| IED ID | IndEnz0010000814 |
| Enzyme Type ID | esterase000814 |
| Protein Name |
Bifunctional esterase/perhydrolase DCH 3,4-dihydrocoumarin hydrolase DCH EC 3.1.1.35 Metal-free haloperoxidase |
| Gene Name | dch |
| Organism | Acinetobacter calcoaceticus |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Moraxellales Moraxellaceae Acinetobacter Acinetobacter calcoaceticus/baumannii complex Acinetobacter calcoaceticus |
| Enzyme Sequence | MGYVTTKDGVDIFYKDWGPRDAPVIFFHHGWPLSSDDWDAQMLFFLKEGFRVVAHDRRGHGRSTQVWDGHDMDHYADDVAAVVEYLGVQGAVHVGHSTGGGEVAYYVARYPNDPVAKAVLISAVPPLMVKTESNPDGLPKEVFDDLQNQLFKNRSQFYHDVPAGPFYGFNRPGAKVSEPVVLNWWRQGMMGGAKAHYDGIVAFSQTDFTEALKKIEVPVLILHGEDDQVVPFEISGKKSAELVKNGKLISYPGFPHGMPTTEAETINKDLLAFIRS |
| Enzyme Length | 276 |
| Uniprot Accession Number | Q83WC8 |
| Absorption | |
| Active Site | ACT_SITE 97; /evidence=ECO:0000250|UniProtKB:P22862; ACT_SITE 227; /evidence=ECO:0000250|UniProtKB:P22862; ACT_SITE 256; /evidence=ECO:0000250|UniProtKB:P22862 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by the serine protease inhibitors diisopropyl fluorophosphate and phenylmethanesulfonyl fluoride. {ECO:0000269|PubMed:10601844}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=3,4-dihydrocoumarin + H2O = 3-(2-hydroxyphenyl)propanoate + H(+); Xref=Rhea:RHEA:10360, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16151, ChEBI:CHEBI:46957; EC=3.1.1.35; Evidence={ECO:0000269|PubMed:10601844, ECO:0000269|PubMed:12542698}; CATALYTIC ACTIVITY: Reaction=H2O + peracetic acid = acetate + H(+) + H2O2; Xref=Rhea:RHEA:68392, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16240, ChEBI:CHEBI:30089, ChEBI:CHEBI:42530; Evidence={ECO:0000269|PubMed:12542698}; CATALYTIC ACTIVITY: Reaction=a percarboxylic acid + H2O = a carboxylate + H(+) + H2O2; Xref=Rhea:RHEA:68396, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16240, ChEBI:CHEBI:29067, ChEBI:CHEBI:177878; Evidence={ECO:0000269|PubMed:12542698}; |
| DNA Binding | |
| EC Number | 3.1.1.35 |
| Enzyme Function | FUNCTION: Multifunctional enzyme, which shows esterase and perhydrolase activities, and is capable of organic acid-assisted bromination of organic compounds (PubMed:10601844, PubMed:12542698). Catalyzes the hydrolysis of 3,4-dihydrocoumarin (PubMed:10601844, PubMed:12542698). Aromatic lactones other than 3,4-dihydrocoumarin, such as 2-coumaranone and homogentisic acid lactone, are also substrates, but their activities relative to that of 3,4-dihydrocoumarin are quite low (PubMed:10601844). Also catalyzes the hydrolysis of several linear esters, with specificity toward methyl esters (PubMed:12436309). In addition, shows perhydrolase activity and catalyzes the dose- and time-dependent degradation of peracetic acid, a broad-spectrum biocide, to acetic acid and hydrogen peroxide (PubMed:12542698). It suggests that in vivo DCH may play a role in the oxidative stress defense system and detoxify peroxoacids in conjunction with the catalase, i.e. peroxoacids are first hydrolyzed to the corresponding acids and hydrogen peroxide by DCH, and then the resulting hydrogen peroxide is degraded by the catalase (PubMed:12542698). Also shows organic acid-assisted bromination activity toward monochlorodimedon when incubated with hydrogen peroxide and dihydrocoumarin or an organic acid, such as acetate and n-butyrate (PubMed:10601844, PubMed:12542698). {ECO:0000269|PubMed:10601844, ECO:0000269|PubMed:12436309, ECO:0000269|PubMed:12542698}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 30 degrees Celsius. Stable below 75 degrees Celsius, and retains 69% of the original activity at 80 degrees Celsius. {ECO:0000269|PubMed:10601844}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0-8.0. {ECO:0000269|PubMed:10601844}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Domain (1); Initiator methionine (1) |
| Keywords | Direct protein sequencing;Hydrolase |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 30,708 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.806 mM for 3,4-dihydrocoumarin {ECO:0000269|PubMed:10601844}; KM=0.390 mM for peracetic acid {ECO:0000269|PubMed:12542698}; KM=0.761 mM for 2-coumaranone {ECO:0000269|PubMed:10601844}; KM=0.560 mM for homogentisic acid gamma-lactone {ECO:0000269|PubMed:10601844}; KM=25.9 mM for methyl DL-beta-acetylthioisobutyrate (DL-MAT) {ECO:0000269|PubMed:12436309}; KM=54.1 mM for dimethyl (R)-methylsuccinate {ECO:0000269|PubMed:12436309}; KM=2.54 mM for methyl 3-(4-hydroxyphenyl)-propionate {ECO:0000269|PubMed:12436309}; KM=6.88 mM for methyl cetraxate hydrochloride {ECO:0000269|PubMed:12436309}; Vmax=4760 umol/min/mg enzyme with 3,4-dihydrocoumarin as substrate {ECO:0000269|PubMed:10601844}; Vmax=12600 umol/min/mg enzyme with peracetic acid as substrate {ECO:0000269|PubMed:12542698}; Vmax=8 umol/min/mg enzyme with 2-coumaranone as substrate {ECO:0000269|PubMed:10601844}; Vmax=0.96 umol/min/mg enzyme with homogentisic acid gamma-lactone as substrate {ECO:0000269|PubMed:10601844}; Vmax=1440 umol/min/mg enzyme with methyl DL-beta-acetylthioisobutyrate as substrate {ECO:0000269|PubMed:12436309}; Vmax=71.4 umol/min/mg enzyme with dimethyl (R)-methylsuccinate as substrate {ECO:0000269|PubMed:12436309}; Vmax=4.54 umol/min/mg enzyme with methyl 3-(4-hydroxyphenyl)-propionate as substrate {ECO:0000269|PubMed:12436309}; Vmax=185 umol/min/mg enzyme with methyl cetraxate hydrochloride as substrate {ECO:0000269|PubMed:12436309}; |
| Metal Binding | |
| Rhea ID | RHEA:10360; RHEA:68392; RHEA:68396 |
| Cross Reference Brenda | 3.1.1.35; |