DB code: S00720

RLCP classification 1.12.30000.10 : Hydrolysis
CATH domain 3.40.50.1820 : Rossmann fold Catalytic domain
E.C. 3.1.1.2
CSA
M-CSA
MACiE

CATH domain Related DB codes (homologues)
3.40.50.1820 : Rossmann fold S00544 S00344 S00517 S00525 S00526 S00723 S00724 S00725 S00919 S00057 S00374 S00345 S00347 S00348 S00346 S00350 S00352 S00353 S00355 S00356 S00358 D00189 D00210 D00539 T00253

Uniprot Enzyme Name
UniprotKB Protein name Synonyms Pfam
P22862 Arylesterase
EC 3.1.1.2
Aryl-ester hydrolase
PFE
Putative bromoperoxidase
EC 1.-.-.-
[Graphical View]
D0VWZ4
None PF00756 (Esterase)
[Graphical View]

KEGG enzyme name
Arylesterase
A-esterase
Paraoxonase
Aromatic esterase

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
P22862 ESTE_PSEFL A phenyl acetate + H(2)O = a phenol + acetate. Homodimer.
D0VWZ4 D0VWZ4_OLEAN

KEGG Pathways
Map code Pathways E.C.
MAP00363 Bisphenol A degradation

Compound table
Substrates Products Intermediates
KEGG-id C00548 C00001 C00146 C00033 I00078 I00125 I00126
E.C.
Compound phenyl acetate H2O phenol acetate Phenyl-tetrahedral intermediate (Peptidyl-Ser-phenylacetate-tetrahedral intermediate) Acetyl-enzyme (Peptidyl-Ser-acetyl group) Peptidyl-Ser-acetyl-tetrahedral-intermediate
Type aromatic ring (only carbon atom),carbohydrate H2O aromatic ring (only carbon atom) carboxyl group
ChEBI 8082
 8082
 		15377
 15377
 		15882
 15882
 		15366
 15366
PubChem 31229
 31229
 		22247451
 962
 22247451
 962
 		20488062
 996
 20488062
 996
 		176
 21980959
 176
 21980959
1va4A00 Unbound Unbound Unbound Unbound Unbound Unbound
1va4B00 Unbound Unbound Unbound Unbound Unbound Unbound
1va4C00 Unbound Unbound Unbound Unbound Unbound Unbound
1va4D00 Unbound Unbound Unbound Unbound Unbound Unbound
1va4E00 Unbound Unbound Unbound Unbound Unbound Unbound
1va4F00 Unbound Unbound Unbound Unbound Unbound Unbound
3heaA00 Unbound Unbound Unbound Transition-state-analogue:EEE Unbound Unbound
3heaB00 Unbound Unbound Unbound Transition-state-analogue:EEE Unbound Unbound
3heaC00 Unbound Unbound Unbound Transition-state-analogue:EEE Unbound Unbound
3heaD00 Unbound Unbound Unbound Transition-state-analogue:EEE Unbound Unbound
3heaE00 Unbound Unbound Unbound Transition-state-analogue:EEE Unbound Unbound
3heaF00 Unbound Unbound Unbound Transition-state-analogue:EEE Unbound Unbound
3hi4A00 Unbound Unbound Bound:ACT_272 Unbound Unbound Unbound
3hi4B00 Unbound Unbound Bound:ACT_272 Unbound Unbound Unbound
3hi4C00 Unbound Unbound Bound:ACT_272 Unbound Unbound Unbound
3hi4D00 Unbound Unbound Bound:ACT_272 Unbound Unbound Unbound
3hi4E00 Unbound Unbound Bound:ACT_272 Unbound Unbound Unbound
3hi4F00 Unbound Unbound Bound:ACT_272 Unbound Unbound Unbound
3ia2A00 Unbound Unbound Unbound Unbound Unbound Transition-state-analogue:J6Z
3ia2B00 Unbound Unbound Unbound Unbound Unbound Transition-state-analogue:J6Z
3ia2C00 Unbound Unbound Unbound Unbound Unbound Transition-state-analogue:J6Z
3ia2D00 Unbound Unbound Unbound Unbound Unbound Transition-state-analogue:J6Z
3ia2E00 Unbound Unbound Unbound Unbound Unbound Transition-state-analogue:J6Z
3ia2F00 Unbound Unbound Unbound Unbound Unbound Transition-state-analogue:J6Z
3i6yA00 Unbound Unbound Unbound Unbound Unbound Unbound
3i6yB00 Unbound Unbound Unbound Unbound Unbound Unbound
3s8yA00 Unbound Unbound Unbound Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.
Literature [6], [9] & Swiss-prot;P22862

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1va4A00 SER 94;ASP 222;HIS 251 TRP 28;MET 95
1va4B00 SER 94;ASP 222;HIS 251 TRP 28;MET 95
1va4C00 SER 94;ASP 222;HIS 251 TRP 28;MET 95
1va4D00 SER 94;ASP 222;HIS 251 TRP 28;MET 95
1va4E00 SER 94;ASP 222;HIS 251 TRP 28;MET 95
1va4F00 SER 94;ASP 222;HIS 251 TRP 28;MET 95
3heaA00 SER 94;ASP 222;HIS 251 TRP 28;MET 95
3heaB00 SER 94;ASP 222;HIS 251 TRP 28;MET 95
3heaC00 SER 94;ASP 222;HIS 251 TRP 28;MET 95
3heaD00 SER 94;ASP 222;HIS 251 TRP 28;MET 95
3heaE00 SER 94;ASP 222;HIS 251 TRP 28;MET 95
3heaF00 SER 94;ASP 222;HIS 251 TRP 28;MET 95
3hi4A00 SER 94;ASP 222;HIS 251 TRP 28;MET 95
3hi4B00 SER 94;ASP 222;HIS 251 TRP 28;MET 95
3hi4C00 SER 94;ASP 222;HIS 251 TRP 28;MET 95
3hi4D00 SER 94;ASP 222;HIS 251 TRP 28;MET 95
3hi4E00 SER 94;ASP 222;HIS 251 TRP 28;MET 95
3hi4F00 SER 94;ASP 222;HIS 251 TRP 28;MET 95
3ia2A00 SER 94;ASP 222;HIS 251 TRP 28;MET 95
3ia2B00 SER 94;ASP 222;HIS 251 TRP 28;MET 95
3ia2C00 SER 94;ASP 222;HIS 251 TRP 28;MET 95
3ia2D00 SER 94;ASP 222;HIS 251 TRP 28;MET 95
3ia2E00 SER 94;ASP 222;HIS 251 TRP 28;MET 95
3ia2F00 SER 94;ASP 222;HIS 251 TRP 28;MET 95
3i6yA00 SER 148;ASP 224;HIS 257 LEU 55;MET 149
3i6yB00 SER 148;ASP 224;HIS 257 LEU 55;MET 149
3s8yA00 SER 148;ASP 224;HIS 257 LEU 55;MET 149

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[6]
Figure 1
[7]
Fig. 5
[8]
Figure 3
[9]
FIGURE 1a

References
[1]
Resource
Comments
Medline ID
PubMed ID 7632719
Journal Biochim Biophys Acta
Year 1995
Volume 1250
Pages 149-57
Authors Pelletier I, Altenbuchner J, Mattes R
Title A catalytic triad is required by the non-heme haloperoxidases to perform halogenation.
Related PDB
Related UniProtKB
[2]
Resource
Comments
Medline ID
PubMed ID 7704276
Journal Microbiology
Year 1995
Volume 141
Pages 459-68
Authors Pelletier I, Altenbuchner J
Title A bacterial esterase is homologous with non-haem haloperoxidases and displays brominating activity.
Related PDB
Related UniProtKB
[3]
Resource
Comments
Medline ID
PubMed ID
Journal Enzyme Microb Technol
Year 1998
Volume 22
Pages 641-6
Authors Krebsfanger N, Zocher F, Altenbuchner J, Bornscheuer UT
Title Characterization and enantioselectivity of a recombinant esterase from Pseudomonas fluorescens.
Related PDB
Related UniProtKB
[4]
Resource
Comments
Medline ID
PubMed ID 9642069
Journal J Mol Biol
Year 1998
Volume 279
Pages 889-900
Authors Hofmann B, Tolzer S, Pelletier I, Altenbuchner J, van Pee KH, Hecht HJ
Title Structural investigation of the cofactor-free chloroperoxidases.
Related PDB
Related UniProtKB
[5]
Resource
Comments
Medline ID
PubMed ID 12369917
Journal Curr Protein Pept Sci
Year 2000
Volume 1
Pages 209-35
Authors Holmquist M
Title Alpha/Beta-hydrolase fold enzymes: structures, functions and mechanisms.
Related PDB
Related UniProtKB
[6]
Resource
Comments X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
Medline ID
PubMed ID 15213385
Journal Acta Crystallogr D Biol Crystallogr
Year 2004
Volume 60
Pages 1237-43
Authors Cheeseman JD, Tocilj A, Park S, Schrag JD, Kazlauskas RJ
Title Structure of an aryl esterase from Pseudomonas fluorescens.
Related PDB 1va4
Related UniProtKB P22862
[7]
Resource
Comments
Medline ID
PubMed ID 15381402
Journal Bioorg Chem
Year 2004
Volume 32
Pages 367-75
Authors Bugg TD
Title Diverse catalytic activities in the alphabeta-hydrolase family of enzymes: activation of H2O, HCN, H2O2, and O2.
Related PDB
Related UniProtKB
[8]
Resource
Comments
Medline ID
PubMed ID 15803517
Journal Angew Chem Int Ed Engl
Year 2005
Volume 44
Pages 2742-6
Authors Bernhardt P, Hult K, Kazlauskas RJ
Title Molecular basis of perhydrolase activity in serine hydrolases.
Related PDB
Related UniProtKB
[9]
Resource
Comments
Medline ID
PubMed ID 20112920
Journal Biochemistry
Year 2010
Volume 49
Pages 1931-42
Authors Yin de LT, Bernhardt P, Morley KL, Jiang Y, Cheeseman JD, Purpero V, Schrag JD, Kazlauskas RJ
Title Switching catalysis from hydrolysis to perhydrolysis in Pseudomonas fluorescens esterase.
Related PDB 3hea 3hi4
Related UniProtKB P22862

Comments
This enzyme has got a classical catalytic triad composed of Ser/His/Asp witha an oxyanion hole (see [6], [8], [9]). Thus, this enzyme seems to have a similar mechanism to that by other serine esterases.
Although this enzyme catalyzes hydrolysis of aryl esters, this enzyme shows low perhydrolysis activity, which is similar to that of non-heme chloroperoxidase (EC 1.11.1.10; S00344 in EzCatDB) (see [8], [9]). Moreover, this enzyme also shows structural similarity with the chloroperoxidase enzyme. Thus, the perhydrolysis mechanism must be similar to that of ester hydrolysis.

Created Updated
2011-01-19 2012-10-22