| IED ID | IndEnz0010000784 |
| Enzyme Type ID | esterase000784 |
| Protein Name |
Monoalkyl phthalate esterase EC 3.1.1.- Fragment |
| Gene Name | |
| Organism | Micrococcus sp. |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Actinobacteria Actinomycetia (high G+C Gram-positive bacteria) Micrococcales Micrococcaceae Micrococcus unclassified Micrococcus Micrococcus sp. |
| Enzyme Sequence | SATAAREEYQRKRSQFIEIG |
| Enzyme Length | 20 |
| Uniprot Accession Number | P84812 |
| Absorption | BIOPHYSICOCHEMICAL PROPERTIES: Absorption: Abs(max)=280 nm {ECO:0000269|PubMed:15713880}; Note=Exhibits a smaller absorbance peak at 290 nm and a minimum at 250 nm. No significant absorption in the visible spectrum. {ECO:0000269|PubMed:15713880}; |
| Active Site | |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by diethylpyrocarbonate, p-chloromercuribenzoate, Hg(2+) and Cu(2+). Not inhibited by the chelating reagents EDTA, 2,2'-dipyridyl, 1,10-phenanthroline, 8-hydroxyquinoline and tiron. {ECO:0000269|PubMed:15713880}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.1.1.- |
| Enzyme Function | FUNCTION: Probably involved in the metabolism of xenobiotics and of natural substrates. Hydrolyzes medium-chain monoalkyl phthalate esters. {ECO:0000269|PubMed:15713880}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 40 degrees Celsius with monobutyl phthalate as substrate. {ECO:0000269|PubMed:15713880}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5 with monobutyl phthalate as substrate. Retains 50% of maximum activity between pH 6.5 and pH 7.8. {ECO:0000269|PubMed:15713880}; |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Non-terminal residue (1) |
| Keywords | Direct protein sequencing;Hydrolase |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | PTM: Exists in two forms, E1 and E2. E2 is probably produced by modification of E1. {ECO:0000269|PubMed:15713880}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 2,341 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |