ESTE_PSEFL
ID ESTE_PSEFL Reviewed; 272 AA.
AC P22862;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Arylesterase {ECO:0000303|PubMed:1368608};
DE EC=3.1.1.2 {ECO:0000269|PubMed:1368608, ECO:0000269|PubMed:15803517, ECO:0000269|PubMed:7704276, ECO:0000269|PubMed:9571805};
DE AltName: Full=Aryl-ester hydrolase;
DE AltName: Full=Carboxylic acid perhydrolase {ECO:0000303|PubMed:22618813};
DE AltName: Full=PFE {ECO:0000303|PubMed:9571805};
DE AltName: Full=Putative bromoperoxidase;
DE EC=1.-.-.-;
GN Name=estF {ECO:0000303|PubMed:9571805};
OS Pseudomonas fluorescens.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=294;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-18, FUNCTION, AND
RP CATALYTIC ACTIVITY.
RC STRAIN=SIK WI;
RX PubMed=1368608; DOI=10.1271/bbb1961.54.2039;
RA Choi K.D., Jeohn G.H., Rhee J.S., Yoo O.J.;
RT "Cloning and nucleotide sequence of an esterase gene from Pseudomonas
RT fluorescens and expression of the gene in Escherichia coli.";
RL Agric. Biol. Chem. 54:2039-2045(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=SIK WI;
RX PubMed=7704276; DOI=10.1099/13500872-141-2-459;
RA Pelletier I., Altenbuchner J.;
RT "A bacterial esterase is homologous with non-haem haloperoxidases and
RT displays brominating activity.";
RL Microbiology 141:459-468(1995).
RN [3]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=9571805; DOI=10.1016/s0168-1656(97)00192-2;
RA Krebsfaenger N., Schierholz K., Bornscheuer U.T.;
RT "Enantioselectivity of a recombinant esterase from Pseudomonas fluorescens
RT towards alcohols and carboxylic acids.";
RL J. Biotechnol. 60:105-111(1998).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP MUTAGENESIS OF LEU-30; TYR-70; MET-96; ASP-100; THR-123 AND PHE-228.
RX PubMed=15803517; DOI=10.1002/anie.200463006;
RA Bernhardt P., Hult K., Kazlauskas R.J.;
RT "Molecular basis of perhydrolase activity in serine hydrolases.";
RL Angew. Chem. Int. Ed. 44:2742-2746(2005).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP MUTAGENESIS OF LEU-30.
RX PubMed=22618813; DOI=10.1002/chem.201200052;
RA Yin D.T., Kazlauskas R.J.;
RT "Revised molecular basis of the promiscuous carboxylic acid perhydrolase
RT activity in serine hydrolases.";
RL Chemistry 18:8130-8139(2012).
RN [6] {ECO:0007744|PDB:1VA4}
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 2-272, FUNCTION, SUBUNIT, AND
RP ACTIVE SITE.
RX PubMed=15213385; DOI=10.1107/s0907444904010522;
RA Cheeseman J.D., Tocilj A., Park S., Schrag J.D., Kazlauskas R.J.;
RT "Structure of an aryl esterase from Pseudomonas fluorescens.";
RL Acta Crystallogr. D 60:1237-1243(2004).
RN [7] {ECO:0007744|PDB:3HEA, ECO:0007744|PDB:3HI4}
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 2-272 OF MUTANT PRO-30 IN COMPLEX
RP WITH ACETATE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES,
RP AND MUTAGENESIS OF LEU-30 AND PHE-58.
RX PubMed=20112920; DOI=10.1021/bi9021268;
RA Yin D.L., Bernhardt P., Morley K.L., Jiang Y., Cheeseman J.D., Purpero V.,
RA Schrag J.D., Kazlauskas R.J.;
RT "Switching catalysis from hydrolysis to perhydrolysis in Pseudomonas
RT fluorescens esterase.";
RL Biochemistry 49:1931-1942(2010).
RN [8] {ECO:0007744|PDB:3IA2}
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 2-272 IN COMPLEX WITH A SULFONATE
RP TRANSITION-STATE ANALOG.
RX PubMed=21351219; DOI=10.1002/cbic.201000693;
RA Jiang Y., Morley K.L., Schrag J.D., Kazlauskas R.J.;
RT "Different active-site loop orientation in serine hydrolases versus
RT acyltransferases.";
RL ChemBioChem 12:768-776(2011).
