EzCatDB: S00720
Related links:    PDB-formatted query search system Fasta-formatted query search system Fasta-formatted query search system

DB codeS00720
RLCP classification1.12.30000.10 : Hydrolysis
CATH domainDomain 13.40.50.1820 : Rossmann foldCatalytic domain
E.C.3.1.1.2

CATH domainRelated DB codes (homologues)
3.40.50.1820 : Rossmann foldS00544,S00344,S00517,S00525,S00526,S00723,S00724,S00725,S00919,S00057,S00374,S00345,S00347,S00348,S00346,S00350,S00352,S00353,S00355,S00356,S00358,D00189,D00210,D00539,T00253

Enzyme Name
UniProtKBKEGG

P22862D0VWZ4
Protein nameArylesterase
Arylesterase
A-esterase
Paraoxonase
Aromatic esterase
SynonymsEC 3.1.1.2
Aryl-ester hydrolase
PFE
Putative bromoperoxidase
EC 1.-.-.-
None
Pfam
PF00756 (Esterase)
[Graphical view]

KEGG pathways
MAP codePathways
MAP00363Bisphenol A degradation

UniProtKB:Accession NumberP22862D0VWZ4
Entry nameESTE_PSEFLD0VWZ4_OLEAN
ActivityA phenyl acetate + H(2)O = a phenol + acetate.
SubunitHomodimer.
Subcellular location

Cofactor


Compound table: links to PDB-related databases & PoSSuM

SubstratesProductsintermediates
KEGG-idC00548C00001C00146C00033I00078I00125I00126
Compoundphenyl acetateH2OphenolacetatePhenyl-tetrahedral intermediate (Peptidyl-Ser-phenylacetate-tetrahedral intermediate)Acetyl-enzyme (Peptidyl-Ser-acetyl group)Peptidyl-Ser-acetyl-tetrahedral-intermediate
Typearomatic ring (only carbon atom),carbohydrateH2Oaromatic ring (only carbon atom)carboxyl group


ChEBI8082
15377
15882
15366



PubChem31229
962
22247451
996
20488062
21980959
176



               
1va4A00Unbound UnboundUnboundUnboundUnboundUnbound
1va4B00Unbound UnboundUnboundUnboundUnboundUnbound
1va4C00Unbound UnboundUnboundUnboundUnboundUnbound
1va4D00Unbound UnboundUnboundUnboundUnboundUnbound
1va4E00Unbound UnboundUnboundUnboundUnboundUnbound
1va4F00Unbound UnboundUnboundUnboundUnboundUnbound
3heaA00Unbound UnboundUnboundTransition-state-analogue:EEEUnboundUnbound
3heaB00Unbound UnboundUnboundTransition-state-analogue:EEEUnboundUnbound
3heaC00Unbound UnboundUnboundTransition-state-analogue:EEEUnboundUnbound
3heaD00Unbound UnboundUnboundTransition-state-analogue:EEEUnboundUnbound
3heaE00Unbound UnboundUnboundTransition-state-analogue:EEEUnboundUnbound
3heaF00Unbound UnboundUnboundTransition-state-analogue:EEEUnboundUnbound
3hi4A00Unbound UnboundBound:ACT 272UnboundUnboundUnbound
3hi4B00Unbound UnboundBound:ACT 272UnboundUnboundUnbound
3hi4C00Unbound UnboundBound:ACT 272UnboundUnboundUnbound
3hi4D00Unbound UnboundBound:ACT 272UnboundUnboundUnbound
3hi4E00Unbound UnboundBound:ACT 272UnboundUnboundUnbound
3hi4F00Unbound UnboundBound:ACT 272UnboundUnboundUnbound
3ia2A00Unbound UnboundUnboundUnboundUnboundTransition-state-analogue:J6Z
3ia2B00Unbound UnboundUnboundUnboundUnboundTransition-state-analogue:J6Z
3ia2C00Unbound UnboundUnboundUnboundUnboundTransition-state-analogue:J6Z
3ia2D00Unbound UnboundUnboundUnboundUnboundTransition-state-analogue:J6Z
3ia2E00Unbound UnboundUnboundUnboundUnboundTransition-state-analogue:J6Z
3ia2F00Unbound UnboundUnboundUnboundUnboundTransition-state-analogue:J6Z
3i6yA00Unbound UnboundUnboundUnboundUnboundUnbound
3i6yB00Unbound UnboundUnboundUnboundUnboundUnbound
3s8yA00Unbound UnboundUnboundUnboundUnboundUnbound

Active-site residues
resource
Literature [6], [9] & Swiss-prot;P22862
pdbCatalytic residuesMain-chain involved in catalysis
          
