| http://dbpedia.org/ontology/abstract
|
Acyl-protein thioesterases are enzymes tha … 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.le to hydrolyze oxygen-linked ester bonds.
|
| http://dbpedia.org/ontology/ecNumber
|
3.1.2.-
|
| http://dbpedia.org/ontology/hgncid
|
6737
, 6738
|
| http://dbpedia.org/ontology/omim
|
616143
, 605599
|
| http://dbpedia.org/ontology/pdb
|
5SYN
, 5SYM
|
| http://dbpedia.org/ontology/refseq
|
NP_001266285.1
, NC_000001.11
|
| http://dbpedia.org/ontology/symbol
|
LYPA2
, Acyl-protein thioesterases (APTs)
, LYPA1
, APT1
, APT2
|
| http://dbpedia.org/ontology/thumbnail
|
http://commons.wikimedia.org/wiki/Special:FilePath/HAPT1_dimer.png?width=300 +
|
| http://dbpedia.org/ontology/uniprot
|
O75608
, O95372
|
| http://dbpedia.org/ontology/wikiPageExternalLink
|
https://creativecommons.org/licenses/by/4.0/ +
, http://www.rcsb.org/pdb/explore/explore.do%3FstructureId=1FJ2 +
|
| http://dbpedia.org/ontology/wikiPageID
|
56635131
|
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|
14484
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|
1039445793
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|
http://dbpedia.org/resource/Sulfur +
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, http://dbpedia.org/resource/Category:Cell_biology +
, http://dbpedia.org/resource/Proteomics +
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, http://dbpedia.org/resource/Catalytic_triad +
, http://dbpedia.org/resource/File:APT_tunnel.png +
, http://dbpedia.org/resource/Ester +
, http://dbpedia.org/resource/Endomembrane_system +
, http://dbpedia.org/resource/Hydrolysis +
, http://dbpedia.org/resource/Oncogene +
, http://dbpedia.org/resource/Cysteine +
, http://dbpedia.org/resource/LYPLA2 +
, http://dbpedia.org/resource/Ion_channel +
, http://dbpedia.org/resource/Ras_subfamily +
, http://dbpedia.org/resource/Protein_secondary_structure +
, http://dbpedia.org/resource/Thioester +
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, http://dbpedia.org/resource/Alpha/beta_hydrolase_superfamily +
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, http://dbpedia.org/resource/Substrate_%28chemistry%29 +
, http://dbpedia.org/resource/Chemical_affinity +
, http://dbpedia.org/resource/Conserved_sequence +
, http://dbpedia.org/resource/Enzyme +
, http://dbpedia.org/resource/Enzyme_inhibitor +
, http://dbpedia.org/resource/Acyl-protein_thioesterase_1 +
, http://dbpedia.org/resource/Acyl-protein_thioesterase_2 +
, http://dbpedia.org/resource/Protein_structure +
, http://dbpedia.org/resource/Cancer +
, http://dbpedia.org/resource/ABHD17 +
, http://dbpedia.org/resource/File:APT_mechanism_and_product_release.png +
, http://dbpedia.org/resource/LYPA1 +
, http://dbpedia.org/resource/LYPA2 +
, http://dbpedia.org/resource/Gap-43_protein +
, http://dbpedia.org/resource/Cell_membrane +
, http://dbpedia.org/resource/Palmitoylation +
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, http://dbpedia.org/resource/Hydrophobic_effect +
, http://dbpedia.org/resource/Oxygen +
, http://dbpedia.org/resource/Category:Post-translational_modification +
|
| http://dbpedia.org/property/altsymbols
|
APT1
, APT2
|
| http://dbpedia.org/property/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.
|
| http://dbpedia.org/property/ecnumber
|
3.1
|
| http://dbpedia.org/property/hgncid
|
6738
, 6737
|
| http://dbpedia.org/property/interpro
|
IPR029058
|
| http://dbpedia.org/property/name
|
http://dbpedia.org/resource/Acyl-protein_thioesterase_1 +
, http://dbpedia.org/resource/Acyl-protein_thioesterase_2 +
|
| http://dbpedia.org/property/omim
|
616143
, 605599
|
| http://dbpedia.org/property/pdb
|
5
|
| http://dbpedia.org/property/pfam
|
PF02230
|
| http://dbpedia.org/property/refseq
|
NP_001266285.1
, NC_000001.11
|
| http://dbpedia.org/property/symbol
|
http://dbpedia.org/resource/LYPA1 +
, http://dbpedia.org/resource/LYPA2 +
, Acyl-protein thioesterases
|
| http://dbpedia.org/property/uniprot
|
O75608
, O95372
|
| http://dbpedia.org/property/wikiPageUsesTemplate
|
http://dbpedia.org/resource/Template:Infobox_protein +
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, http://dbpedia.org/resource/Template:Infobox_protein_family +
|
| http://purl.org/dc/terms/subject
|
http://dbpedia.org/resource/Category:Peripheral_membrane_proteins +
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, http://dbpedia.org/resource/Category:Lysophospholipases +
, http://dbpedia.org/resource/Category:Cell_biology +
|
| http://www.w3.org/ns/prov#wasDerivedFrom
|
http://en.wikipedia.org/wiki/Acyl-protein_thioesterase?oldid=1039445793&ns=0 +
|
| http://xmlns.com/foaf/0.1/depiction
|
http://commons.wikimedia.org/wiki/Special:FilePath/HAPT1_dimer.png +
, http://commons.wikimedia.org/wiki/Special:FilePath/APT_mechanism_and_product_release.png +
, http://commons.wikimedia.org/wiki/Special:FilePath/APT_tunnel.png +
|
| http://xmlns.com/foaf/0.1/isPrimaryTopicOf
|
http://en.wikipedia.org/wiki/Acyl-protein_thioesterase +
|
| http://xmlns.com/foaf/0.1/name
|
Acyl-protein thioesterase 1
, Acyl-protein thioesterase 2
|
| owl:sameAs |
http://dbpedia.org/resource/Acyl-protein_thioesterase +
, http://www.wikidata.org/entity/Q55603179 +
, https://global.dbpedia.org/id/5aeqE +
|
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http://www.wikidata.org/entity/Q8054 +
, http://dbpedia.org/ontology/Biomolecule +
, http://dbpedia.org/ontology/Protein +
, http://www.wikidata.org/entity/Q206229 +
|
| rdfs:comment |
Acyl-protein thioesterases are enzymes tha … 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.le to hydrolyze oxygen-linked ester bonds.
|
| rdfs:label |
Acyl-protein thioesterase
|
