ARE_SACSO
ID ARE_SACSO Reviewed; 306 AA.
AC B5BLW5;
DT 17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 34.
DE RecName: Full=Arylesterase {ECO:0000303|PubMed:18931117};
DE Short=A-esterase {ECO:0000303|PubMed:18931117};
DE EC=3.1.1.2 {ECO:0000269|PubMed:18931117};
DE AltName: Full=Paraoxonase {ECO:0000303|PubMed:18931117};
DE EC=3.1.8.1 {ECO:0000269|PubMed:18931117};
GN Name=are {ECO:0000303|PubMed:18931117};
OS Saccharolobus solfataricus (Sulfolobus solfataricus).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Saccharolobus.
OX NCBI_TaxID=2287 {ECO:0000312|EMBL:CAR57941.1};
RN [1] {ECO:0000312|EMBL:CAR57941.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 14-20, FUNCTION,
RP CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES,
RP SUBSTRATE SPECIFICITY, SUBUNIT, MASS SPECTROMETRY, AND MUTAGENESIS OF
RP CYS-105; CYS-107; CYS-129; SER-156; ASP-251 AND HIS-281.
RC STRAIN=ATCC 35091 / DSM 1616 / JCM 8930 / NBRC 15331 / P1
RC {ECO:0000303|PubMed:18931117};
RX PubMed=18931117; DOI=10.1128/jb.00803-08;
RA Park Y.J., Yoon S.J., Lee H.B.;
RT "A novel thermostable arylesterase from the archaeon Sulfolobus
RT solfataricus P1: purification, characterization, and expression.";
RL J. Bacteriol. 190:8086-8095(2008).
CC -!- FUNCTION: Has a broad substrate specificity. Hydrolyzes various p-
CC nitrophenyl phosphates, aromatic esters and p-nitrophenyl fatty acids
CC in vitro. Most active against paraoxon, phenyl acetate and p-
CC nitrophenyl caproate (C6), respectively. Has also tributyrinase
CC activity, but shows no hydrolytic activity toward other
CC triacylglycerols including tricaprylin, trimyristin, tripalmitin or
CC triolein in vitro. {ECO:0000269|PubMed:18931117}.
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:18931117};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=An aryl dialkyl phosphate + H2O = dialkyl phosphate + an aryl
CC alcohol.; EC=3.1.8.1; Evidence={ECO:0000269|PubMed:18931117};
CC -!- ACTIVITY REGULATION: Completely inhibited by chemical modifiers that
CC are specific to Cys (HgCl(2) and p-chloromercuribenzoic acid), His
CC (diethyl pyrocarbonate) and Ser (diisopropyl fluorophosphate and
CC phenylmethanesulfonyl fluoride). No significant effect with chemical
CC modifiers specific to Lys (pyridoxal 5'-phosphate) and Arg
CC (phenylglyoxal). Not inhibited by inhibitors of A-esterases (paraoxon)
CC or C-esterases (physostigmine/eserine). Activity is also not effected
CC by incubation with 5 mM divalent cations for 30 minutes at 30 degrees
CC Celsius or with 10 mM EDTA for 60 minutes at 75 degrees Celsius.