1va4A00SER  94;ASP 222;HIS 251
TRP 28;MET  95
1va4B00SER  94;ASP 222;HIS 251
TRP 28;MET  95
1va4C00SER  94;ASP 222;HIS 251
TRP 28;MET  95
1va4D00SER  94;ASP 222;HIS 251
TRP 28;MET  95
1va4E00SER  94;ASP 222;HIS 251
TRP 28;MET  95
1va4F00SER  94;ASP 222;HIS 251
TRP 28;MET  95
3heaA00SER  94;ASP 222;HIS 251
TRP 28;MET  95
3heaB00SER  94;ASP 222;HIS 251
TRP 28;MET  95
3heaC00SER  94;ASP 222;HIS 251
TRP 28;MET  95
3heaD00SER  94;ASP 222;HIS 251
TRP 28;MET  95
3heaE00SER  94;ASP 222;HIS 251
TRP 28;MET  95
3heaF00SER  94;ASP 222;HIS 251
TRP 28;MET  95
3hi4A00SER  94;ASP 222;HIS 251
TRP 28;MET  95
3hi4B00SER  94;ASP 222;HIS 251
TRP 28;MET  95
3hi4C00SER  94;ASP 222;HIS 251
TRP 28;MET  95
3hi4D00SER  94;ASP 222;HIS 251
TRP 28;MET  95
3hi4E00SER  94;ASP 222;HIS 251
TRP 28;MET  95
3hi4F00SER  94;ASP 222;HIS 251
TRP 28;MET  95
3ia2A00SER  94;ASP 222;HIS 251
TRP 28;MET  95
3ia2B00SER  94;ASP 222;HIS 251
TRP 28;MET  95
3ia2C00SER  94;ASP 222;HIS 251
TRP 28;MET  95
3ia2D00SER  94;ASP 222;HIS 251
TRP 28;MET  95
3ia2E00SER  94;ASP 222;HIS 251
TRP 28;MET  95
3ia2F00SER  94;ASP 222;HIS 251
TRP 28;MET  95
3i6yA00SER 148;ASP 224;HIS 257
LEU 55;MET 149
3i6yB00SER 148;ASP 224;HIS 257
LEU 55;MET 149
3s8yA00SER 148;ASP 224;HIS 257
LEU 55;MET 149

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[6]Figure 1
[7]Fig. 5
[8]Figure 3
[9]FIGURE 1a

references
[1]
PubMed ID7632719
JournalBiochim Biophys Acta
Year1995
Volume1250
Pages149-57
AuthorsPelletier I, Altenbuchner J, Mattes R
TitleA catalytic triad is required by the non-heme haloperoxidases to perform halogenation.
[2]
PubMed ID7704276
JournalMicrobiology
Year1995
Volume141
Pages459-68
AuthorsPelletier I, Altenbuchner J
TitleA bacterial esterase is homologous with non-haem haloperoxidases and displays brominating activity.
[3]
JournalEnzyme Microb Technol
Year1998
Volume22
Pages641-6
AuthorsKrebsfanger N, Zocher F, Altenbuchner J, Bornscheuer UT
TitleCharacterization and enantioselectivity of a recombinant esterase from Pseudomonas fluorescens.
[4]
PubMed ID9642069
JournalJ Mol Biol
Year1998
Volume279
Pages889-900
AuthorsHofmann B, Tolzer S, Pelletier I, Altenbuchner J, van Pee KH, Hecht HJ
TitleStructural investigation of the cofactor-free chloroperoxidases.
[5]
PubMed ID12369917
JournalCurr Protein Pept Sci
Year2000
Volume1
Pages209-35
AuthorsHolmquist M
TitleAlpha/Beta-hydrolase fold enzymes: structures, functions and mechanisms.
[6]
CommentsX-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
PubMed ID15213385
JournalActa Crystallogr D Biol Crystallogr
Year2004
Volume60
Pages1237-43
AuthorsCheeseman JD, Tocilj A, Park S, Schrag JD, Kazlauskas RJ
TitleStructure of an aryl esterase from Pseudomonas fluorescens.
Related PDB1va4
Related UniProtKBP22862
[7]
PubMed ID15381402
JournalBioorg Chem
Year2004
Volume32
Pages367-75
AuthorsBugg TD
TitleDiverse catalytic activities in the alphabeta-hydrolase family of enzymes: activation of H2O, HCN, H2O2, and O2.
[8]
PubMed ID15803517
JournalAngew Chem Int Ed Engl
Year2005
Volume44
Pages2742-6
AuthorsBernhardt P, Hult K, Kazlauskas RJ
TitleMolecular basis of perhydrolase activity in serine hydrolases.
[9]
PubMed ID20112920
JournalBiochemistry
Year2010
Volume49
Pages1931-42
AuthorsYin de LT, Bernhardt P, Morley KL, Jiang Y, Cheeseman JD, Purpero V, Schrag JD, Kazlauskas RJ
TitleSwitching catalysis from hydrolysis to perhydrolysis in Pseudomonas fluorescens esterase.
Related PDB3hea,3hi4
Related UniProtKBP22862

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.

createdupdated
2011-01-192012-10-22


Copyright: Nozomi Nagano, JST & CBRC-AIST
Funded by PRESTO/Japan Science and Technology Corporation (JST) (December 2001 - November 2004)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
Funded by Grant-in-Aid for Scientific Research (B)/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2012 - March 2013)
Supported by the commission for the Development of Artificial Gene Synthesis Technology for Creating Innovative Biomaterial from the Ministry of Economy, Trade and Industry (METI) (October 2012 - )
© Biotechnology Research Institute for Drug Discovery, AIST, 2015-2016 All Rights Reserved.
© Computational Biology Research Center, AIST, 2004-2016 All Rights Reserved.