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Substrate Report for: Butyrylthiocholine

Butyrylthiocholine is a sulfur-containing analog of butyrylcholine which is hydrolyzed by butyrylcholinesterase to butyrate and thiocholine. It is used as a reagent in the determination of butyrylcholinesterase activity. Entry of reference human-BCHE


General
Type Butyrate, Trimethylammonium, Choline ester, Chromogen
Chemical_Nomenclature 2-butanoylsulfanylethyl(trimethyl)azanium
Canonical SMILES CCCC(=O)SCC[N+](C)(C)C
InChI InChI=1S/C9H20NOS/c1-5-6-9(11)12-8-7-10(2,3)4/h5-8H2,1-4H3/q+1
InChIKey AWBGQVBMGBZGLS-UHFFFAOYSA-N
Other name(s) CHEMBL139908 ; 2-(butanoylsulfanyl)-N,N,N-trimethylethanaminium ; 2-(BUTYRYLSULFANYL)-N,N,N-TRIMETHYLETHANAMINIUM ; CHEMBL148530 ; BTC
________________________________________________________________________________________________
MW|190.32
Formula|C9H20NOS
CAS_number|4555-00-4, 22026-63-7
PubChem|20689, 74630, 3015121, 25021344
UniChem|AWBGQVBMGBZGLS-UHFFFAOYSA-N
IUPHAR|
Wikipedia|

Target
Families | Butyrylthiocholine ligand of proteins in family: BCHE
Stucture | 1 structure: 2HA7: Crystal structure of mutant S203A of mouse acetylcholinesterase complexed with butyrylthiocholine
Protein | human-BCHE, mouse-BCHE, horse-BCHE

References:
Search PubMed for references concerning: Butyrylthiocholine

5 more
    Title: Substrate and product trafficking through the active center gorge of acetylcholinesterase analyzed by crystallography and equilibrium binding
    Bourne Y, Radic Z, Sulzenbacher G, Kim E, Taylor P, Marchot P
    Ref: Journal of Biological Chemistry, 281:29256, 2006 : PubMed

            

    Title: Effects of mutations of active site residues and amino acids interacting with the Omega loop on substrate activation of butyrylcholinesterase
    Masson P, Xie W, Froment MT, Lockridge O
    Ref: Biochimica & Biophysica Acta, 1544:166, 2001 : PubMed

            

    Title: Fasciculin 2 binds to the peripheral site on acetylcholinesterase and inhibits substrate hydrolysis by slowing a step involving proton transfer during enzyme acylation
    Eastman J, Wilson EJ, Cervenansky C, Rosenberry TL
    Ref: Journal of Biological Chemistry, 270:19694, 1995 : PubMed

            


human-ACHE
MutationKmKcatConditionPaper
> Mutations for human-ACHE (12)

human-BCHE
MutationKmKcatConditionPaper
> Mutations for human-BCHE (40)

mouse-ACHE
MutationKmKcatConditionPaper
> Mutations for mouse-ACHE (7)

mouse-BCHE
MutationKmKcatConditionPaper
WT 55 uM 37000 /min 100mM NaPhosphate Ph7.0 T22C Hosea_1995_Biochemistry_34_11528

WT Kinetics
Kinetic parametersKmKcatConditionsPapers
human-ACHE0.30 mM0.08 10+5/min IS 50mM phosphate pH8 T27C Kaplan_2001_Biochemistry_40_7433
human-ACHE2.5 mM70000 /min 50mM NaPhosphate pH7.4 Loewenstein-Lichtenstein_1996_Mol.Pharmacol_50_1423
human-BCHE0.05 mM1.1 10+5 /min IS 50mM phosphate pH8 T27C Kaplan_2001_Biochemistry_40_7433
human-BCHE2.8 & 0.7 mM98000 & 33000 /min 50mM NaPhosphate pH7.4 Loewenstein-Lichtenstein_1996_Mol.Pharmacol_50_1423
human-BCHE7 & 0.7 uM24000 & 10000 /min100mM K phosphate pH7.0 T25C Blong_1997_Biochem.J_327_747
human-BCHE2.2 mM-100mM Na phosphate pH7.4 T22C Gnatt_1994_J.Neurochem_62_749
mouse-ACHE93 uM1100 /min100mM NaPhosphate Ph7.0 T22C Hosea_1995_Biochemistry_34_11528
mouse-BCHE55 uM37000 /min100mM NaPhosphate Ph7.0 T22C Hosea_1995_Biochemistry_34_11528