CC {ECO:0000269|PubMed:18931117}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=17 uM for phenyl acetate (PA) {ECO:0000269|PubMed:18931117};
CC KM=29 uM for alpha-naphthyl acetate (alpha-NA)
CC {ECO:0000269|PubMed:18931117};
CC KM=224 uM for p-nitrophenyl butyrate (C4)
CC {ECO:0000269|PubMed:18931117};
CC KM=31 uM for p-nitrophenyl caproate (C6)
CC {ECO:0000269|PubMed:18931117};
CC KM=28 uM for p-nitrophenyl caprylate (C8)
CC {ECO:0000269|PubMed:18931117};
CC KM=81 uM for p-nitrophenyl caprate (C10)
CC {ECO:0000269|PubMed:18931117};
CC KM=122 uM for p-nitrophenyl laurate (C12)
CC {ECO:0000269|PubMed:18931117};
CC KM=276 uM for p-nitrophenyl palmitate (C16)
CC {ECO:0000269|PubMed:18931117};
CC KM=234 uM for p-nitrophenyl phosphate {ECO:0000269|PubMed:18931117};
CC KM=5 uM for paraoxon {ECO:0000269|PubMed:18931117};
CC KM=246 uM for methyl paraoxon {ECO:0000269|PubMed:18931117};
CC Note=kcat is 521 sec(-1) with PA as substrate. kcat is 450 sec(-1)
CC with alpha-NA as substrate. kcat is 285 sec(-1) with p-nitrophenyl
CC butyrate (C4) as substrate. kcat is 467 sec(-1) with p-nitrophenyl
CC caproate (C6) as substrate. kcat is 410 sec(-1) with p-nitrophenyl
CC caprylate (C8) as substrate. kcat is 341 sec(-1) with p-nitrophenyl
CC caprate (C10) as substrate. kcat is 264 sec(-1) with p-nitrophenyl
CC laurate (C12) as substrate. kcat is 265 sec(-1) with p-nitrophenyl
CC palmitate (C16) as substrate. kcat is 269 sec(-1) with p-nitrophenyl
CC phosphate as substrate. kcat is 597 sec(-1) with paraoxon as
CC substrate. kcat is 342 sec(-1) with methyl paraoxon as substrate.
CC {ECO:0000269|PubMed:18931117};
CC pH dependence:
CC Optimum pH is 7.0. {ECO:0000269|PubMed:18931117};
CC Temperature dependence:
CC Optimum temperature is 94 degrees Celsius. Very thermostable, but
CC rapidly inactivated above 94 degrees Celsius. Most of the activity is
CC retained for 5 days at 50 degrees Celsius, and approximately 70% of
CC the activity is retained after 5 days at 70 degrees Celsius. 52% of
CC the activity is still retained after 50 hours at 90 degrees Celsius,
CC but completely inactivated after 5 days at 90 degrees Celsius.
CC {ECO:0000269|PubMed:18931117};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:18931117}.
CC -!- MASS SPECTROMETRY: Mass=35174.88; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:18931117};
CC -!- SIMILARITY: Belongs to the 'GDXG' lipolytic enzyme family.
CC {ECO:0000305}.
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DR EMBL; FM205057; CAR57941.1; -; Genomic_DNA.
DR PDB; 5L2P; X-ray; 2.56 A; A/B/C/D=1-306.
DR PDBsum; 5L2P; -.
DR AlphaFoldDB; B5BLW5; -.
DR SMR; B5BLW5; -.
DR ESTHER; sulac-q4j9s2; Hormone-sensitive_lipase_like.
DR BioCyc; MetaCyc:MON-20863; -.
DR BRENDA; 3.1.1.2; 6163.
DR BRENDA; 3.1.8.1; 6163.
DR GO; GO:0004063; F:aryldialkylphosphatase activity; IDA:UniProtKB.
DR GO; GO:0004064; F:arylesterase activity; IDA:UniProtKB.
DR GO; GO:0019439; P:aromatic compound catabolic process; IDA:UniProtKB.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR013094; AB_hydrolase_3.
DR Pfam; PF07859; Abhydrolase_3; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Hydrolase; Serine esterase.
FT CHAIN 1..306
FT /note="Arylesterase"
FT /id="PRO_0000435565"
FT MOTIF 82..84
FT /note="Involved in the stabilization of the negatively
FT charged intermediate by the formation of the oxyanion hole"
FT /evidence="ECO:0000250|UniProtKB:Q5NUF3"
FT ACT_SITE 156
FT /evidence="ECO:0000305|PubMed:18931117"
FT ACT_SITE 251
FT /evidence="ECO:0000305|PubMed:18931117"
FT ACT_SITE 281
FT /evidence="ECO:0000305|PubMed:18931117"
FT MUTAGEN 105
FT /note="C->S: 3-fold loss of activity compared to wild-
FT type."
FT /evidence="ECO:0000269|PubMed:18931117"
FT MUTAGEN 107
FT /note="C->S: 4-fold loss of activity compared to wild-
FT type."
