palmitoyl protein thioesterase 2; palmitoyl-protein hydrolase 2 (PPT2, G14)

Function: - removes thioester-linked fatty acyl groups from various substrates including S-palmitoyl-CoA - highest S-thioesterase activity for the acyl groups palmitic & myristic acid followed by other short- & long-chain acyl substrates - prefers acyl chain lengths of 14-18 carbons - however, because of structural constraints, is unable to remove palmitate from peptides or proteins Kinetic parameters: - KM=67 uM for S-palmitoyl-CoA - KM=37 uM for S-palmitoyl-N-acetylcysteamine - Vmax=1.7 umol/min/mg enzyme toward S-palmitoyl-CoA - Vmax=3.3 umol/min/mg enzyme toward S-palmitoyl-N-acetyl- cysteamine - ptimum pH is 7.0 Structure: belongs to the palmitoyl-protein thioesterase family Compartment: lysosome Alternative splicing: named isoforms=2 isoform(s) may be catalytically inactive due to lack of His-283, or may be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay Expression: - broadly expressed, with highest levels in skeletal muscle

General

glycoprotein thiol esterase or thioesterase

Properties

SIZE: MW = 34 kD entity length = 302 aa MOTIF: signal sequence {1-27} N-glycosylation site {N60} serine residue {S111} N-glycosylation site {N190} N-glycosylation site {N206} aspartate residue {D228} N-glycosylation site {N245} histidine residue {H283} N-glycosylation site {N289}

Database Correlations

OMIM 603298 UniProt Q9UMR5 Pfam PF02089 Entrez Gene 9374 KEGG correlations ENZYME 3.1.2.22

References

OMIM :accession 600722