Literature summary for 3.1.1.1 extracted from

Alves, M.; Lamego, J.; Bandeiras, T.; Castro, R.; Tomas, H.; Coroadinha, A.S.; Costa, J.; Simplicio, A.L.
Human carboxylesterase 2 studies on the role of glycosylation for enzymatic activity (2016), Biochem. Biophys. Rep., 5, 105-110 .

Search for more literature for 3.1.1.1

Cloned(Commentary)

Cloned (Comment)	Organism
CES2, recombinant expression of His10-tagged wild-type and mutant enzymes in HEK-293T cells, the enzyme is secreted to the cell medium	Homo sapiens

Protein Variants

Protein Variants	Comment	Organism
additional information	site-directed mutagenesis is used to replace the asparagine residues in the Asn-X-Ser/Thr sequons, by glutamine thus precluding binding of the sugar moieties to those putative sites. Each or the two potential N-glycosylation sites are mutated resulting in three mutated forms of the protein which lack either the first (p.Asn175Gln,Glyco1), the second (p. Asn340Gln, Glyco2) or both (p.Asn175Gln/Asn340Gln,Glyco1+2) glycosylation sites	Homo sapiens
N175Q	site-directed mutagenesis, the mutant lacks the first glycosylation site, the mutation reduces the catalytic activity (by 43%) and the thermostability of the enzyme compared to wild-type	Homo sapiens
N175Q/N340Q	site-directed mutagenesis, the mutant lacks both the glycosylation sites, the mutation reduces the catalytic activity (by 75%) and the thermostability of the enzyme compared to wild-type	Homo sapiens
N340Q	site-directed mutagenesis, the mutant lacks the second glycosylation site, the mutation reduces the catalytic activity (by 39%) and the thermostability of the enzyme compared to wild-type	Homo sapiens

Inhibitors

Inhibitors	Comment	Organism	Structure
additional information	tunicamycin leads to decreased levels of secreted hCES2, but the enzyme is still active	Homo sapiens

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
extracellular	the enzyme is secreted. Tunicamycin leads to decreased levels of secreted hCES2, but the enzyme is still active. Mutation of each and both N-glycosylation sites leads to decreased levels of secreted active hCES2	Homo sapiens	-	-

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	O00748	-	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
glycoprotein	N-glycosylation of hCES2 is relevant for thermostability of the enzyme and also for its in vivo folding or secretion, but is not crucial for enzyme activity. Carboxylesterase 2 (hCES2) is a glycoprotein. Partial or non-glycosylated forms of a secreted form of hCES2 are obtained by three approaches: (i) enzymatic deglycosylation with peptide N-glycosidase F, (ii) incubation with the inhibitor tunicamycin, (iii) site-directed mutagenesis of each or both N-glycosylation sites. Deglycosylated protein does not show a detectable decrease in enzyme activity. The glycans are involved, to some extent, in protein folding in vivo, but removal of glycans does not abrogate the activity of secreted hCES2. Deglycosylation of purified recombinant His10-tagged hCES2 shows a decreased level of detection using the glycoprotein detection method with the deglycosylated bands only being faintly detected probably due to nonspecific binding or to O-glycosylation	Homo sapiens

Synonyms

Synonyms	Comment	Organism
carboxylesterase 2	-	Homo sapiens
CES2	-	Homo sapiens
HCE2	-	Homo sapiens

General Information

General Information	Comment	Organism
evolution	carboxylesterases (CES) are a subset of esterases that belong to the alpha/beta hydrolase family	Homo sapiens
malfunction	mutation of each and both N-glycosylation sites leads to decreased levels of secreted active hCES2. The thermostability of the glycosylation mutants is decreased	Homo sapiens

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)