Information on EC 3.1.1.98 - [Wnt protein] O-palmitoleoyl-L-serine hydrolase and Organism(s) Homo sapiens

for references in articles please use BRENDA:EC3.1.1.98
Word Map on EC 3.1.1.98
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:
This record set is specific for:
Homo sapiens


The taxonomic range for the selected organisms is: Homo sapiens

The enzyme appears in selected viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.1.1.98
-
RECOMMENDED NAME
GeneOntology No.
[Wnt protein] O-palmitoleoyl-L-serine hydrolase
-
SYSTEMATIC NAME
IUBMB Comments
[Wnt]-O-(9Z)-hexadec-9-enoyl-L-serine acylhydrolase
The enzyme removes the palmitoleate modification that is introduced to specific L-serine residues in Wnt proteins by EC 2.3.1.250, [Wnt protein]-O-palmitoleoyl transferase.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
Notum requires glypicans to suppress Wnt signalling, but does not cleave their glycophosphatidylinositol anchor. Glycosaminoglycan binding sites on Notum probably help to co-localize with Wnt proteins. A large hydrophobic pocket at the active site accommodates palmitoleate
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
show the reaction diagram
-
-
-
?
[Wnt]-O-(9Z)-hexadec-9-enoyl-L-serine + H2O
[Wnt]-L-serine + (9Z)-hexadec-9-enoate
show the reaction diagram
-
Notum is a carboxylesterase that removes an essential palmitoleate moiety from Wnt proteins
-
?
additional information
?
-
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Phenylmethanesulfonylfluoride
strong inhibition of 4-nitrophenylacetate hydrolysis
Triton X-100
strong inhibition of 4-nitrophenylacetate hydrolysis
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
nine crystal forms at resolutions between 1.4 and 2.8 A. The catalytic triad comprises Ser232, Asp340 and His389