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2.3.1.225: protein S-acyltransferase

This is an abbreviated version!
For detailed information about protein S-acyltransferase, go to the full flat file.

Word Map on EC 2.3.1.225

Reaction

palmitoyl-CoA
+
[protein]-L-cysteine
=
[protein]-S-palmitoyl-L-cysteine
+
CoA

Synonyms

Akr1, Akr1p, APT1, Asp-His-His-Cys motif palmitoyl transferase, At3g51390, DHHC palmitoyl transferase, DHHC protein, DHHC protein acyltransferase, DHHC-2, DHHC-21, DHHC-21 palmitoyl transferase, DHHC-3, DHHC-3 palmitoyl transferase, DHHC-7, DHHC-8, DHHC-CRD S-acyltransferase, DHHC16, DHHC17, DHHC2, DHHC3, DHHC4, DHHC5, Erf2, Erf2p, G-protein palmitoyltransferase, HIP14, palmitoyl acyltransferase, Pat, PAT10, PAT14, PAT15, PAT21, PAT24, PAT4, Pfa3, Pfa4, PFA5, protein acyl transferase, protein acyltransferase, protein S-acyl transferase 4, Ras PAT, S-protein acyltransferase, SEC18p, Swf1, ZDHHC3, ZDHHC5

ECTree

     2 Transferases
         2.3 Acyltransferases
             2.3.1 Transferring groups other than aminoacyl groups
                2.3.1.225 protein S-acyltransferase

Engineering

Engineering on EC 2.3.1.225 - protein S-acyltransferase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C157S
mutation in DHHC motif, mutant is not able to complement a yeast akr1 mutant strain
C192A
mutation in the DHHC motif, loss of autoacylation capacity and the ability to complement a yeast akr1 mutant
C159S
the DHHC15 mutant shows reduced activity compared to the wild-type
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
C164R
substitution of the conserved cysteine in the DHHC motif. Overexpression of this mutant allows to partially complement an isoform Swf1 gene deletion and to acylate the Swf1 substrates Tlg1, Syn8, and Snc1. Mutant protein is not acylated
H162Q
substitution in the DHHC motif, mutant is partially active
H162Q/C164R
substitutions in the DHHC motif, mutant is inactive
additional information