About: Acyl-protein thioesterase

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Acyl-protein thioesterases are enzymes that cleave off lipid modifications on proteins, located on the sulfur atom of cysteine residues linked via a thioester bond. Acyl-protein thioesterases are part of the α/β hydrolase superfamily of proteins and have a conserved catalytic triad. For that reason, acyl-protein thioesterases are also able to hydrolyze oxygen-linked ester bonds.

Attributes	Values
rdf:type	Thing Biomolecule Biomolecule Protein protein
rdfs:label	Acyl-protein thioesterase (en)
rdfs:comment	Acyl-protein thioesterases are enzymes that cleave off lipid modifications on proteins, located on the sulfur atom of cysteine residues linked via a thioester bond. Acyl-protein thioesterases are part of the α/β hydrolase superfamily of proteins and have a conserved catalytic triad. For that reason, acyl-protein thioesterases are also able to hydrolyze oxygen-linked ester bonds. (en)
foaf:name	Acyl-protein thioesterase 1 (en) Acyl-protein thioesterase 2 (en)
name	dbr:Acyl-protein_thioesterase_1 dbr:Acyl-protein_thioesterase_2
foaf:depiction
dcterms:subject	Cell biology Post-translational modification Lysophospholipases Peripheral membrane proteins
Wikipage page ID	56635131 (xsd:integer)
Wikipage revision ID	1039445793 (xsd:integer)
Link from a Wikipage to another Wikipage	Cancer Catalytic triad Protein secondary structure Endomembrane system Enzyme inhibitor Enzyme kinetics Proteomics Cell biology Post-translational modification Chemical affinity Ester Thioester Enzyme Conserved sequence LYPLA1 Substrate (chemistry) PPT1 Palmitoyl protein thioesterase Post-translational modification Protein structure Microinjection Active site Lysophospholipases G alpha subunit Gap-43 protein Ion channel Lipid-anchored protein Peripheral membrane proteins Cysteine Alpha/beta hydrolase superfamily Oxygen Cell membrane Golgi apparatus Ras subfamily Hydrolysis Hydrophobic effect Biological target Sulfur Sequence homology Oncogene Palmitoylation dbr:Acyl-protein_thioesterase_1 dbr:Acyl-protein_thioesterase_2 dbr:LYPA1 dbr:LYPA2 dbr:LYPLA2 dbr:ABHD17
Link from a Wikipage to an external page	http://www.rcsb.org/pdb/explore/explore.do%3FstructureId=1FJ2 https://creativecommons.org/licenses/by/4.0/
sameAs	Acyl-protein thioesterase Acyl-protein thioesterase
dbp:wikiPageUsesTemplate	dbt:Infobox_protein_family dbt:Reflist dbt:Infobox_protein
thumbnail	wiki-commons:Special:FilePath/HAPT1_dimer.png?width=300
OMIM	605599 (xsd:integer) 616143 (xsd:integer)
AltSymbols	APT1 (en) APT2 (en)
caption	Crystal structure of human APT1, PDB code 1fj2. Alpha helices are in red, beta strands in gold, catalytic site residues in black. The 2 different monomers of the dimer are shaded in green and brown. (en)
ECnumber	3.100000 (xsd:double)
InterPro	IPR029058 (en)
Pfam	PF02230 (en)
symbol	dbr:LYPA1 dbr:LYPA2 Acyl-protein thioesterases (en)
UniProt	O75608 (en) O95372 (en)
has abstract	Acyl-protein thioesterases are enzymes that cleave off lipid modifications on proteins, located on the sulfur atom of cysteine residues linked via a thioester bond. Acyl-protein thioesterases are part of the α/β hydrolase superfamily of proteins and have a conserved catalytic triad. For that reason, acyl-protein thioesterases are also able to hydrolyze oxygen-linked ester bonds. (en)
HGNCid	6737 (xsd:integer) 6738 (xsd:integer)
PDB	5 (xsd:integer)
RefSeq	NC_000001.11 (en) NP_001266285.1 (en)
HGNCid	6737 6738
PDB ID	5SYM 5SYN

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