Structural highlights
Function
[ESTE_PSEFL] Bifunctional enzyme, capable of both ester hydrolysis and halogenation. Has a low bromoperoxidase activity. Acts on many phenolic esters.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The structure of PFE, an aryl esterase from Pseudomonas fluorescens, has been solved to a resolution of 1.8 A by X-ray diffraction and shows a characteristic alpha/beta-hydrolase fold. In addition to catalyzing the hydrolysis of esters in vitro, PFE also shows low bromoperoxidase activity. PFE shows highest structural similarity, including the active-site environment, to a family of non-heme bacterial haloperoxidases, with an r.m.s. deviation in 271 C(alpha) atoms between PFE and its five closest structural neighbors averaging 0.8 A. PFE has far less similarity (r.m.s. deviation in 218 C(alpha) atoms of 5.0 A) to P. fluorescens carboxyl esterase. PFE favors activated esters with small acyl groups, such as phenyl acetate. The X-ray structure of PFE reveals a significantly occluded active site. In addition, several residues, including Trp28 and Met95, limit the size of the acyl-binding pocket, explaining its preference for small acyl groups.
Structure of an aryl esterase from Pseudomonas fluorescens.,Cheeseman JD, Tocilj A, Park S, Schrag JD, Kazlauskas RJ Acta Crystallogr D Biol Crystallogr. 2004 Jul;60(Pt 7):1237-43. Epub 2004, Jun 22. PMID:15213385[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Cheeseman JD, Tocilj A, Park S, Schrag JD, Kazlauskas RJ. Structure of an aryl esterase from Pseudomonas fluorescens. Acta Crystallogr D Biol Crystallogr. 2004 Jul;60(Pt 7):1237-43. Epub 2004, Jun 22. PMID:15213385 doi:10.1107/S0907444904010522
