Palmitoyl(protein) hydrolase
| palmitoyl-(protein) hydrolase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 3.1.2.22 | ||||||||
| CAS number | 150605-49-5 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / EGO | ||||||||
| |||||||||
In enzymology, a palmitoyl[protein] hydrolase (EC 3.1.2.22) is an enzyme that catalyzes the chemical reaction
- palmitoyl[protein] + H2O palmitate + protein
Thus, the two substrates of this enzyme are [[palmitoyl[protein]]] and H2O, whereas its two products are palmitate and protein.
This enzyme belongs to the family of hydrolases, specifically those acting on thioester bonds. The systematic name of this enzyme class 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.
Structural studies
As of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes 1EH5, 1EI9, 1EXW, and 1PJA.
References
- Camp LA, Hofmann SL (1995). "Assay and isolation of palmitoyl-protein thioesterase from bovine brain using palmitoylated H-Ras as substrate". Methods Enzymol. Methods in Enzymology. 250: 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.
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