Literature summary for 2.3.1.225 extracted from

Gottlieb, C.D.; Zhang, S.; Linder, M.E.
The cysteine-rich domain of the DHHC3 palmitoyltransferase is palmitoylated and contains tightly bound zinc (2015), J. Biol. Chem., 290, 29259-29269.

Search for more literature for 2.3.1.225

Protein Variants

Protein Variants	Comment	Organism
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	Mus musculus
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	Mus musculus
C133S	mutation of unconserved cysteine residue of the cysteine-rich domain. About 90% of wild-type activity	Mus musculus
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	Mus musculus
C157	mutation reduces the palmitoylation level of DHHC3	Mus musculus

Metals/Ions

Metals/Ions	Comment	Organism	Structure
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	Mus musculus

Organism

Organism	UniProt	Comment	Textmining
Mus musculus	Q8R173	-	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
additional information	isoform DHHC3 is palmitoylated at the cysteine residue in the DHHC motif	Mus musculus

Synonyms

Synonyms	Comment	Organism
DHHC3	-	Mus musculus

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Release 2023.1 (January 2023)