1pja

Structural highlights

Function

PPT2_HUMAN Removes thioester-linked fatty acyl groups from various substrates including S-palmitoyl-CoA. Has the highest S-thioesterase activity for the acyl groups palmitic and myristic acid followed by other short- and long-chain acyl substrates. However, because of structural constraints, is unable to remove palmitate from peptides or proteins.^{[1] [2] [3]}

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

• Thioesterase 3D structures

References

1. ↑ Soyombo AA, Hofmann SL. Molecular cloning and expression of palmitoyl-protein thioesterase 2 (PPT2), a homolog of lysosomal palmitoyl-protein thioesterase with a distinct substrate specificity. J Biol Chem. 1997 Oct 24;272(43):27456-63. PMID:9341199
2. ↑ Aguado B, Campbell RD. Characterization of a human MHC class III region gene product with S-thioesterase activity. Biochem J. 1999 Aug 1;341 ( Pt 3):679-89. PMID:10417332
3. ↑ Calero G, Gupta P, Nonato MC, Tandel S, Biehl ER, Hofmann SL, Clardy J. The crystal structure of palmitoyl protein thioesterase-2 (PPT2) reveals the basis for divergent substrate specificities of the two lysosomal thioesterases, PPT1 and PPT2. J Biol Chem. 2003 Sep 26;278(39):37957-64. Epub 2003 Jul 10. PMID:12855696 doi:http://dx.doi.org/10.1074/jbc.M301225200