Jump to content

Alpha/beta hydrolase superfamily

From Wikipedia, the free encyclopedia

This is an old revision of this page, as edited by Tom.Reding (talk | contribs) at 23:34, 20 May 2016 (CS1 maintenance: vauthors/veditors or enumerate multiple authors/editors; WP:GenFixes on; using AWB). The present address (URL) is a permanent link to this revision, which may differ significantly from the current revision.

A bacterial lipase, one of this family members
Identifiers
SymbolAbhydrolase_1
PfamPF00561
InterProIPR000073
SCOP21ede / SCOPe / SUPFAM
OPM superfamily135
OPM protein1qge
CDDcl21494
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
PDB1q0zA:52-292 1q0rA:52-292 1y7iA:32-106

1xklB:32-106 1y7hA:32-106 1eb8A:31-252 1dwqA:31-252 1e89B:31-252 1e8dA:31-252 1dwoA:31-252 1dwpA:31-252 1eb9B:31-252 1sc9A:31-251 6yasA:31-251 1sckA:31-251 3yasA:31-251 1sciA:31-251 5yasA:31-251 7yasA:31-251 1qj4A:31-251 1yb7A:31-251 4yasA:31-251 1scqA:31-251 2yasA:31-251 1yb6A:31-251 1m33A:40-251 1a88C:50-272 1a8s :48-270 1a8q :48-271 1va4E:48-268 1a7uA:52-274 1a8uA:52-274 1broB:52-274 1brt :52-274 1hl7B:52-276 1hkhA:52-276 1u2eD:71-288 1ukbA:55-268 1uk7A:55-268 1uk9A:55-268 1c4xA:59-280 1j1iA:66-277 1qtrA:64-315 1wm1A:64-315 1azwA:61-308 1r3dA:43-256 1ehyD:56-291 1qo7B:142-201 2eda :75-305 1ede :75-305 1bez :75-305 1bn6A:59-288 1cqwA:59-288 1bn7A:59-288 1mj5A:56-288 1d07A:56-288 1womB:45-263 1wprB:45-263 1xqxA:56-287 1xrmA:56-287 1xrqA:56-287 1mt3A:56-287 1xqwA:56-287 2b61A:92-353 1tahD:81-334 1qgeD:81-261 1cvl :81-334 4lipE:86-340 3lip :86-340 1ex9A:45-290 1i6wB:78-117 1r50A:78-117 1r4zB:78-117 1t4mA:78-117 1t2nA:78-117 1ispA:78-117 1hlgB:111-391 1k8qA:111-392

1s8oA:286-540 1vj5A:286-540 1cr6A:284-539

In molecular biology, the alpha/beta hydrolase fold is common to a number of hydrolytic enzymes of widely differing phylogenetic origin and catalytic function.[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, 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.

This catalytic domain is found in a very wide range of enzymes which do not share obvious sequence similarity. 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 family of proteins.[4]

Subfamilies

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; MEST; MGLL; PPME1; SERHL; SERHL2; SPG21; CES1; CES2; C4orf29

See also

  • Serine hydrolase - an enzyme family that is composed largely of proteins with alpha-beta hydrolase folds

References

  1. ^ 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". Protein Eng. 5 (3): 197–211. doi:10.1093/protein/5.3.197. PMID 1409539. {{cite journal}}: Unknown parameter |last-author-amp= ignored (|name-list-style= suggested) (help)
  2. ^ Carr PD, Ollis DL (2009). "Alpha/beta hydrolase fold: an update". Protein Pept. Lett. 16 (10): 1137–48. PMID 19508187.
  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.
  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.