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Information on EC 2.3.1.225 - protein S-acyltransferase and Organism(s) Mus musculus and UniProt Accession Q8VDZ4

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EC Tree
     2 Transferases
         2.3 Acyltransferases
             2.3.1 Transferring groups other than aminoacyl groups
                2.3.1.225 protein S-acyltransferase
IUBMB Comments
The enzyme catalyses the posttranslational protein palmitoylation that plays a role in protein-membrane interactions, protein trafficking, and enzyme activity. Palmitoylation increases the hydrophobicity of proteins or protein domains and contributes to their membrane association.
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This record set is specific for:
Mus musculus
UNIPROT: Q8VDZ4
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Word Map
The taxonomic range for the selected organisms is: Mus musculus
The enzyme appears in selected viruses and cellular organisms
Synonyms
hip14, dhhc3, palmitoyl acyltransferase, dhhc5, zdhhc5, dhhc2, akr1p, zdhhc3, protein acyltransferase, dhhc protein, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
DHHC protein
-
DHHC protein acyltransferase
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
palmitoyl-CoA + [protein]-L-cysteine = [protein]-S-palmitoyl-L-cysteine + CoA
show the reaction diagram
two-step transfer mechanism, ping-pong kinetic mechanism
SYSTEMATIC NAME
IUBMB Comments
palmitoyl-CoA:[protein]-L-cysteine S-palmitoyltransferase
The enzyme catalyses the posttranslational protein palmitoylation that plays a role in protein-membrane interactions, protein trafficking, and enzyme activity. Palmitoylation increases the hydrophobicity of proteins or protein domains and contributes to their membrane association.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
palmitoyl-CoA + [phospholemman]-L-cysteine
[phospholemman]-S-palmitoyl-L-cysteine + CoA
show the reaction diagram
-
isoform DHHC5 palmitoylates cardiac phosphoprotein phospholemman at two juxtamembrane cysteines, C40 and C42. C40 is the principal palmitoylation site
-
?
palmitoyl-CoA + [N-myristoylated G-protein alphai1]-L-cysteine
[N-myristoylated G-protein alphai1]-S-palmitoyl-L-cysteine + CoA
show the reaction diagram
-
-
-
r
palmitoyl-CoA + [N-myristoylated Gly-Cys-Gly tripeptide]-L-cysteine
[N-myristoylated Gly-Cys-Gly tripeptide]-S-palmitoyl-L-cysteine + CoA
show the reaction diagram
peptide substrate si tagged via ethylenediamine with fluorescent NBD
-
-
r
palmitoyl-CoA + [protein]-L-cysteine
[protein]-S-palmitoyl-L-cysteine + CoA
show the reaction diagram
-
-
-
r
additional information
?
-
DHHC3 has a broad protein substrate specificity, but only myristoyl-, palmitoyl-, and palmioleoyl-CoA are effective, and longer acyl-CoAs compete less well. The acyl-CoA chain length specificity of DHHC enzyme autoacylation parallels substrate specificity, overview
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
palmitoyl-CoA + [protein]-L-cysteine
[protein]-S-palmitoyl-L-cysteine + CoA
show the reaction diagram
-
-
-
r
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Zinc
bound in the cysteine-rich domain. Treatment of isoform DHHC3 with chelating agents in vitro leads to specific structural perturbations and activity deficits also observed in conserved cysteine mutants. The stoichiometry of zinc binding is 2 mol of zinc/mol of DHHC3 protein
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0059
palmitoyl-CoA
pH 7.4, 25°C, recombinant DHHC3
0.0013
[N-myristoylated Gly-Cys-Gly tripeptide]-L-cysteine
pH 7.4, 25°C, recombinant DHHC3
additional information
additional information
Michaelis-Menten kinetics
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
expression in the hippocampal subfield CA3 and the dentate gyrus
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
localized to synaptic membranes
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
ZDHC5_MOUSE
715
4
77501
Swiss-Prot
Secretory Pathway (Reliability: 2)
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
isoform DHHC3 is palmitoylated at the cysteine residue in the DHHC motif
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C129S
mutation of highly conserved cysteine residue of the cysteine-rich domain, results in activity deficits and a structural perturbation. About 10% of wild-type activity
C132S
mutation of highly conserved cysteine residue of the cysteine-rich domain, results in activity deficits and a structural perturbation. Less than 5% of wild-type activity
C133S
mutation of unconserved cysteine residue of the cysteine-rich domain. About 90% of wild-type activity
C146S
mutation of highly conserved cysteine residue of the cysteine-rich domain, results in activity deficits and a structural perturbation. About 15% of wild-type activity. Mutation reduces the palmitoylation level of DHHC3
C157
mutation reduces the palmitoylation level of DHHC3
C157S
site-directed mutagenesis, inactive mutant
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant FLAG- and His6-tagged wild-type and C157S mutant DHHC3 from Sf9 cells by nickel and FLAG affinity chromatography to near homogeneity
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of FLAG- and His6-tagged wild-type and C157S mutant DHHC3 in Spodopterafrugiperda Sf9 cells using the baculovirus transfection system
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Li, Y.; Hu, J.; Hoefer, K.; Wong, A.M.; Cooper, J.D.; Birnbaum, S.G.; Hammer, R.E.; Hofmann, S.L.
DHHC5 interacts with PDZ domain 3 of post-synaptic density-95 (PSD-95) protein and plays a role in learning and memory
J. Biol. Chem.
285
13022-13031
2010
Mus musculus (Q8VDZ4)
Manually annotated by BRENDA team
Jennings, B. C.; Linder, M. E.
DHHC protein S-acyltransferases use similar ping-pong kinetic mechanisms but display different acyl-CoA specificities
J. Biol. Chem.
287
7236-7245
2012
Homo sapiens, Mus musculus (Q8R173)
Manually annotated by BRENDA team
Gottlieb, C.D.; Zhang, S.; Linder, M.E.
The cysteine-rich domain of the DHHC3 palmitoyltransferase is palmitoylated and contains tightly bound zinc
J. Biol. Chem.
290
29259-29269
2015
Mus musculus (Q8R173)
Manually annotated by BRENDA team
Howie, J.; Reilly, L.; Fraser, N.J.; Vlachaki Walker, J.M.; Wypijewski, K.J.; Ashford, M.L.; Calaghan, S.C.; McClafferty, H.; Tian, L.; Shipston, M.J.; Boguslavskyi, A.; Shattock, M.J.; Fuller, W.
Substrate recognition by the cell surface palmitoyl transferase DHHC5
Proc. Natl. Acad. Sci. USA
111
17534-17539
2014
Rattus norvegicus (Q2THW7), Mus musculus (Q8VDZ4)
Manually annotated by BRENDA team