Palmitoyl protein hydrolase/thioesterases is an enzyme (EC 3.1.2.22) that removes thioester-linked fatty acyl groups such as palmitate from modified cysteine residues in proteins or peptides during lysosomal degradation. It catalyzes the reaction
Palmitoyl protein thioesterase
Palmitoyl protein thioesterase 1. Red plane shows hydrocarbon boundary of the lipid bilayer
This enzyme belongs to the family of hydrolases, specifically those acting on thioester bonds. The systematic name is palmitoyl[protein] hydrolase. Other names in common use include palmitoyl-protein thioesterase, and palmitoyl-(protein) hydrolase. This enzyme participates in fatty acid elongation in mitochondria.
Neuronal ceroid lipofuscinoses (NCL) represent a group of encephalopathies that occur in 1 in 12,500 children. Mutations in the palmitoyl protein thioesterase gene causing infantile neuronal ceroid lipofuscinosis.[1] The most common mutation results in intracellular accumulation of the polypeptide and undetectable enzyme activity in the brain. Direct sequencing of cDNAs derived from brain RNA of INCL patients has shown a mis-sense transversion of A to T at nucleotide position 364, which results in substitution of Trp for Arg at position 122 in the protein - Arg 122 is immediately adjacent to a lipase consensus sequence that contains the putative active site Ser of PPT. The occurrence of this and two other independent mutations in the PPT gene strongly suggests that defects in this gene cause INCL.
^Hofmann SL, Vesa J, Hellsten E, Verkruyse LA, Camp LA, Rapola J, Santavuori P, Peltonen L (1995). "Mutations in the palmitoyl protein thioesterase gene causing infantile neuronal ceroid lipofuscinosis". Nature. 376 (6541): 584–587. Bibcode:1995Natur.376..584V. doi:10.1038/376584a0. PMID 7637805. S2CID 4322423.
Further readingedit
Camp LA, Hofmann SL (1995). "Assay and isolation of palmitoyl-protein thioesterase from bovine brain using palmitoylated H-Ras as substrate". Lipid Modifications of Proteins. Methods in Enzymology. Vol. 250. pp. 336–47. doi:10.1016/0076-6879(95)50083-9. ISBN978-0-12-182151-7. PMID 7651163.
Schriner JE, Yi W, Hofmann SL (1996). "cDNA and genomic cloning of human palmitoyl-protein thioesterase (PPT), the enzyme defective in infantile neuronal ceroid lipofuscinosis". Genomics. 34 (3): 317–22. doi:10.1006/geno.1996.0292. PMID 8786130.
Verkruyse LA, Hofmann SL (1996). "Lysosomal targeting of palmitoyl-protein thioesterase". J. Biol. Chem. 271 (26): 15831–6. doi:10.1074/jbc.271.26.15831. PMID 8663305.
palmitoyl, protein, hydrolase, palmitoyl, protein, hydrolase, thioesterases, enzyme, that, removes, thioester, linked, fatty, acyl, groups, such, palmitate, from, modified, cysteine, residues, proteins, peptides, during, lysosomal, degradation, catalyzes, reac. Palmitoyl protein hydrolase thioesterases is an enzyme EC 3 1 2 22 that removes thioester linked fatty acyl groups such as palmitate from modified cysteine residues in proteins or peptides during lysosomal degradation It catalyzes the reactionPalmitoyl protein thioesterasePalmitoyl protein thioesterase 1 Red plane shows hydrocarbon boundary of the lipid bilayerIdentifiersSymbolPalm thioestPfamPF02089Pfam clanCL0028InterProIPR002472SCOP21exw SCOPe SUPFAMOPM superfamily127OPM protein1eh5Available protein structures Pfam structures ECOD PDBRCSB PDB PDBe PDBjPDBsumstructure summarypalmitoyl protein hydrolaseIdentifiersEC no 3 1 2 22CAS no 150605 49 5DatabasesIntEnzIntEnz viewBRENDABRENDA entryExPASyNiceZyme viewKEGGKEGG entryMetaCycmetabolic pathwayPRIAMprofilePDB