| IED ID | IndEnz0010000090 |
| Enzyme Type ID | esterase000090 |
| Protein Name |
Esterase EstB EC 3.1.1.- |
| Gene Name | estB |
| Organism | Burkholderia gladioli (Pseudomonas marginata) (Phytomonas marginata) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Betaproteobacteria Burkholderiales Burkholderiaceae Burkholderia Burkholderia gladioli (Pseudomonas marginata) (Phytomonas marginata) |
| Enzyme Sequence | MTAASLDPTAFSLDAASLAARLDAVFDQALRERRLVGAVAIVARHGEILYRRAQGLADREAGRPMREDTLFRLASVTKPIVALAVLRLVARGELALDAPVTRWLPEFRPRLADGSEPLVTIHHLLTHTSGLGYWLLEGAGSVYDRLGISDGIDLRDFDLDENLRRLASAPLSFAPGSGWQYSLALDVLGAVVERATGQPLAAAVDALVAQPLGMRDCGFVSAEPERFAVPYHDGQPEPVRMRDGIEVPLPEGHGAAVRFAPSRVFEPGAYPSGGAGMYGSADDVLRALEAIRANPGFLPETLADAARRDQAGVGAETRGPGWGFGYLSAVLDDPAAAGTPQHAGTLQWGGVYGHSWFVDRALGLSVLLLTNTAYEGMSGPLTIALRDAVYAR |
| Enzyme Length | 392 |
| Uniprot Accession Number | Q9KX40 |
| Absorption | |
| Active Site | ACT_SITE 75; /note=Acyl-ester intermediate |
| Activity Regulation | ACTIVITY REGULATION: Strongly inhibited by eserin, NaF, HgCl2, SDS and Triton X-100. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.1.1.- |
| Enzyme Function | FUNCTION: Acts on short-chain (C4-C6) fatty acid esters and triglycerides, including tertiary alcohol esters. Activity on p-nitrophenyl esters is generally higher than on o-nitrophenyl esters. Lacks beta-lactamase activity; it hydrolyzes the ester bond of cephalosporin substrates but there is no opening of the beta-lactam ring observed. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 43 degrees Celsius.; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0.; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Beta strand (13); Chain (1); Helix (20); Mutagenesis (2); Turn (3) |
| Keywords | 3D-structure;Cytoplasm;Hydrolase |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (2) |
| Cross Reference PDB | 1CI8; 1CI9; |
| Mapped Pubmed ID | 15299891; |
| Motif | |
| Gene Encoded By | |
| Mass | 41,707 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.3 mM for cephalosporin C; KM=1.0 mM for 7-amino cephalosporinic acid; Vmax=79 umol/min/mg enzyme for cephalosporin C; Vmax=77 umol/min/mg enzyme for 7-amino cephalosporinic acid; Note=Esterase, not beta-lactamase activity of the enzyme.; |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |