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Literature summary for 3.1.1.7 extracted from

  • Kim, J.H.; Hwang, C.E.; Yoon, K.A.; Seong, K.M.; Lee, J.; Kim, J.H.; Lee, S.H.
    Molecular and biochemical characterization of the bed bug salivary gland cholinesterase as an acetylcholine-sequestering enzyme (2018), Insect Biochem. Mol. Biol., 102, 52-58 .
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
recombinant expression of His-tagged enzyme ClSChE in Spodoptera frugiperda SF9 cells via transfection using the baculovirus system Cimex lectularius

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information Michaelis-Menten kinetics, recombinant enzyme Cimex lectularius
0.0000569
-
Acetylcholine pH 8.0, 25°C, recombinant enzyme Cimex lectularius

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular secretion of monomeric ClSChE through the proboscis during feeding Cimex lectularius
-
-
additional information isozyme ClSChE exists as two types, a dimer and a monomer, and neither is membrane-anchored, the soluble monomers of ClSChE are connected by a disulfide bond to form a dimer Cimex lectularius
-
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
acetylcholine + H2O Cimex lectularius
-
choline + acetate
-
?

Organism

Organism UniProt Comment Textmining
Cimex lectularius
-
Florida strain
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged enzyme ClSChE from Spodoptera frugiperda SF9 cells by affinity chromatography Cimex lectularius

Source Tissue

Source Tissue Comment Organism Textmining
salivary gland the common bed bug, Cimex lectularius, possesses a cholinesterase expressed exclusively in the salivary gland (ClSChE), molecular forms and tissue distribution patterns of ClSChE, immunohistochemical analysis confirms that ClSChE is expressed in the epithelial cells of both the salivary gland and the duct. ClSChE signal is slightly higher at the apical region of the main salivary gland than at the proximal part, and some ClSChE appears as aggregates dispersed inside the cytosol. In gland ducts, ClSChE staining is mainly localized in duct cells at the junction connecting to the main salivary gland. The salivary gland cells and some duct cells likely produce and secrete soluble ClSChE Cimex lectularius
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acetylcholine + H2O
-
Cimex lectularius choline + acetate
-
?

Subunits

Subunits Comment Organism
dimer 1 * 130000, SDS-PAGE, salivary gland enzyme ClSChE exists as a soluble monomeric form or a soluble dimeric form connected by a disulfide bridge Cimex lectularius
monomer 1 * 64000, SDS-PAGE, salivary gland enzyme ClSChE exists as a soluble monomeric form or a soluble dimeric form connected by a disulfide bridge, 1 * 54000, recombinant His-tagged enzyme, SDS-PAGE Cimex lectularius

Synonyms

Synonyms Comment Organism
ClSChE
-
Cimex lectularius
salivary gland-specific cholinesterase
-
Cimex lectularius

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
assay at Cimex lectularius

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.00008
-
Acetylcholine pH 8.0, 25°C, recombinant enzyme Cimex lectularius

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
assay at Cimex lectularius

General Information

General Information Comment Organism
evolution the bed bug uniquely possesses three genes encoding different cholinesterase (ChE) types [AChE1, AChE2 and salivary gland-specific cholinesterase (SChE)]. According to phylogenetic analysis, all three bed bug ChEs are categorized into a large clade of invertebrate ChEs. ClAChE1 is classified into the insect AChE1-type clade, whereas ClAChE2 is categorized into the insect AChE2-type clade. ClSChE is categorized into the clade containing the nematode and arachnid AChE1, which is closely located in an insect AChE1-type clade Cimex lectularius
physiological function salivary gland enzyme ClSChE functions virtually as an acetylcholine-sequestering protein by having a very strong affinity to acetylcholine but an extremely long turnover time. Given that ACh regulates a wide variety of host physiologies, the tentative roles of ClSChE in blood vessel constriction and itch/pain regulation in the host are analyzed Cimex lectularius

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
1.41
-
Acetylcholine pH 8.0, 25°C, recombinant enzyme Cimex lectularius