structuresRCSB PDB PDBe PDBsumGene OntologyAmiGO QuickGOSearchPMCarticlesPubMedarticlesNCBIproteins palmitoyl protein H2O displaystyle rightleftharpoons palmitate proteinThis enzyme belongs to the family of hydrolases specifically those acting on thioester bonds The systematic name is palmitoyl protein hydrolase Other names in common use include palmitoyl protein thioesterase and palmitoyl protein hydrolase This enzyme participates in fatty acid elongation in mitochondria Neuronal ceroid lipofuscinoses NCL represent a group of encephalopathies that occur in 1 in 12 500 children Mutations in the palmitoyl protein thioesterase gene causing infantile neuronal ceroid lipofuscinosis 1 The most common mutation results in intracellular accumulation of the polypeptide and undetectable enzyme activity in the brain Direct sequencing of cDNAs derived from brain RNA of INCL patients has shown a mis sense transversion of A to T at nucleotide position 364 which results in substitution of Trp for Arg at position 122 in the protein Arg 122 is immediately adjacent to a lipase consensus sequence that contains the putative active site Ser of PPT The occurrence of this and two other independent mutations in the PPT gene strongly suggests that defects in this gene cause INCL Contents 1 Examples 2 Structural studies 3 See also 4 References 5 Further reading 6 External linksExamples editHuman proteins containing this domain include palmitoyl protein thioesterase 1IdentifiersSymbolPPT1Alt symbolsPPTNCBI gene5538HGNC9325OMIM600722RefSeqNM 000310UniProtP50897Other dataEC number3 1 2 22LocusChr 1 p32Search forStructuresSwiss modelDomainsInterPro palmitoyl protein thioesterase 2IdentifiersSymbolPPT2Alt symbolsG14NCBI gene9374HGNC9326OMIM603298RefSeqNM 138717UniProtQ9UMR5Other dataEC number3 1 2 22LocusChr 6 p21 3Search forStructuresSwiss modelDomainsInterProStructural studies editAs of late 2007 4 structures have been solved for this class of enzymes with PDB accession codes 1EH5 1EI9 1EXW and 1PJA See also editpalmitoyl Acyl protein thioesterasesReferences edit Hofmann SL Vesa J Hellsten E Verkruyse LA Camp LA Rapola J Santavuori P Peltonen L 1995 Mutations in the palmitoyl protein thioesterase gene causing infantile neuronal ceroid lipofuscinosis Nature 376 6541 584 587 Bibcode 1995Natur 376 584V doi 10 1038 376584a0 PMID 7637805 S2CID 4322423 Further reading editCamp LA Hofmann SL 1995 Assay and isolation of palmitoyl protein thioesterase from bovine brain using palmitoylated H Ras as substrate Lipid Modifications of Proteins Methods in Enzymology Vol 250 pp 336 47 doi 10 1016 0076 6879 95 50083 9 ISBN 978 0 12 182151 7 PMID 7651163 Schriner JE Yi W Hofmann SL 1996 cDNA and genomic cloning of human palmitoyl protein thioesterase PPT the enzyme defective in infantile neuronal ceroid lipofuscinosis Genomics 34 3 317 22 doi 10 1006 geno 1996 0292 PMID 8786130 Verkruyse LA Hofmann SL 1996 Lysosomal targeting of palmitoyl protein thioesterase J Biol Chem 271 26 15831 6 doi 10 1074 jbc 271 26 15831 PMID 8663305 External links editPalmitoyl Thioesterase at the U S National Library of Medicine Medical Subject Headings MeSH GeneReviews NCBI NIH UW entry on Neuronal Ceroid LipofuscinosesThis article incorporates text from the public domain Pfam and InterPro IPR002472 Portal nbsp Biology This EC 3 1 enzyme related article is a stub You can help Wikipedia by expanding it vte Retrieved from https en wikipedia org w index php title Palmitoyl protein hydrolase amp oldid 1194446539, wikipedia, wiki, book, books, library,
