Alpha/beta hydrolase superfamily

Available protein structures:
Pfam	structures / ECOD
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary

	A bacterial lipase, one of this family members
Identifiers
Symbol	Abhydrolase_1
Pfam	PF00561
InterPro	IPR000073
SCOP2	1ede / SCOPe / SUPFAM
OPM superfamily	127
OPM protein	1qge
CDD	cl21494
Membranome	300
Pfam
Available protein structures:
Pfam	structures / ECOD
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary

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]

Database

The ESTHER database provides a large collection of information about this superfamily of proteins.[4]

Subfamilies

3-oxoadipate enol-lactonase InterPro: IPR012790

Human proteins containing this domain

ABHD10; ABHD11; ABHD12; ABHD12B; ABHD13; ABHD2; ABHD3; ABHD4; ABHD5; ABHD6; ABHD7; ABHD8; ABHD9; BAT5; BPHL; C20orf135; EPHX1; EPHX2; FAM108B1; LIPA; LIPF; LIPJ; LIPK; LIPM; LIPN; LYPLAL1; MEST; MGLL; PPME1; SERHL; SERHL2; SPG21; CES1; CES2; C4orf29

External links

The ESTHER database

References

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.
Renault L, Nègre V, Hotelier T, Cousin X, Marchot P, Chatonnet A (December 2005). "New friendly tools for users of ESTHER, the database of the alpha/beta-hydrolase fold superfamily of proteins". Chem. Biol. Interact. 157–158: 339–43. doi:10.1016/j.cbi.2005.10.100. PMID 16297901.

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[PUB00004958-1] 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.

[pmid19508187-2] Carr PD, Ollis DL (2009). "Alpha/beta hydrolase fold: an update". Protein Pept. Lett. 16 (10): 1137–48. doi:10.2174/092986609789071298. PMID 19508187.

[pmid10607665-3] 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.

[pmid16297901-4] Renault L, Nègre V, Hotelier T, Cousin X, Marchot P, Chatonnet A (December 2005). "New friendly tools for users of ESTHER, the database of the alpha/beta-hydrolase fold superfamily of proteins". Chem. Biol. Interact. 157–158: 339–43. doi:10.1016/j.cbi.2005.10.100. PMID 16297901.