| IED ID | IndEnz0005000673 |
| Enzyme Type ID | lipase000673 |
| Protein Name |
Monoterpene epsilon-lactone hydrolase EC 3.1.1.83 |
| Gene Name | mlhB |
| Organism | Rhodococcus erythropolis (Arthrobacter picolinophilus) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Actinobacteria Actinomycetia (high G+C Gram-positive bacteria) Corynebacteriales Nocardiaceae Rhodococcus Rhodococcus erythropolis group Rhodococcus erythropolis (Arthrobacter picolinophilus) |
| Enzyme Sequence | MSATDTARAKELLASLVSMPDATIDDFRALYEQVCATFELPDDAQVEPVDANGADALWVSAPGVSADTVAVVVHGGGFTMGSAHGYRELGYRLSKSGNLRALVVDYRLAPESPFPAPVDDVVAAYRYARSLDGVENVFLVGDSAGGGIAMSALITLRDAGEQLPDAAVVLSPLVDLAGESPSLVDRAHLDPLPAAVLVNGMGGLYLNGLDVRHPVASPMHGDLTGLPATLVLVGTDEGLHDDSTRLVDKLKAADVEVQLEIGEGLPHIWPIFSFHPDAVAATDRIGEFLRSHVAAPR |
| Enzyme Length | 297 |
| Uniprot Accession Number | Q9EX73 |
| Absorption | |
| Active Site | ACT_SITE 143; /evidence=ECO:0000250|UniProtKB:O06350; ACT_SITE 237; /evidence=ECO:0000250|UniProtKB:O06350; ACT_SITE 267; /evidence=ECO:0000250|UniProtKB:O06350 |
| Activity Regulation | ACTIVITY REGULATION: Strongly inhibited by the imidazole-modifying compound 2-bromo-4'-nitroacetophenone, by HgCl(2) and CoCl(2). Not inhibited by the thiol reagents iodoacetate and dithiothreitol. {ECO:0000269|PubMed:11157238}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=4-isopropenyl-7-methyloxepan-2-one + H2O = 6-hydroxy-3-isopropenylheptanoate + H(+); Xref=Rhea:RHEA:32507, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:50238, ChEBI:CHEBI:64224; EC=3.1.1.83; Evidence={ECO:0000269|PubMed:11157238}; CATALYTIC ACTIVITY: Reaction=7-isopropyl-4-methyloxepan-2-one + H2O = 6-hydroxy-3,7-dimethyloctanoate + H(+); Xref=Rhea:RHEA:32595, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:50243, ChEBI:CHEBI:64223; EC=3.1.1.83; Evidence={ECO:0000269|PubMed:11157238}; |
| DNA Binding | |
| EC Number | 3.1.1.83 |
| Enzyme Function | FUNCTION: Lactone hydrolase that is required for the degradation of monocyclic monoterpenes such as menthol and carvone. Catalyzes the ring opening of lactones formed during degradation of monocyclic monoterpenes. Can hydrolyze epsilon-caprolactone, the lactone derivatives of dihydrocarvone (4R)-4-isopropenyl-7-methyl-2-oxo-oxepanone and (6R)-6-isopropenyl-3-methyl-2-oxo-oxepanone, and ethyl caproate. {ECO:0000269|PubMed:11157238}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 30 degrees Celsius. Inactivated above 40 degrees Celsius. {ECO:0000269|PubMed:11157238}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 9.5. {ECO:0000269|PubMed:11157238}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Initiator methionine (1); Motif (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 | MOTIF 74..76; /note=Involved in the stabilization of the negatively charged intermediate by the formation of the oxyanion hole; /evidence=ECO:0000250|UniProtKB:Q5NUF3 |
| Gene Encoded By | |
| Mass | 31,134 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:32507; RHEA:32595 |
| Cross Reference Brenda |