Any feedback?
Information on EC 2.3.1.250 - [Wnt protein] O-palmitoleoyl transferase
for references in articles please use BRENDA:EC2.3.1.250Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
2.3.1.250 [Wnt protein] O-palmitoleoyl transferaseIUBMB Comments
The enzyme, found in animals, modifies a specific serine residue in Wnt proteins, e.g. Ser209 in human Wnt3a and Ser224 in chicken WNT1 [2,3]. The enzyme can accept C13 to C16 fatty acids in vitro, but only (9Z)-hexadecenoate modification is observed in vivo . cf. EC 3.1.1.98, [Wnt protein]-O-palmitoleoyl-L-serine hydrolase.
Specify your search results
Word Map
The enzyme appears in viruses and cellular organisms
Reaction Schemes
+
[Wnt]-L-serine
=
+
[Wnt]-O-(9Z)-hexadec-9-enoyl-L-serine
Synonyms
porcupine, porcn, mom-1, mporc, mporcd, xporc, 
more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
PORC
PORCN
porcupine
PORCN
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(9Z)-hexadec-9-enoyl-CoA + [Wnt]-L-serine = CoA + [Wnt]-O-(9Z)-hexadec-9-enoyl-L-serine
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
(9Z)-hexadec-9-enoyl-CoA:[Wnt]-L-serine O-hexadecenoyltransferase
The enzyme, found in animals, modifies a specific serine residue in Wnt proteins, e.g. Ser209 in human Wnt3a and Ser224 in chicken WNT1 [2,3]. The enzyme can accept C13 to C16 fatty acids in vitro, but only (9Z)-hexadecenoate modification is observed in vivo [1]. cf. EC 3.1.1.98, [Wnt protein]-O-palmitoleoyl-L-serine hydrolase.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(9Z)-hexadec-9-enoyl-CoA + [Wnt3a]-L-serine
CoA + [Wnt3a]-O-(9Z)-hexadec-9-enoyl-L-serine
(9Z)-hexadec-9-enoyl-CoA + [Wnt3]-L-serine
CoA + [Wnt3]-O-(9Z)-hexadec-9-enoyl-L-serine
-
-
-
?
(9Z)-hexadec-9-enoyl-CoA + [Wnt5]-L-serine
CoA + [Wnt5]-O-(9Z)-hexadec-9-enoyl-L-serine
-
-
-
?
decanoyl-CoA + [Wnt]-L-serine
CoA + [Wnt]-O-decanoyl-L-serine
about 30% of the activity as compared to (9Z)-hexadec-9-enoyl-CoA. There is an increase in the catalytic activity from hexanoyl-CoA to decanoyl-CoA, after which there is an abrupt drop for dodecanoyl-CoA. Upon further increase in fatty acyl chain length, the activity stays at approximately the same level until the unsaturated palmitoleoyl-CoA, which is the best substrate
-
-
?
dodecanoyl-CoA + [Wnt]-L-serine
CoA + [Wnt]-O-dodecanoyl-L-serine
about 15% of the activity as compared to (9Z)-hexadec-9-enoyl-CoA. There is an increase in the catalytic activity from hexanoyl-CoA to decanoyl-CoA, after which there is an abrupt drop for dodecanoyl-CoA. Upon further increase in fatty acyl chain length, the activity stays at approximately the same level until the unsaturated palmitoleoyl-CoA, which is the best substrate
-
-
?
hexanoyl-CoA + [Wnt]-L-serine
CoA + [Wnt]-O-hexanoyl-L-serine
about 20% of the activity as compared to (9Z)-hexadec-9-enoyl-CoA. There is an increase in the catalytic activity from hexanoyl-CoA to decanoyl-CoA, after which there is an abrupt drop for dodecanoyl-CoA. Upon further increase in fatty acyl chain length, the activity stays at approximately the same level until the unsaturated palmitoleoyl-CoA, which is the best substrate
-
-
?
octanoyl-CoA + [Wnt]-L-serine
CoA + [Wnt]-O-octanoyl-L-serine
about 25% of the activity as compared to (9Z)-hexadec-9-enoyl-CoA. There is an increase in the catalytic activity from hexanoyl-CoA to decanoyl-CoA, after which there is an abrupt drop for dodecanoyl-CoA. Upon further increase in fatty acyl chain length, the activity stays at approximately the same level until the unsaturated palmitoleoyl-CoA, which is the best substrate
-
-
?
tetradecanoyl-CoA + [Wnt]-L-serine
CoA + [Wnt]-O-tetradecanoyl-L-serine
about 10% of the activity as compared to (9Z)-hexadec-9-enoyl-CoA. There is an increase in the catalytic activity from hexanoyl-CoA to decanoyl-CoA, after which there is an abrupt drop for dodecanoyl-CoA. Upon further increase in fatty acyl chain length, the activity stays at approximately the same level until the unsaturated palmitoleoyl-CoA, which is the best substrate
-
-
?