FT /evidence="ECO:0000269|PubMed:18931117"
FT MUTAGEN 129
FT /note="C->S: 28-fold loss of activity compared to wild-
FT type."
FT /evidence="ECO:0000269|PubMed:18931117"
FT MUTAGEN 156
FT /note="S->A: Nearly loss of activity."
FT /evidence="ECO:0000269|PubMed:18931117"
FT MUTAGEN 251
FT /note="D->N: Nearly loss of activity."
FT /evidence="ECO:0000269|PubMed:18931117"
FT MUTAGEN 281
FT /note="H->N: 5-fold loss of activity compared to wild-
FT type."
FT /evidence="ECO:0000269|PubMed:18931117"
FT HELIX 5..17
FT /evidence="ECO:0007829|PDB:5L2P"
FT TURN 22..24
FT /evidence="ECO:0007829|PDB:5L2P"
FT HELIX 27..39
FT /evidence="ECO:0007829|PDB:5L2P"
FT STRAND 48..56
FT /evidence="ECO:0007829|PDB:5L2P"
FT STRAND 61..68
FT /evidence="ECO:0007829|PDB:5L2P"
FT STRAND 77..81
FT /evidence="ECO:0007829|PDB:5L2P"
FT TURN 85..87
FT /evidence="ECO:0007829|PDB:5L2P"
FT TURN 91..94
FT /evidence="ECO:0007829|PDB:5L2P"
FT HELIX 95..105
FT /evidence="ECO:0007829|PDB:5L2P"
FT STRAND 107..112
FT /evidence="ECO:0007829|PDB:5L2P"
FT TURN 117..119
FT /evidence="ECO:0007829|PDB:5L2P"
FT HELIX 124..138
FT /evidence="ECO:0007829|PDB:5L2P"
FT HELIX 140..143
FT /evidence="ECO:0007829|PDB:5L2P"
FT STRAND 150..155
FT /evidence="ECO:0007829|PDB:5L2P"
FT HELIX 157..171
FT /evidence="ECO:0007829|PDB:5L2P"
FT STRAND 177..183
FT /evidence="ECO:0007829|PDB:5L2P"
FT HELIX 193..197
FT /evidence="ECO:0007829|PDB:5L2P"
FT STRAND 198..203
FT /evidence="ECO:0007829|PDB:5L2P"
FT STRAND 208..210
FT /evidence="ECO:0007829|PDB:5L2P"
FT HELIX 212..217
FT /evidence="ECO:0007829|PDB:5L2P"
FT HELIX 221..225
FT /evidence="ECO:0007829|PDB:5L2P"
FT TURN 227..229
FT /evidence="ECO:0007829|PDB:5L2P"
FT HELIX 231..233
FT /evidence="ECO:0007829|PDB:5L2P"
FT STRAND 242..250
FT /evidence="ECO:0007829|PDB:5L2P"
FT HELIX 254..266
FT /evidence="ECO:0007829|PDB:5L2P"
FT STRAND 271..280
FT /evidence="ECO:0007829|PDB:5L2P"
FT HELIX 281..283
FT /evidence="ECO:0007829|PDB:5L2P"
FT HELIX 287..305
FT /evidence="ECO:0007829|PDB:5L2P"
SQ SEQUENCE 306 AA; 34552 MW; 69DB277CFC26F24B CRC64;
MPLDPEVRNF LQVYYKANII DFTKYQFQEI RQKVNELLAK AVPKDPVGET RDMKIKLEDY
ELPIRIYSPI KRTNNGLVMH FHGGAWILGS IETEDAISRI LSNSCECTVI SVDYRLAPEY
KFPTAVYDCF NAIVWARDNA GELGIDKDKI ATFGISAGGN LVAATSLLAR DNKLKLTAQV
PVVPFVYLDL ASKSMNRYRK GYFLDINLPV DYGVKMYIRD EKDLYNPLFS PLIAEDLSNL
PQAIVVTAEY DPLRDQGEAY AYRLMESGVP TLSFRVNGNV HAFLGSPRTS RQVTVMIGAL
LKDIFK
