DCH_ACICA
ID DCH_ACICA Reviewed; 276 AA.
AC Q83WC8;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 23-FEB-2022, entry version 47.
DE RecName: Full=Bifunctional esterase/perhydrolase DCH {ECO:0000305};
DE AltName: Full=3,4-dihydrocoumarin hydrolase {ECO:0000303|PubMed:10601844};
DE Short=DCH {ECO:0000303|PubMed:12436309};
DE EC=3.1.1.35 {ECO:0000269|PubMed:10601844};
DE AltName: Full=Metal-free haloperoxidase {ECO:0000305};
GN Name=dch {ECO:0000303|PubMed:12542698};
OS Acinetobacter calcoaceticus.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX NCBI_TaxID=471;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND DISRUPTION PHENOTYPE.
RC STRAIN=F46;
RX PubMed=12542698; DOI=10.1046/j.1432-1033.2003.03407.x;
RA Honda K., Kataoka M., Sakuradani E., Shimizu S.;
RT "Role of Acinetobacter calcoaceticus 3,4-dihydrocoumarin hydrolase in
RT oxidative stress defence against peroxoacids.";
RL Eur. J. Biochem. 270:486-494(2003).
RN [2]
RP PROTEIN SEQUENCE OF 2-237; 239-244 AND 248-276, FUNCTION, CATALYTIC
RP ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC STRAIN=F46;
RX PubMed=10601844; DOI=10.1046/j.1432-1327.2000.00889.x;
RA Kataoka M., Honda K., Shimizu S.;
RT "3,4-Dihydrocoumarin hydrolase with haloperoxidase activity from
RT Acinetobacter calcoaceticus F46.";
RL Eur. J. Biochem. 267:3-10(2000).
RN [3]
RP FUNCTION IN LINEAR ESTERS HYDROLYSIS, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP BIOTECHNOLOGY.
RC STRAIN=F46;
RX PubMed=12436309; DOI=10.1007/s00253-002-1116-3;
RA Honda K., Kataoka M., Shimizu S.;
RT "Enzymatic preparation of D-beta-acetylthioisobutyric acid and cetraxate
RT hydrochloride using a stereo- and/or regioselective hydrolase, 3,4-
RT dihydrocoumarin hydrolase from Acinetobacter calcoaceticus.";
RL Appl. Microbiol. Biotechnol. 60:288-292(2002).
CC -!- FUNCTION: Multifunctional enzyme, which shows esterase and perhydrolase
CC activities, and is capable of organic acid-assisted bromination of
CC organic compounds (PubMed:10601844, PubMed:12542698). Catalyzes the
CC hydrolysis of 3,4-dihydrocoumarin (PubMed:10601844, PubMed:12542698).
CC Aromatic lactones other than 3,4-dihydrocoumarin, such as 2-coumaranone
CC and homogentisic acid lactone, are also substrates, but their
CC activities relative to that of 3,4-dihydrocoumarin are quite low
CC (PubMed:10601844). Also catalyzes the hydrolysis of several linear
CC esters, with specificity toward methyl esters (PubMed:12436309). In
CC addition, shows perhydrolase activity and catalyzes the dose- and time-
CC dependent degradation of peracetic acid, a broad-spectrum biocide, to
CC acetic acid and hydrogen peroxide (PubMed:12542698). It suggests that
CC in vivo DCH may play a role in the oxidative stress defense system and
CC detoxify peroxoacids in conjunction with the catalase, i.e. peroxoacids
CC are first hydrolyzed to the corresponding acids and hydrogen peroxide
CC by DCH, and then the resulting hydrogen peroxide is degraded by the
CC catalase (PubMed:12542698). Also shows organic acid-assisted
CC bromination activity toward monochlorodimedon when incubated with
CC hydrogen peroxide and dihydrocoumarin or an organic acid, such as
CC acetate and n-butyrate (PubMed:10601844, PubMed:12542698).
CC {ECO:0000269|PubMed:10601844, ECO:0000269|PubMed:12436309,
CC ECO:0000269|PubMed:12542698}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3,4-dihydrocoumarin + H2O = 3-(2-hydroxyphenyl)propanoate +
CC H(+); Xref=Rhea:RHEA:10360, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16151, ChEBI:CHEBI:46957; EC=3.1.1.35;
CC Evidence={ECO:0000269|PubMed:10601844, ECO:0000269|PubMed:12542698};
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:12542698};
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:12542698};
CC -!- ACTIVITY REGULATION: Inhibited by the serine protease inhibitors
CC diisopropyl fluorophosphate and phenylmethanesulfonyl fluoride.
CC {ECO:0000269|PubMed:10601844}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.806 mM for 3,4-dihydrocoumarin {ECO:0000269|PubMed:10601844};
CC KM=0.390 mM for peracetic acid {ECO:0000269|PubMed:12542698};
CC KM=0.761 mM for 2-coumaranone {ECO:0000269|PubMed:10601844};
CC KM=0.560 mM for homogentisic acid gamma-lactone
CC {ECO:0000269|PubMed:10601844};
CC KM=25.9 mM for methyl DL-beta-acetylthioisobutyrate (DL-MAT)
CC {ECO:0000269|PubMed:12436309};
CC KM=54.1 mM for dimethyl (R)-methylsuccinate
CC {ECO:0000269|PubMed:12436309};
CC KM=2.54 mM for methyl 3-(4-hydroxyphenyl)-propionate
CC {ECO:0000269|PubMed:12436309};
CC KM=6.88 mM for methyl cetraxate hydrochloride
CC {ECO:0000269|PubMed:12436309};
CC Vmax=4760 umol/min/mg enzyme with 3,4-dihydrocoumarin as substrate
CC {ECO:0000269|PubMed:10601844};
CC Vmax=12600 umol/min/mg enzyme with peracetic acid as substrate
CC {ECO:0000269|PubMed:12542698};
CC Vmax=8 umol/min/mg enzyme with 2-coumaranone as substrate
CC {ECO:0000269|PubMed:10601844};
CC Vmax=0.96 umol/min/mg enzyme with homogentisic acid gamma-lactone as
CC substrate {ECO:0000269|PubMed:10601844};
CC Vmax=1440 umol/min/mg enzyme with methyl DL-beta-
CC acetylthioisobutyrate as substrate {ECO:0000269|PubMed:12436309};
CC Vmax=71.4 umol/min/mg enzyme with dimethyl (R)-methylsuccinate as
CC substrate {ECO:0000269|PubMed:12436309};
CC Vmax=4.54 umol/min/mg enzyme with methyl 3-(4-hydroxyphenyl)-
CC propionate as substrate {ECO:0000269|PubMed:12436309};
CC Vmax=185 umol/min/mg enzyme with methyl cetraxate hydrochloride as
CC substrate {ECO:0000269|PubMed:12436309};
CC pH dependence:
CC Optimum pH is 7.0-8.0. {ECO:0000269|PubMed:10601844};
CC Temperature dependence:
CC Optimum temperature is 30 degrees Celsius. Stable below 75 degrees
CC Celsius, and retains 69% of the original activity at 80 degrees
CC Celsius. {ECO:0000269|PubMed:10601844};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:10601844}.
CC -!- DISRUPTION PHENOTYPE: Disruption mutant is more sensitive to growth
CC inhibition by peracetic acid than the parent strain. The sensitivities
CC to hydrogen peroxide and acetic acid are not affected.
CC {ECO:0000269|PubMed:12542698}.
CC -!- BIOTECHNOLOGY: Can convert substrates at high concentrations to
CC desirable products in a short time. Thus, DCH exhibits significant
CC hydrolysis activity, with stereo and/or regioselectivity, toward the
CC methyl esters of bacetylthioisobutyrate and cetraxate, and is expected
CC to be applicable to the practical synthesis of these compounds.
CC {ECO:0000269|PubMed:12436309}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Bacterial non-heme
CC haloperoxidase / perhydrolase family. {ECO:0000305}.
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DR EMBL; AB092339; BAC55927.1; -; Genomic_DNA.
DR SMR; Q83WC8; -.
DR ESTHER; acica-DCH; Haloperoxidase.
DR BRENDA; 3.1.1.35; 99.
DR GO; GO:0018733; F:3,4-dihydrocoumarin hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0047856; F:dihydrocoumarin hydrolase activity; IEA:UniProtKB-EC.
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 Direct protein sequencing; Hydrolase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:10601844"
FT CHAIN 2..276
FT /note="Bifunctional esterase/perhydrolase DCH"
FT /id="PRO_0000453900"
FT DOMAIN 23..254
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255"
FT ACT_SITE 97
FT /evidence="ECO:0000250|UniProtKB:P22862"
FT ACT_SITE 227
FT /evidence="ECO:0000250|UniProtKB:P22862"
FT ACT_SITE 256
FT /evidence="ECO:0000250|UniProtKB:P22862"
SQ SEQUENCE 276 AA; 30708 MW; 3A90646583402D37 CRC64;
MGYVTTKDGV DIFYKDWGPR DAPVIFFHHG WPLSSDDWDA QMLFFLKEGF RVVAHDRRGH
GRSTQVWDGH DMDHYADDVA AVVEYLGVQG AVHVGHSTGG GEVAYYVARY PNDPVAKAVL
ISAVPPLMVK TESNPDGLPK EVFDDLQNQL FKNRSQFYHD VPAGPFYGFN RPGAKVSEPV
VLNWWRQGMM GGAKAHYDGI VAFSQTDFTE ALKKIEVPVL ILHGEDDQVV PFEISGKKSA
ELVKNGKLIS YPGFPHGMPT TEAETINKDL LAFIRS