[125I]iodo-pentadecenoyl-CoA + [Wnt]-L-serine
CoA + [Wnt]-O-[125I]iodo-pentadecenoyl-L-serine
[125I]iodo-pentadecenoyl-CoA is a radioiodinated palmitoleate analog
-
-
?
(9Z)-hexadec-9-enoyl-CoA + [Wg]-L-serine
CoA + [Wg]-O-(9Z)-hexadec-9-enoyl-L-serine
-
-
-
?
(9Z)-hexadec-9-enoyl-CoA + [Wg]-L-serine
CoA + [Wg]-O-(9Z)-hexadec-9-enoyl-L-serine
Wnt substrate from Drosophila melanogaster
-
-
?
(9Z)-hexadec-9-enoyl-CoA + [Wnt1]-L-serine
CoA + [Wnt1]-O-(9Z)-hexadec-9-enoyl-L-serine
-
-
-
-
?
(9Z)-hexadec-9-enoyl-CoA + [Wnt1]-L-serine
CoA + [Wnt1]-O-(9Z)-hexadec-9-enoyl-L-serine
-
chicken substrate, and chimeric recombinant substrate containing amino acids 1-63 from mouse Wnt1 (-EPSLQL) and amino acids 64-370 from chicken Wnt1 (LSRKQ-)
-
-
?
(9Z)-hexadec-9-enoyl-CoA + [Wnt1]-L-serine
CoA + [Wnt1]-O-(9Z)-hexadec-9-enoyl-L-serine
-
-
-
?
(9Z)-hexadec-9-enoyl-CoA + [Wnt1]-L-serine
CoA + [Wnt1]-O-(9Z)-hexadec-9-enoyl-L-serine
chick WNT1 protein, the enzyme is an O-acyl transferase for WNT1 protein, WNT1 residues 214-234 are sufficient for PORCN-dependent palmitoylation of Ser224. Substitution of Ser224 with Thr, but not Cys, is tolerated in palmitoylation and biological assays. Transiently transfection of HEK-293T cells with WNT1. WNT1 mutant S224T is accepted as substrate, while mutants S224A and S224C are inactive
-
-
?
(9Z)-hexadec-9-enoyl-CoA + [Wnt1]-L-serine
CoA + [Wnt1]-O-(9Z)-hexadec-9-enoyl-L-serine
chicken substrate, and chimeric recombinant substrate containing amino acids 1-63 from mouse Wnt1 (-EPSLQL) and amino acids 64-370 from chicken Wnt1 (LSRKQ-)
-
-
?
(9Z)-hexadec-9-enoyl-CoA + [Wnt1]-L-serine
CoA + [Wnt1]-O-(9Z)-hexadec-9-enoyl-L-serine
-
-
-
?
(9Z)-hexadec-9-enoyl-CoA + [Wnt1]-L-serine
CoA + [Wnt1]-O-(9Z)-hexadec-9-enoyl-L-serine
chicken substrate, and chimeric recombinant substrate containing amino acids 1-63 from mouse Wnt1 (-EPSLQL) and amino acids 64-370 from chicken Wnt1 (LSRKQ-)
-
-
?
(9Z)-hexadec-9-enoyl-CoA + [Wnt3a]-L-serine
CoA + [Wnt3a]-O-(9Z)-hexadec-9-enoyl-L-serine
-
the enzyme catalyzes the palmitoylation of Ser209 and Cys77 of Wnt3a
-
-
?
(9Z)-hexadec-9-enoyl-CoA + [Wnt3a]-L-serine
CoA + [Wnt3a]-O-(9Z)-hexadec-9-enoyl-L-serine
-
-
-
-
?
(9Z)-hexadec-9-enoyl-CoA + [Wnt3a]-L-serine
CoA + [Wnt3a]-O-(9Z)-hexadec-9-enoyl-L-serine
-
chicken substrate, and substrate from Mus musculus
-
-
?
(9Z)-hexadec-9-enoyl-CoA + [Wnt3a]-L-serine
CoA + [Wnt3a]-O-(9Z)-hexadec-9-enoyl-L-serine
-
-
-
?
(9Z)-hexadec-9-enoyl-CoA + [Wnt3a]-L-serine
CoA + [Wnt3a]-O-(9Z)-hexadec-9-enoyl-L-serine
the enzyme catalyzes the palmitoylation of the serine corresponding to Ser209 of Wnt3a
-
-
?
(9Z)-hexadec-9-enoyl-CoA + [Wnt3a]-L-serine
CoA + [Wnt3a]-O-(9Z)-hexadec-9-enoyl-L-serine
Wnt3a is palmitoylated in the endoplasmic reticulum and targeted to exosomes, palmitoylated Wnt3a proteins are found throughout the cytosol and at the plasma membrane but not in the nucleus, overview
-
-
?
(9Z)-hexadec-9-enoyl-CoA + [Wnt3a]-L-serine
CoA + [Wnt3a]-O-(9Z)-hexadec-9-enoyl-L-serine
chicken substrate, and substrate from Mus musculus
-
-
?
(9Z)-hexadec-9-enoyl-CoA + [Wnt3a]-L-serine
CoA + [Wnt3a]-O-(9Z)-hexadec-9-enoyl-L-serine
Wnt3a is palmitoylated by fatty acids 13-16 carbons in length at Ser209 but not at Cys77, consistent with a slow turnover rate, glycosylation is not required for Wnt3a palmitoylation, which is necessary but not sufficient for Wnt3a secretion
-
-
?
(9Z)-hexadec-9-enoyl-CoA + [Wnt3a]-L-serine
CoA + [Wnt3a]-O-(9Z)-hexadec-9-enoyl-L-serine
-
-
-
?
(9Z)-hexadec-9-enoyl-CoA + [Wnt3a]-L-serine
CoA + [Wnt3a]-O-(9Z)-hexadec-9-enoyl-L-serine
-
the enzyme catalyzes the palmitoylation of Ser209 and Cys77 of Wnt3a
-
-
?
(9Z)-hexadec-9-enoyl-CoA + [Wnt3a]-L-serine
CoA + [Wnt3a]-O-(9Z)-hexadec-9-enoyl-L-serine
-
the enzyme catalyzes the palmitoylation of Ser209 and Cys77 of Wnt3a expressed in L cells
-
-
?
(9Z)-hexadec-9-enoyl-CoA + [Wnt3a]-L-serine
CoA + [Wnt3a]-O-(9Z)-hexadec-9-enoyl-L-serine
the enzyme catalyzes the palmitoylation of the serine corresponding to Ser209 of Wnt3a
-
-
?
(9Z)-hexadec-9-enoyl-CoA + [Wnt3a]-L-serine
CoA + [Wnt3a]-O-(9Z)-hexadec-9-enoyl-L-serine
Wnt3a is palmitoylated in the endoplasmic reticulum and targeted to exosomes, palmitoylated Wnt3a proteins are found throughout the cytosol and at the plasma membrane but not in the nucleus, overview
-
-
?
(9Z)-hexadec-9-enoyl-CoA + [Wnt3a]-L-serine
CoA + [Wnt3a]-O-(9Z)-hexadec-9-enoyl-L-serine
chicken substrate, and substrate from Mus musculus
-
-
?
(9Z)-hexadec-9-enoyl-CoA + [Wnt3a]-L-serine
CoA + [Wnt3a]-O-(9Z)-hexadec-9-enoyl-L-serine
Wnt3a is palmitoylated by fatty acids 13-16 carbons in length at Ser209 but not at Cys77, consistent with a slow turnover rate, glycosylation is not required for Wnt3a palmitoylation, which is necessary but not sufficient for Wnt3a secretion
-
-
?
(9Z)-hexadec-9-enoyl-CoA + [Wnt5a]-L-serine
CoA + [Wnt5a]-O-(9Z)-hexadec-9-enoyl-L-serine
-
-
-
?
(9Z)-hexadec-9-enoyl-CoA + [Wnt5a]-L-serine
CoA + [Wnt5a]-O-(9Z)-hexadec-9-enoyl-L-serine
palmitoylation of Wnt-5a at Cys104
-
-
?
(9Z)-hexadec-9-enoyl-CoA + [WntWg]-L-serine
CoA + [WntWg]-O-(9Z)-hexadec-9-enoyl-L-serine
the enzyme catalyzes the palmitoylation of Wnt Wingless or Wg
-
-
?
(9Z)-hexadec-9-enoyl-CoA + [WntWg]-L-serine
CoA + [WntWg]-O-(9Z)-hexadec-9-enoyl-L-serine
the enzyme catalyzes the palmitoylation of Wnt Wingless or Wg. The enzyme binds the N-terminal 24-amino acid domain (residues 83-106) of Wg
-
-
?
(9Z)-hexadec-9-enoyl-CoA + [Wnt]-L-serine
CoA + [Wnt]-O-(9Z)-hexadec-9-enoyl-L-serine
-
-
-
?
(9Z)-hexadec-9-enoyl-CoA + [Wnt]-L-serine
CoA + [Wnt]-O-(9Z)-hexadec-9-enoyl-L-serine
-
-
-
?
(9Z)-hexadec-9-enoyl-CoA + [Wnt]-L-serine
CoA + [Wnt]-O-(9Z)-hexadec-9-enoyl-L-serine
-
-
-
?
(9Z)-hexadec-9-enoyl-CoA + [Wnt]-L-serine
CoA + [Wnt]-O-(9Z)-hexadec-9-enoyl-L-serine
the enzyme catalyzes posttranslational modification of Wnts with palmitoleic acid. PORCN is necessary and sufficient for Wnt acylation. PORCN intimately recognizes the local structure of Wnt around the site of acylation
-
-
?
(9Z)-hexadec-9-enoyl-CoA + [Wnt]-L-serine
CoA + [Wnt]-O-(9Z)-hexadec-9-enoyl-L-serine
there is an increase in the catalytic activity from hexanoyl-CoA to decanoyl-CoA, after which there is an abrupt drop for dodecanoyl-CoA. Upon further increase in fatty acyl chain length, the activity stays at approximately the same level until the unsaturated palmitoleoyl-CoA, which is the best substrate
-
-
?
(9Z)-hexadec-9-enoyl-CoA + [Wnt]-L-serine
CoA + [Wnt]-O-(9Z)-hexadec-9-enoyl-L-serine
-
-
-
?
(9Z)-hexadec-9-enoyl-CoA + [Wnt]-L-serine
CoA + [Wnt]-O-(9Z)-hexadec-9-enoyl-L-serine
the enzyme is an essential mediators of Wnt secretion and signaling
-
-
?
(9Z)-hexadec-9-enoyl-CoA + [Wnt]-L-serine
CoA + [Wnt]-O-(9Z)-hexadec-9-enoyl-L-serine
-
-
-
?
additional information
?
-
-
enzyme Porc functions on the N-terminal 24-amino acid domain (83-106) of Wg, binding of Porc with Wg is essential for its activity
-
-
?
additional information
?
-
enzyme Porc functions on the N-terminal 24-amino acid domain (83-106) of Wg, binding of Porc with Wg is essential for its activity
-
-
?
additional information
?
-
-
recombinant c-Myc-tagged substrate Wg mutants T51A, S105A, S110A, and T416A
-
-
?
additional information
?
-
recombinant c-Myc-tagged substrate Wg mutants T51A, S105A, S110A, and T416A
-
-
?
additional information
?
-
-
vertebrate Wnt1 and Wnt3a possess at least one additional site for porcupine-mediated lipid-modification, localization of Wnt proteins in the chick neural tube, overview
-
-
?
additional information
?
-
PORCN splice variants differ globally in signaling activity
-
-
?
additional information
?
-
generation of a fusion protein that is palmitoylated in a PORCN-dependent manner, overview
-
-
?
additional information
?
-
no activity with palmitoylation-defective Wnt3aS209A mutant
-
-
?
additional information
?
-
-
no activity with palmitoylation-defective Wnt3aS209A mutant
-
-
?
additional information
?
-
vertebrate Wnt1 and Wnt3a possess at least one additional site for porcupine-mediated lipid-modification
-
-
?
additional information
?
-
-
vertebrate Wnt1 and Wnt3a possess at least one additional site for porcupine-mediated lipid-modification
-
-
?
additional information
?
-
no activity with palmitoylation-defective Wnt3aS209A mutant
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(9Z)-hexadec-9-enoyl-CoA + [Wnt3]-L-serine
CoA + [Wnt3]-O-(9Z)-hexadec-9-enoyl-L-serine
-
-
-
?
(9Z)-hexadec-9-enoyl-CoA + [Wnt5a]-L-serine
CoA + [Wnt5a]-O-(9Z)-hexadec-9-enoyl-L-serine
-
-
-
?
(9Z)-hexadec-9-enoyl-CoA + [Wnt5]-L-serine
CoA + [Wnt5]-O-(9Z)-hexadec-9-enoyl-L-serine
-
-
-
?
(9Z)-hexadec-9-enoyl-CoA + [WntWg]-L-serine
CoA + [WntWg]-O-(9Z)-hexadec-9-enoyl-L-serine
the enzyme catalyzes the palmitoylation of Wnt Wingless or Wg
-
-
?
(9Z)-hexadec-9-enoyl-CoA + [Wnt1]-L-serine
CoA + [Wnt1]-O-(9Z)-hexadec-9-enoyl-L-serine
-
-
-
-
?
(9Z)-hexadec-9-enoyl-CoA + [Wnt1]-L-serine
CoA + [Wnt1]-O-(9Z)-hexadec-9-enoyl-L-serine
-
-
-
?
(9Z)-hexadec-9-enoyl-CoA + [Wnt1]-L-serine
CoA + [Wnt1]-O-(9Z)-hexadec-9-enoyl-L-serine
-
-
-
?
(9Z)-hexadec-9-enoyl-CoA + [Wnt3a]-L-serine
CoA + [Wnt3a]-O-(9Z)-hexadec-9-enoyl-L-serine
-
the enzyme catalyzes the palmitoylation of Ser209 and Cys77 of Wnt3a
-
-
?
(9Z)-hexadec-9-enoyl-CoA + [Wnt3a]-L-serine
CoA + [Wnt3a]-O-(9Z)-hexadec-9-enoyl-L-serine
-
-
-
-
?
(9Z)-hexadec-9-enoyl-CoA + [Wnt3a]-L-serine
CoA + [Wnt3a]-O-(9Z)-hexadec-9-enoyl-L-serine
-
-
-
?
(9Z)-hexadec-9-enoyl-CoA + [Wnt3a]-L-serine
CoA + [Wnt3a]-O-(9Z)-hexadec-9-enoyl-L-serine
the enzyme catalyzes the palmitoylation of the serine corresponding to Ser209 of Wnt3a
-
-
?
(9Z)-hexadec-9-enoyl-CoA + [Wnt3a]-L-serine
CoA + [Wnt3a]-O-(9Z)-hexadec-9-enoyl-L-serine
Wnt3a is palmitoylated in the endoplasmic reticulum and targeted to exosomes, palmitoylated Wnt3a proteins are found throughout the cytosol and at the plasma membrane but not in the nucleus, overview
-
-
?
(9Z)-hexadec-9-enoyl-CoA + [Wnt3a]-L-serine
CoA + [Wnt3a]-O-(9Z)-hexadec-9-enoyl-L-serine
-
-
-
?
(9Z)-hexadec-9-enoyl-CoA + [Wnt3a]-L-serine
CoA + [Wnt3a]-O-(9Z)-hexadec-9-enoyl-L-serine
-
the enzyme catalyzes the palmitoylation of Ser209 and Cys77 of Wnt3a expressed in L cells
-
-
?
(9Z)-hexadec-9-enoyl-CoA + [Wnt3a]-L-serine
CoA + [Wnt3a]-O-(9Z)-hexadec-9-enoyl-L-serine
the enzyme catalyzes the palmitoylation of the serine corresponding to Ser209 of Wnt3a
-
-
?
(9Z)-hexadec-9-enoyl-CoA + [Wnt3a]-L-serine
CoA + [Wnt3a]-O-(9Z)-hexadec-9-enoyl-L-serine
Wnt3a is palmitoylated in the endoplasmic reticulum and targeted to exosomes, palmitoylated Wnt3a proteins are found throughout the cytosol and at the plasma membrane but not in the nucleus, overview
-
-
?
(9Z)-hexadec-9-enoyl-CoA + [Wnt]-L-serine
CoA + [Wnt]-O-(9Z)-hexadec-9-enoyl-L-serine
-
-
-
?
(9Z)-hexadec-9-enoyl-CoA + [Wnt]-L-serine
CoA + [Wnt]-O-(9Z)-hexadec-9-enoyl-L-serine
-
-
-
?
(9Z)-hexadec-9-enoyl-CoA + [Wnt]-L-serine
CoA + [Wnt]-O-(9Z)-hexadec-9-enoyl-L-serine
-
-
-
?
(9Z)-hexadec-9-enoyl-CoA + [Wnt]-L-serine
CoA + [Wnt]-O-(9Z)-hexadec-9-enoyl-L-serine
the enzyme catalyzes posttranslational modification of Wnts with palmitoleic acid. PORCN is necessary and sufficient for Wnt acylation. PORCN intimately recognizes the local structure of Wnt around the site of acylation
-
-
?
(9Z)-hexadec-9-enoyl-CoA + [Wnt]-L-serine
CoA + [Wnt]-O-(9Z)-hexadec-9-enoyl-L-serine
-
-
-
?
(9Z)-hexadec-9-enoyl-CoA + [Wnt]-L-serine
CoA + [Wnt]-O-(9Z)-hexadec-9-enoyl-L-serine
the enzyme is an essential mediators of Wnt secretion and signaling
-
-
?
(9Z)-hexadec-9-enoyl-CoA + [Wnt]-L-serine
CoA + [Wnt]-O-(9Z)-hexadec-9-enoyl-L-serine
-
-
-
?
additional information
?
-
-
enzyme Porc functions on the N-terminal 24-amino acid domain (83-106) of Wg, binding of Porc with Wg is essential for its activity
-
-
?
additional information
?
-
enzyme Porc functions on the N-terminal 24-amino acid domain (83-106) of Wg, binding of Porc with Wg is essential for its activity
-
-
?
additional information
?
-
PORCN splice variants differ globally in signaling activity
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-((3,6-dimethyl-4-oxo-3,4,6,7-tetrahydrothieno[3,2-d]pyrimidin-2-yl)thio)-N-(6-methylbenzo[d]thiazol-2-yl)acetamide
-
-
2-((3-(3-methoxyphenyl)-4-oxo-3,4,4a,6,7,7a-hexahydrothieno[3,2-d]pyrimidin-2-yl)thio)-N-(6-methylbenzo[d]thiazol-2-yl)acetamide
-
-
2-((3-(4-fluorophenyl)-4-oxo-3,4,4a,6,7,7a-hexahydrothieno[3,2-d]pyrimidin-2-yl)thio)-N-(6-methylbenzo[d]thiazol-2-yl)acetamide
-
-
2-((3-cyclopentyl-4-oxo-3,4-dihydroquinazolin-2-yl)thio)-N-(4-(dimethylamino)phenyl)acetamide
-
-
2-((4-oxo-3-phenyl-3,4,6,7-tetrahydrothieno[3,2-d]pyrimidin-2-yl)thio)-N-(4-(piperidin-1-yl)phenyl)acetamide
-
-
2-((4-oxo-3-phenyl-3,4,6,7-tetrahydrothieno[3,2-d]pyrimidin-2-yl)thio)-N-(4-phenylthiazol-2-yl)acetamide
-
-
2-((4-oxo-3-phenyl-3,4,6,7-tetrahydrothieno[3,2-d]pyrimidin-2-yl)thio)-N-(5-(prop-1-en-2-yl)pyridin-2-yl)acetamide
-
-
2-((4-oxo-3-phenyl-3,4,6,7-tetrahydrothieno[3,2-d]pyrimidin-2-yl)thio)-N-(5-phenylthiazol-2-yl)acetamide
-
-
2-(4-(2-methylpyridin-4-yl)phenyl)-N-(4-(pyridin-3-yl)phenyl)acetamide
i.e. C59
2-[(4-oxo-3-phenyl-3,4,6,7-tetrahydrothieno[3,2-d]pyrimidin-2-yl)sulfanyl]-N-(5-phenylpyridin-2-yl)acetamide
-
-
2-[(4-oxo-3-phenyl-3,4,6,7-tetrahydrothieno[3,2-d]pyrimidin-2-yl)sulfanyl]-N-(5-phenylpyrimidin-2-yl)acetamide
-
-
2-[(4-oxo-3-phenyl-3,4,6,7-tetrahydrothieno[3,2-d]pyrimidin-2-yl)sulfanyl]-N-(6-phenylpyridin-3-yl)acetamide
-
-
2-[(4-oxo-3-phenyl-3,4,6,7-tetrahydrothieno[3,2-d]pyrimidin-2-yl)sulfanyl]-N-[4-(pyridin-2-yl)phenyl]acetamide
-
-
2-[(4-oxo-3-phenyl-3,4,6,7-tetrahydrothieno[3,2-d]pyrimidin-2-yl)sulfanyl]-N-[4-(pyridin-3-yl)phenyl]acetamide
-
-
2-[(4-oxo-3-phenyl-3,4,6,7-tetrahydrothieno[3,2-d]pyrimidin-2-yl)sulfanyl]-N-[4-(pyridin-4-yl)phenyl]acetamide
-
-
2-[(4-oxo-3-phenyl-3,4,6,7-tetrahydrothieno[3,2-d]pyrimidin-2-yl)sulfanyl]-N-[5-(pyrimidin-5-yl)pyridin-2-yl]acetamide
-
-
2-[(4-oxo-3-phenyl-3,4,6,7-tetrahydrothieno[3,2-d]pyrimidin-2-yl)sulfanyl]-N-[5-(thiophen-2-yl)pyridin-2-yl]acetamide
-
-
2-[(4-oxo-3-phenyl-3,4,6,7-tetrahydrothieno[3,2-d]pyrimidin-2-yl)sulfanyl]-N-[5-(thiophen-3-yl)pyridin-2-yl]acetamide
-
-
5-((3aR,4R,6aS)-6-(4-(2-((2-((6-methylbenzo[d]thiazol-2-yl)amino)-2-oxoethyl)thio)-4-oxo-4a,6,7,7a-tetrahydrothieno[3,2-d]pyrimidin-3(4H)-yl)phenethyl)-2-oxohexahydro-1H-thieno[3,4-d]imidazol-4-yl)pentanoic acid
-
-
6-oxo-N-(2-oxo-2-(thiazol-2-ylamino)ethyl)-1-phenyl-1,6-dihydropyridazine-3-carboxamide
-
-
ethyl 4-(2-((4-oxo-3-phenyl-3,4,6,7-tetrahydrothieno[3,2-d]pyrimidin-2-yl)thio)acetamido)benzoate
-
-
N-(2-((6-methoxybenzo[d]thiazol-2-yl)amino)-2-oxoethyl)-3-(4-methoxyphenyl)-4-oxo-3,4-dihydrophthalazine-1-carboxamide
-
-
N-(2-((6-methoxybenzo[d]thiazol-2-yl)amino)-2-oxoethyl)-6-oxo-1-phenyl-1,6-dihydropyridine-3-carboxamide
-
-
N-(3,3'-bipyridin-6-yl)-2-[(4-oxo-3-phenyl-3,4,6,7-tetrahydrothieno[3,2-d]pyrimidin-2-yl)sulfanyl]acetamide
-
-
N-(4-(dimethylamino)phenyl)-2-((4-oxo-3-phenyl-3,4,6,7-tetrahydrothieno[3,2-d]pyrimidin-2-yl)thio)acetamide
-
-
N-(4-butylphenyl)-2-((4-oxo-3-phenyl-3,4,6,7-tetrahydrothieno[3,2-d]pyrimidin-2-yl)thio)acetamide
-
-
N-(5-ethoxypyridin-2-yl)-2-((4-oxo-3-phenyl-3,4,6,7-tetrahydrothieno[3,2-d]pyrimidin-2-yl)thio)acetamide
-
-
N-(6-methoxyquinolin-2-yl)-2-((4-oxo-3-phenyl-3,4,6,7-tetrahydrothieno[3,2-d]pyrimidin-2-yl)thio)acetamide
-
-
N-(6-methylbenzo[d]thiazol-2-yl)-2-((4-oxo-3-phenyl-3,4,4a,6,7,7a-hexahydrothieno[3,2-d]pyrimidin-2-yl)thio)acetamide
-
-
N-(benzo[d]thiazol-2-yl)-2-((3-ethyl-6-methyl-4-oxo-3,4,6,7-tetrahydrothieno[3,2-d]pyrimidin-2-yl)thio)acetamide
-
-
N-(biphenyl-2-yl)-2-[(4-oxo-3-phenyl-3,4,6,7-tetrahydrothieno[3,2-d]pyrimidin-2-yl)sulfanyl]acetamide
-
-
N-(biphenyl-3-yl)-2-[(4-oxo-3-phenyl-3,4,6,7-tetrahydrothieno[3,2-d]pyrimidin-2-yl)sulfanyl]acetamide
-
-
N-([1,1'-biphenyl]-4-yl)-2-((4-oxo-3-phenyl-3,4,6,7-tetrahydrothieno[3,2-d]pyrimidin-2-yl)thio)acetamide
-
-
N-[5-(furan-2-yl)pyridin-2-yl]-2-[(4-oxo-3-phenyl-3,4,6,7-tetrahydrothieno[3,2-d]pyrimidin-2-yl)sulfanyl]acetamide
-
-
N-[5-(furan-2-yl)pyrimidin-2-yl]-2-[(4-oxo-3-phenyl-3,4,6,7-tetrahydrothieno[3,2-d]pyrimidin-2-yl)sulfanyl]acetamide
-
-
N-[5-(furan-3-yl)pyridin-2-yl]-2-[(4-oxo-3-phenyl-3,4,6,7-tetrahydrothieno[3,2-d]pyrimidin-2-yl)sulfanyl]acetamide
-
-
N-[5-(furan-3-yl)pyrimidin-2-yl]-2-[(4-oxo-3-phenyl-3,4,6,7-tetrahydrothieno[3,2-d]pyrimidin-2-yl)sulfanyl]acetamide
-
-
additional information
-
identification, synthesis, and analysis of small molecule enzyme IWP inhibitors, i.e. inhibitors of Wnt production, structure-activity relationship, overview
-
2-[5-methyl-6-(2-methylpyridin-4-yl)pyridin-3-yl]-N-(5-pyrazin-2-ylpyridin-2-yl)acetamide
i.e. LGK-974
2-[5-methyl-6-(2-methylpyridin-4-yl)pyridin-3-yl]-N-(5-pyrazin-2-ylpyridin-2-yl)acetamide
i.e. LGK-974. Directly inhibits PORCN-mediated Wnt acylation
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
glycosylation is not required for substrate Wnt3a palmitoylation, which is necessary but not sufficient for Wnt3a secretion
-
additional information
-
glycosylation is not required for substrate Wnt3a palmitoylation, which is necessary but not sufficient for Wnt3a secretion
-
additional information
substrate glycosylation promotes, but is not absolutely required for Wnt1 palmitoylation
-
additional information
glycosylation is not required for substrate Wnt3a palmitoylation, which is necessary but not sufficient for Wnt3a secretion
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
single gene and alternative splicing resulting in several variants
UniProt
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
additional information
Mporc mRNA is differentially expressed during embryogenesis and in various adult tissues, demonstrating that the alternative splicing is regulated to synthesize the specific types of Mporc, pattern of expression of Mporc at fetal and adult stages of development, overview
brenda
additional information
-
Mporc mRNA is differentially expressed during embryogenesis and in various adult tissues, demonstrating that the alternative splicing is regulated to synthesize the specific types of Mporc, pattern of expression of Mporc at fetal and adult stages of development, overview
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
endoplasmic reticulum-resident integral membrane enzyme
brenda
the enzyme has multiple transmembrane domains
brenda
a multispanning transmembrane protein
brenda
the enzyme has multiple transmembrane domains, Drosophila Porc is localized at the endoplasmic reticulum when expressed in Drosophila cells as an epitope-tagged protein
brenda
integral membrane protein, enzyme structure and topology model with cytoplasmic and endoplasmic reticulum luman parts, overview
brenda
the enzyme has multiple transmembrane domains
brenda
integral membrane protein, enzyme structure and topology model with cytoplasmic and endoplasmic reticulum luman parts, overview
brenda
the enzyme has multiple transmembrane domains
brenda
the enzyme has multiple transmembrane domains
brenda
additional information