RN [9] {ECO:0007744|PDB:3T4U, ECO:0007744|PDB:3T52}
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 2-272 OF MUTANT ILE-30 IN COMPLEX
RP WITH ACETATE AND HYDROGEN PEROXIDE, AND MUTAGENESIS OF LEU-30.
RX PubMed=23325572; DOI=10.1002/chem.201202027;
RA Yin D.T., Purpero V.M., Fujii R., Jing Q., Kazlauskas R.J.;
RT "New structural motif for carboxylic acid perhydrolases.";
RL Chemistry 19:3037-3046(2013).
CC -!- FUNCTION: Hydrolyzes phenolic esters, such as phenyl acetate,
CC nitrophenyl acetate and naphtyl acetate (PubMed:1368608,
CC PubMed:7704276, PubMed:9571805, PubMed:15803517). Can act on a wide
CC range of esters, but reaction rate and enantioselectivity differ
CC significantly depending on the substrate (PubMed:1368608,
CC PubMed:9571805). Shows a preference for esters with small acyl groups
CC (PubMed:15213385). Also shows low perhydrolase activity, and catalyzes
CC the reversible formation of peroxycarboxylic acids from carboxylic
CC acids and hydrogen peroxide (PubMed:15803517, PubMed:20112920,
CC PubMed:22618813). In vitro, enzyme-generated peracetic acid oxidizes
CC bromide ion to bromonium, which reacts with monochlorodimedone to form
CC bromochlorodimedone (PubMed:7704276, PubMed:20112920, PubMed:22618813).
CC {ECO:0000269|PubMed:1368608, ECO:0000269|PubMed:15213385,
CC ECO:0000269|PubMed:15803517, ECO:0000269|PubMed:20112920,
CC ECO:0000269|PubMed:22618813, ECO:0000269|PubMed:7704276,
CC ECO:0000269|PubMed:9571805}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a phenyl acetate + H2O = a phenol + acetate + H(+);
CC Xref=Rhea:RHEA:17309, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30089, ChEBI:CHEBI:33853, ChEBI:CHEBI:140310; EC=3.1.1.2;
CC Evidence={ECO:0000269|PubMed:1368608, ECO:0000269|PubMed:15803517,
CC ECO:0000269|PubMed:7704276, ECO:0000269|PubMed:9571805};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + peracetic acid = acetate + H(+) + H2O2;
CC Xref=Rhea:RHEA:68392, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:30089, ChEBI:CHEBI:42530;
CC Evidence={ECO:0000269|PubMed:15803517, ECO:0000269|PubMed:20112920};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a percarboxylic acid + H2O = a carboxylate + H(+) + H2O2;
CC Xref=Rhea:RHEA:68396, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:29067, ChEBI:CHEBI:177878;
CC Evidence={ECO:0000269|PubMed:15803517, ECO:0000269|PubMed:20112920,
CC ECO:0000269|PubMed:22618813};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=92 uM for 4-nitrophenyl acetate {ECO:0000269|PubMed:7704276};
CC KM=2.8 mM for 4-nitrophenyl acetate {ECO:0000269|PubMed:15803517};
CC KM=33 mM for ethyl acetate {ECO:0000269|PubMed:20112920};
CC KM=43 mM for methyl acetate {ECO:0000269|PubMed:20112920};
CC KM=60 mM for methyl acetate {ECO:0000269|PubMed:22618813};
CC KM=0.041 mM for peracetic acid {ECO:0000269|PubMed:20112920};
CC KM=500 mM for acetic acid {ECO:0000269|PubMed:20112920};
CC KM=3.3 mM for hydrogen peroxide {ECO:0000269|PubMed:20112920};
CC KM=17 mM for H(2)O(2) {ECO:0000269|PubMed:15803517};
CC Note=kcat is 9 sec(-1) with ethyl acetate as substrate. kcat is 25
CC sec(-1) with methyl acetate as substrate. kcat is 100 sec(-1) with
CC peracetic acid as substrate. kcat is 0.12 sec(-1) with acetic acid as
CC substrate. kcat is 0.094 sec(-1) with hydrogen peroxide as substrate
CC (PubMed:20112920). kcat is 15 sec(-1) with methyl acetate as
CC substrate (PubMed:22618813). {ECO:0000269|PubMed:20112920,
CC ECO:0000269|PubMed:22618813};
CC pH dependence:
CC Optimum pH is above 9.0 for esterase activity.
CC {ECO:0000269|PubMed:7704276};
CC Temperature dependence:
CC Optimum temperature is 70 degrees Celsius for esterase activity.
CC {ECO:0000269|PubMed:7704276};
CC -!- SUBUNIT: Dimer of trimers. {ECO:0000269|PubMed:15213385}.
CC -!- MISCELLANEOUS: It is unlikely that perhydrolysis is the natural
CC function of perhydrolases. Instead, perhydrolysis is probably an
CC accidental (promiscuous) activity (Probable). Perhydrolysis is an
CC important reaction that makes peroxycarboxylic acids, which are useful
CC oxidants in organic chemistry, for lignin removal and pulp bleaching
CC and for disinfecting wastewater and disinfecting equipment for food and
CC medical applications (PubMed:23325572). Perhydrolases were previously
CC known as metal-free haloperoxidases (Probable).
CC {ECO:0000269|PubMed:23325572, ECO:0000305, ECO:0000305|PubMed:22618813,
CC ECO:0000305|PubMed:23325572}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Bacterial non-heme
CC haloperoxidase / perhydrolase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA02052.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; D12484; BAA02052.1; ALT_FRAME; Genomic_DNA.
DR EMBL; U12537; AAB60168.1; -; Genomic_DNA.
DR PIR; JQ0606; JQ0606.
DR PDB; 1VA4; X-ray; 1.80 A; A/B/C/D/E/F=2-272.
DR PDB; 3HEA; X-ray; 1.90 A; A/B/C/D/E/F=2-272.
DR PDB; 3HI4; X-ray; 2.25 A; A/B/C/D/E/F=2-272.
DR PDB; 3IA2; X-ray; 1.65 A; A/B/C/D/E/F=2-272.
DR PDB; 3T4U; X-ray; 2.02 A; A/B/C/D/E/F=2-272.
DR PDB; 3T52; X-ray; 2.00 A; A/B/C/D/E/F=2-272.
DR PDBsum; 1VA4; -.
DR PDBsum; 3HEA; -.
DR PDBsum; 3HI4; -.
DR PDBsum; 3IA2; -.
DR PDBsum; 3T4U; -.
DR PDBsum; 3T52; -.
DR AlphaFoldDB; P22862; -.
DR SMR; P22862; -.
DR ESTHER; psefl-este; Haloperoxidase.
DR PeroxiBase; 5910; PfHalNPrx03_SIKWI.
DR SABIO-RK; P22862; -.
DR EvolutionaryTrace; P22862; -.
DR GO; GO:0004064; F:arylesterase activity; IEA:UniProtKB-EC.
DR GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR InterPro; IPR000639; Epox_hydrolase-like.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR PRINTS; PR00111; ABHYDROLASE.
DR PRINTS; PR00412; EPOXHYDRLASE.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Hydrolase; Oxidoreductase;
KW Peroxidase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1368608"
FT CHAIN 2..272
FT /note="Arylesterase"
FT /id="PRO_0000207059"
FT DOMAIN 21..253
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255"
FT ACT_SITE 95
FT /evidence="ECO:0000305|PubMed:15213385"
FT ACT_SITE 223
FT /evidence="ECO:0000305|PubMed:15213385"
FT ACT_SITE 252
FT /evidence="ECO:0000305|PubMed:15213385"
FT BINDING 29
FT /ligand="acetate"
FT /ligand_id="ChEBI:CHEBI:30089"
FT /evidence="ECO:0000269|PubMed:20112920,
FT ECO:0007744|PDB:3HI4"
FT BINDING 96
FT /ligand="acetate"
FT /ligand_id="ChEBI:CHEBI:30089"
FT /evidence="ECO:0000269|PubMed:20112920,
FT ECO:0007744|PDB:3HI4"
FT MUTAGEN 30
FT /note="L->I: 125-fold increase in catalytic efficiency for
FT perhydrolase activity with acetic acid as substrate. 2-fold
FT decrease in catalytic efficiency for perhydrolase activity
FT with ethyl acetate as substrate. 1.5-fold increase in
FT catalytic efficiency for hydrolase activity with ethyl
FT acetate as substrate. 2.4-fold increase in kcat for
FT hydrolysis of peracetic acid."
FT /evidence="ECO:0000269|PubMed:23325572"
FT MUTAGEN 30
FT /note="L->P: Shows faster acetyl-enzyme formation. Tenfold
FT more efficient at hydrolysis than perhydrolysis with methyl
FT acetate as substrate. 3-fold decrease in catalytic
FT efficiency for hydrolase activity with methyl acetate as
FT substrate. 15-fold decrease in catalytic efficiency for
FT perhydrolase activity with methyl acetate as substrate
FT (PubMed:22618813). 100-fold decrease in hydrolase activity
FT with 4-nitrophenyl acetate as substrate. 28-fold increase
FT in perhydrolase activity with acetate as substrate
FT (PubMed:15803517). 100-fold increase in catalytic
FT efficiency with acetic acid as substrate. 50-fold increase
FT in catalytic efficiency with acetic acid as substrate; when
FT associated with H-58 (PubMed:20112920)."
FT /evidence="ECO:0000269|PubMed:15803517,
FT ECO:0000269|PubMed:20112920, ECO:0000269|PubMed:22618813"
FT MUTAGEN 58
FT /note="F->H: 50-fold increase in catalytic efficiency with
FT acetic acid as substrate; when associated with P-30."
FT /evidence="ECO:0000269|PubMed:20112920"
FT MUTAGEN 70
FT /note="Y->M: Does not affect esterase and perhydrolase
FT activities."
FT /evidence="ECO:0000269|PubMed:15803517"
FT MUTAGEN 96
FT /note="M->T: 4-fold decrease in esterase activity. Loss of
FT perhydrolase activity."
FT /evidence="ECO:0000269|PubMed:15803517"
FT MUTAGEN 100
FT /note="D->E: Small decrease in esterase and perhydrolase
FT activities."
FT /evidence="ECO:0000269|PubMed:15803517"
FT MUTAGEN 123
FT /note="T->P: Does not affect esterase and perhydrolase
FT activities."
FT /evidence="ECO:0000269|PubMed:15803517"
FT MUTAGEN 228
FT /note="F->I: 3-fold increase in esterase activity. No
FT change in perhydrolase activity."
FT /evidence="ECO:0000269|PubMed:15803517"
FT STRAND 3..5
FT /evidence="ECO:0007829|PDB:3IA2"
FT STRAND 11..26
FT /evidence="ECO:0007829|PDB:3IA2"
FT HELIX 33..36
FT /evidence="ECO:0007829|PDB:3IA2"
FT HELIX 37..44
FT /evidence="ECO:0007829|PDB:3IA2"
FT TURN 45..47
FT /evidence="ECO:0007829|PDB:3IA2"
FT STRAND 49..53
FT /evidence="ECO:0007829|PDB:3IA2"
FT HELIX 70..84
FT /evidence="ECO:0007829|PDB:3IA2"
FT STRAND 88..94
FT /evidence="ECO:0007829|PDB:3IA2"
FT HELIX 97..108
FT /evidence="ECO:0007829|PDB:3IA2"
FT STRAND 113..120
FT /evidence="ECO:0007829|PDB:3IA2"
FT HELIX 138..164
FT /evidence="ECO:0007829|PDB:3IA2"
FT HELIX 166..168
FT /evidence="ECO:0007829|PDB:3IA2"
FT HELIX 174..186
FT /evidence="ECO:0007829|PDB:3IA2"
FT HELIX 189..201
FT /evidence="ECO:0007829|PDB:3IA2"
FT HELIX 205..208
FT /evidence="ECO:0007829|PDB:3IA2"
FT STRAND 215..220
FT /evidence="ECO:0007829|PDB:3IA2"
FT STRAND 224..226
FT /evidence="ECO:0007829|PDB:3IA2"
FT HELIX 228..230
FT /evidence="ECO:0007829|PDB:3IA2"
FT HELIX 232..238
FT /evidence="ECO:0007829|PDB:3IA2"
FT STRAND 243..247
FT /evidence="ECO:0007829|PDB:3IA2"
FT HELIX 254..257
FT /evidence="ECO:0007829|PDB:3IA2"
FT HELIX 259..270
FT /evidence="ECO:0007829|PDB:3IA2"
SQ SEQUENCE 272 AA; 30092 MW; 92E3D1ADBDBE0135 CRC64;
MSTFVAKDGT QIYFKDWGSG KPVLFSHGWL LDADMWEYQM EYLSSRGYRT IAFDRRGFGR
SDQPWTGNDY DTFADDIAQL IEHLDLKEVT LVGFSMGGGD VARYIARHGS ARVAGLVLLG
AVTPLFGQKP DYPQGVPLDV FARFKTELLK DRAQFISDFN APFYGINKGQ VVSQGVQTQT
LQIALLASLK ATVDCVTAFA ETDFRPDMAK IDVPTLVIHG DGDQIVPFET TGKVAAELIK
GAELKVYKDA PHGFAVTHAQ QLNEDLLAFL KR
