 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. | |||||||||
| Identifiers | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Symbol | Acyl-protein thioesterases (APTs) | ||||||||
| Pfam | PF02230 | ||||||||
| InterPro | IPR029058 | ||||||||
| |||||||||
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.[1] Acyl-protein thioesterases are part of the α/β hydrolase superfamily of proteins and have a conserved catalytic triad.[2] For that reason, acyl-protein thioesterases are also able to hydrolyze oxygen-linked ester bonds.
- ^ Zeidman R, Jackson CS, Magee AI (January 2009). "Protein acyl thioesterases (Review)". Molecular Membrane Biology. 26 (1): 32–41. doi:10.1080/09687680802629329. hdl:10044/1/1452. PMID 19115143. S2CID 10591154.
- ^ Devedjiev Y, Dauter Z, Kuznetsov SR, Jones TL, Derewenda ZS (November 2000). "Crystal structure of the human acyl protein thioesterase I from a single X-ray data set to 1.5 A". Structure. 8 (11): 1137–46. doi:10.1016/s0969-2126(00)00529-3. PMID 11080636.