemistry, 9:2633, 1970 : PubMed

            


bunfa-ACHE
MutationKmKcatConditionPaper
K285D 58.7 & 4.1 uM - T25C IS 50 mM phosphate Cousin_1996_J.Biol.Chem_271_15099
M70Y 108.6 & 4.5 uM - T25C IS 50 mM phosphate Cousin_1996_J.Biol.Chem_271_15099
M70Y/K285D 95.3 & 5.9 uM - T25C IS 50 mM phosphate Cousin_1996_J.Biol.Chem_271_15099
WT 78.8 & 6.3 uM - T25C IS 50 mM phosphate Cousin_1996_J.Biol.Chem_271_15099

chick-ACHE
MutationKmKcatConditionPaper
WT - 175000/min 100mM NaP T28C pH7.0 Vigny_1978_Eur.J.Biochem_85_317

eleel-ACHE
MutationKmKcatConditionPaper
WT - 733333/min 100mM NaP T28C pH7.0 Vigny_1978_Eur.J.Biochem_85_317
WT 130 uM 900000 /min   Salih_1992_Biochem.J_285_451

human-ACHE
MutationKmKcatConditionPaper
> Mutations for human-ACHE (61)

human-BCHE
MutationKmKcatConditionPaper
WT 40 uM 0.5 10+5 /min IS 50mM phosphate pH8 T27C Kaplan_2001_Biochemistry_40_7433

mouse-ACHE
MutationKmKcatConditionPaper
> Mutations for mouse-ACHE (24)

mouse-BCHE
MutationKmKcatConditionPaper
WT 23 uM 40000 /min 100mM NaPhosphate Ph7.0 T22C Hosea_1995_Biochemistry_34_11528
WT 35 & 2 uM 40000 & 7000/min 100mM NaP pH7 T22C eq3 sch3 Radic_1993_Biochemistry_32_12074

mouse-chimerae-ACHE-BCHE
MutationKmKcatConditionPaper
B5-174-A175-487-B488-575 160 & 15 uM 120000 & 40000/min 100mM NaP pH7 T22C eq3 sch3 Radic_1993_Biochemistry_32_12074
B5-174-A175-575 160 & 2 uM 170000 & 20000/min 100mM NaP pH7 T22C eq3 sch3 Radic_1993_Biochemistry_32_12074

ratno-ACHE
MutationKmKcatConditionPaper
WT - 220000/min 100mM NaP T28C pH7.0 Vigny_1978_Eur.J.Biochem_85_317

torca-ACHE
MutationKmKcatConditionPaper
WT - 481666/min T25C pH7.8 Taylor_1974_Mol.Pharmacol_10_78

torma-ACHE
MutationKmKcatConditionPaper
WT - 273333/min 100mM NaP T28C pH7.0 Vigny_1978_Eur.J.Biochem_85_317
WT 81.2 & 4.2 uM - T25C IS 50 mM phosphate Cousin_1996_J.Biol.Chem_271_15099

WT Kinetics
Kinetic parametersKmKcatConditionsPapers
bunfa-ACHE78.8 & 6.3 uM- T25C IS 50 mM phosphate Cousin_1996_J.Biol.Chem_271_15099
chick-ACHE-175000/min 100mM NaP T28C pH7.0 Vigny_1978_Eur.J.Biochem_85_317
eleel-ACHE-733333/min 100mM NaP T28C pH7.0 Vigny_1978_Eur.J.Biochem_85_317
eleel-ACHE130 uM900000 /min  Salih_1992_Biochem.J_285_451
human-ACHE117 uM390000 /min50mM Na phosphate pH8.0 T27C Velan_1991_J.Biol.Chem_266_23977
human-ACHE140 uM370000/min IS 50mM phosphate pH8 T27C Ordentlich_1993_J.Biol.Chem_268_17083
human-ACHE140 uM4.0 10+5 /min IS 50mM phosphate pH8 T27C Kaplan_2001_Biochemistry_40_7433
human-ACHE140 & 50 uM370000 & 10000/min pH8 T27C 50mM Na phosphate Shafferman_1992_EMBO.J_11_3561
human-ACHE140 & 10 uM400000 & 50000/min 50mM NaPhosphate pH8 Kronman_1994_J.Biol.Chem_269_27819
human-ACHE120 uM420000/min 50mM Na phosphate pH8 Barak_1994_J.Biol.Chem_269_6296
human-ACHE140 & 20 uM400000 & 60000/min IS 150mM Shafferman_1994_EMBO.J_13_3448
human-ACHE80 & 10 uM400000 & 60000/min IS 5mM Shafferman_1994_EMBO.J_13_3448
human-ACHE140 uM400000/min 5 or 50mM Na Phosphate pH8 T27C Ordentlich_1995_J.Biol.Chem_270_2082
human-BCHE40 uM0.5 10+5 /min IS 50mM phosphate pH8 T27C Kaplan_2001_Biochemistry_40_7433
mouse-ACHE46 uM140000 /min100mM NaPhosphate Ph7.0 T22C Hosea_1995_Biochemistry_34_11528
mouse-ACHE 46 & 3 uM140000 & 10000/min 100mM NaP pH7 T22C eq3 sch3 Radic_1993_Biochemistry_32_12074
mouse-BCHE23 uM40000 /min100mM NaPhosphate Ph7.0 T22C Hosea_1995_Biochemistry_34_11528
mouse-BCHE 35 & 2 uM40000 & 7000/min 100mM NaP pH7 T22C eq3 sch3 Radic_1993_Biochemistry_32_12074
ratno-ACHE-220000/min 100mM NaP T28C pH7.0 Vigny_1978_Eur.J.Biochem_85_317
torca-ACHE-481666/minT25C pH7.8 Taylor_1974_Mol.Pharmacol_10_78
torma-ACHE-273333/min 100mM NaP T28C pH7.0 Vigny_1978_Eur.J.Biochem_85_317
torma-ACHE81.2 & 4.2 uM- T25C IS 50 mM phosphate Cousin_1996_J.Biol.Chem_271_15099