 A bacterial lipase, one of this family members | |||||||||
| Identifiers | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Symbol | Abhydrolase_1 | ||||||||
| Pfam | PF00561 | ||||||||
| Pfam clan | CL0028 | ||||||||
| ECOD | 7579.1.1 | ||||||||
| InterPro | IPR029058 | ||||||||
| SCOP2 | 1ede / SCOPe / SUPFAM | ||||||||
| OPM superfamily | 127 | ||||||||
| OPM protein | 1qge | ||||||||
| CDD | cl21494 | ||||||||
| Membranome | 300 | ||||||||
| |||||||||
The alpha/beta hydrolase superfamily is a superfamily of hydrolytic enzymes of widely differing phylogenetic origin and catalytic function that share a common fold.[1] The core of each enzyme is an alpha/beta-sheet (rather than a barrel), containing 8 beta strands connected by 6 alpha helices.[1][2] The enzymes are believed to have diverged from a common ancestor, retaining little obvious sequence similarity, but preserving the arrangement of the catalytic residues. All have a catalytic triad, the elements of which are borne on loops, which are the best-conserved structural features of the fold.
The alpha/beta hydrolase fold includes proteases, lipases, peroxidases, esterases, epoxide hydrolases and dehalogenases.[3]
- ^ a b Ollis, D. L.; Cheah, E.; Cygler, M.; Dijkstra, B.; Frolow, F.; Franken, S. M.; Harel, M.; Remington, S. J.; Silman, I.; Schrag, J.; Sussman, J. L.; Verschueren, K. H. G. & Goldman, A. (1992). "The alpha/beta hydrolase fold" (PDF). Protein Eng. 5 (3): 197–211. doi:10.1093/protein/5.3.197. hdl:11370/2d4c057d-1a67-437d-ad10-701f7a60f1e6. PMID 1409539.
- ^ Carr PD, Ollis DL (2009). "Alpha/beta hydrolase fold: an update". Protein Pept. Lett. 16 (10): 1137–48. doi:10.2174/092986609789071298. PMID 19508187.
- ^ Nardini M, Dijkstra BW (December 1999). "Alpha/beta hydrolase fold enzymes: the family keeps growing". Curr. Opin. Struct. Biol. 9 (6): 732–7. doi:10.1016/S0959-440X(99)00037-8. PMID 10607665.