| IED ID | IndEnz0010000704 |
| Enzyme Type ID | esterase000704 |
| Protein Name |
Thermostable monoacylglycerol lipase MGLP bMGL EC 3.1.1.23 |
| Gene Name | |
| Organism | Bacillus sp. (strain H-257) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Bacillaceae Bacillus unclassified Bacillus (in: Bacteria) Bacillus sp. (strain H-257) |
| Enzyme Sequence | MSEQYPVLSGAEPFYAENGPVGVLLVHGFTGTPHSMRPLAEAYAKAGYTVCLPRLKGHGTHYEDMERTTFHDWVASVEEGYGWLKQRCQTIFVTGLSMGGTLTLYLAEHHPDICGIVPINAAVDIPAIAAGMTGGGELPRYLDSIGSDLKNPDVKELAYEKTPTASLLQLARLMAQTKAKLDRIVCPALIFVSDEDHVVPPGNADIIFQGISSTEKEIVRLRNSYHVATLDYDQPMIIERSLEFFAKHAG |
| Enzyme Length | 250 |
| Uniprot Accession Number | P82597 |
| Absorption | |
| Active Site | ACT_SITE 97; /note=Nucleophile; ACT_SITE 196; /note=Charge relay system; ACT_SITE 226; /note=Charge relay system |
| Activity Regulation | ACTIVITY REGULATION: Not inhibited by cholate, but slightly inhibited by triton X-100 and deoxycholate. Completely inhibited by PMSF (phenylmethylsulfonyl fluoride) at a concentration of 200 uM. {ECO:0000269|PubMed:10731713, ECO:0000269|PubMed:22561231}. |
| Binding Site | BINDING 29; /note=Substrate; via amide nitrogen; BINDING 98; /note=Substrate; via amide nitrogen |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Hydrolyzes glycerol monoesters of long-chain fatty acids.; EC=3.1.1.23; Evidence={ECO:0000269|PubMed:10731713, ECO:0000269|PubMed:22561231, ECO:0000269|PubMed:24014019}; |
| DNA Binding | |
| EC Number | 3.1.1.23 |
| Enzyme Function | FUNCTION: Hydrolyzes monoacylglycerols, with the highest activity occurring with 1-monolauroylglycerol. {ECO:0000269|PubMed:10731713}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 75 degrees Celsius.; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6-8.; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Beta strand (12); Binding site (2); Chain (1); Helix (11); Initiator methionine (1); Mutagenesis (3); Site (1) |
| Keywords | 3D-structure;Direct protein sequencing;Hydrolase;Serine esterase |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (8) |
| Cross Reference PDB | 3RLI; 3RM3; 4KE6; 4KE7; 4KE8; 4KE9; 4KEA; 4LHE; |
| Mapped Pubmed ID | 24894647; |
| Motif | |
| Gene Encoded By | |
| Mass | 27,359 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.1.1.23; |