palmitoylated Wnt3a proteins are found throughout the cytosol and at the plasma membrane but not in the nucleus
-
brenda
additional information
-
palmitoylated Wnt3a proteins are found throughout the cytosol and at the plasma membrane but not in the nucleus
-
brenda
additional information
the enzyme is predicted to palmitoylate Wnt either co-translationally or post-translationally, so that in either case, the catalytic site is likely to be in the membrane or in the lumen of the endoplasmic reticulum
-
brenda
additional information
palmitoylated Wnt3a proteins are found throughout the cytosol and at the plasma membrane but not in the nucleus
-
brenda
additional information
the enzyme is predicted to palmitoylate Wnt either co-translationally or post-translationally, so that in either case, the catalytic site is likely to be in the membrane or in the lumen of the endoplasmic reticulum
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
Drosophila Porc has an extra hydrophilic N-terminal sequence, which is not found in other Porc enzymes
evolution
-
the enzyme belongs to the family of membrane-bound O-acyltransferases (MBOAT), which transfer acyl groups, such as a palmitoyl group, to substrates
evolution
-
the enzyme belongs to the family of membrane-bound O-acyltransferases (MBOAT), which transfer acyl groups, such as a palmitoyl group, to substrates
evolution
the enzyme belongs to the membrane-bound O-acyltransferase family
evolution
the enzyme belongs to the membrane-bound O-acyltransferase family
evolution
the enzyme is a member of the membrane-bound O-acyl transferase (MBOAT) superfamily
evolution
-
the enzyme is a member of the membrane-bound O-acyltransferase family proteins
malfunction
-
compromised Porcn activity commonly results in developmental disorders including focal dermal hypoplasia (Goltz syndrome) whereas hyperactivity of Porcn is associated with cancerous cell growth. Enzyme inhibition by small molecule IWP inhibitors affect Wnt-dependent developmental processes including zebrafish posterior axis formation and kidney tubule formation
malfunction
enzyme mutation, with a 219-kb deletion in Xp11.23 in two affected females, causes focal dermal hypoplasia is an X-linked dominant disorder characterized by patchy hypoplastic skin and digital, ocular and dental malformations
malfunction
gene deletion causes embryonic lethality in mice. PORCN null cells cannot activate WNT3A, PORCN null cells do not secrete WNT3A
malfunction
mutations in gene PORCN are associated with focal dermal hypoplasia. PORCN null cells are completely incapable of autocrine Wnt signaling
malfunction
the catalytically inactive porcupine is able to act as an inhibitor of endogenous porcupine, possibly via direct competition for substrate
malfunction
-
treatment with a chemical inhibitor of acyltransferases produces defective intracellular trafficking of Wingless
malfunction
-
Wnt-3a with defective acylation is not transferred from the endoplasmic reticulum
metabolism
porcupine (PORCN) and Wntless (WLS) are essential mediators of Wnt secretion and signaling. PORCN and WLS form a complex. THes compete for binding to WNT1. Overexpression of PORCN promotes palmitoylation of WNT1
metabolism
the enzyme catalyzes posttranslational modification of Wnts with palmitoleic acid. This unique form of lipidation with palmitoleic acid is a vital step in the biogenesis and secretion of Wnt
physiological function
ectopic expression of porc stimulates the N-glycosylation of both endogenously and exogenously express