The cysteine-rich domain of the DHHC3 palmitoyltransferase is palmitoylated and contains tightly bound zinc

Journal of Biological Chemistry

Volumn 290, Issue 49, 2015, Pages 29259-29269

  Gottlieb, Colin D ^a   Zhang, Sheng ^a   Linder, Maurine E ^a  

^a Cornell University ^*  (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; BINS; CHELATION; CYTOLOGY; ENZYMES; FATTY ACIDS; MAMMALS; MASS SPECTROMETRY; METAL IONS; METALS; PROTEINS; ZINC;

CATALYTIC MECHANISMS; CYSTEINE-RICH DOMAINS; CYTOPLASMIC LEAFLET; DHHC PROTEIN FAMILIES; FLUORESCENT INDICATORS; PALMITOYLATED CYSTEINE; PALMITOYLTRANSFERASE; STRUCTURAL PERTURBATION;

PALMITIC ACID;

CHELATING AGENT; DHHC3 PALMITOYLTRANSFERASE; PALMITIC ACID; TRANSFERASE; UNCLASSIFIED DRUG; ZINC; BIOTIN; CYSTEINE; GODZ PROTEIN, MOUSE; IODOACETAMIDE; ION; LYSINE; MEMBRANE PROTEIN; METAL; PROTEIN BINDING;

ACYLATION; AMINO ACID SUBSTITUTION; AMINO TERMINAL SEQUENCE; ARTICLE; AUTOACYLATION; BINDING KINETICS; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; CYSTEINE RICH DOMAIN; ENZYME ACTIVITY; ENZYME CONFORMATION; ENZYME STRUCTURE; ENZYME SUBSTRATE COMPLEX; FEASIBILITY STUDY; IN VITRO STUDY; METAL ION BINDING; MOLECULAR DYNAMICS; MOLECULAR INTERACTION; PALMITOYLATION; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN MOTIF; STOICHIOMETRY; STRUCTURE ACTIVITY RELATION; STRUCTURE ANALYSIS; TANDEM MASS SPECTROMETRY; ANIMAL; CHEMISTRY; ENZYME ACTIVE SITE; LIPOYLATION; MASS SPECTROMETRY; METABOLISM; MOUSE; MUTATION; PROTEIN PROCESSING; SF9 CELL LINE; SPODOPTERA;

AMINO ACID MOTIFS; ANIMALS; BIOTIN; CATALYTIC DOMAIN; CHELATING AGENTS; CYSTEINE; IODOACETAMIDE; IONS; LIPOYLATION; LYSINE; MASS SPECTROMETRY; MEMBRANE PROTEINS; METALS; MICE; MUTATION; PROTEIN BINDING; PROTEIN PROCESSING, POST-TRANSLATIONAL; SF9 CELLS; SPODOPTERA; ZINC;

EID: 84949008123     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M115.691147     Document Type: Article

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