Literature summary for 3.1.1.1 extracted from

Correy, G.J.; Carr, P.D.; Meirelles, T.; Mabbitt, P.D.; Fraser, N.J.; Weik, M.; Jackson, C.J.
Mapping the accessible conformational landscape of an insect carboxylesterase using conformational ensemble analysis and kinetic crystallography (2016), Structure, 24, 977-987 .

Crystallization (Commentary)

Crystallization (Comment)	Organism
for investigation of binding-pocket heterogeneity, several previously published structures of enzyme LcalphaE7 in apostructure, with bound substrate and in phosphorylated form are re-processed to increase the amount of crystallographic data available, conformational selection upon substrate binding (PDB IDs are 5CH3, 5CH5, 5IVD, 5IVI, 5IVH, 5IVK, 4QWM, 4UBI, 4UBJ, 4UBK, 4UBM, 4UBL, 4UBN, 4UBO, 4W1Q, 4W1P, 4W1R, and 4W1S), overview	Lucilia cuprina

Crystallization (Comment)

Organism

for investigation of binding-pocket heterogeneity, several previously published structures of enzyme LcalphaE7 in apostructure, with bound substrate and in phosphorylated form are re-processed to increase the amount of crystallographic data available, conformational selection upon substrate binding (PDB IDs are 5CH3, 5CH5, 5IVD, 5IVI, 5IVH, 5IVK, 4QWM, 4UBI, 4UBJ, 4UBK, 4UBM, 4UBL, 4UBN, 4UBO, 4W1Q, 4W1P, 4W1R, and 4W1S), overview

Lucilia cuprina

Protein Variants

Protein Variants	Comment	Organism
M147A	site-directed mutagenesis, the mutant shows altered inhibition kinetics for inhibitor diethylumbelliferyl phosphate compared to wild-type enzyme	Lucilia cuprina
Y457A	site-directed mutagenesis, the mutant shows altered inhibition kinetics for inhibitor diethylumbelliferyl phosphate compared to wild-type enzyme	Lucilia cuprina

Inhibitors

Inhibitors	Comment	Organism	Structure
diethylumbelliferyl phosphate	-	Lucilia cuprina

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
additional information	-	additional information	Michaelis-Menten kinetics	Lucilia cuprina

Organism

Organism	UniProt	Comment	Textmining
Lucilia cuprina	Q25252	-	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
phosphoprotein	-	Lucilia cuprina

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	dephosphorylation is the rate-limiting step in the hydrolysis of organophosphates by enzyme LcalphaE7	Lucilia cuprina	?	-	?

Synonyms

Synonyms	Comment	Organism
alpha-esterase 7	-	Lucilia cuprina
LcalphaE7	-	Lucilia cuprina

General Information

General Information	Comment	Organism
additional information	residues Phe100, Met147, and Tyr457 are located near the substrate-binding pocket, multi-conformer modeling of Tyr457. Kinetic analysis of the role of Tyr457 and Met147 reveals catalytic evidence for dynamic coupling	Lucilia cuprina