Detail Information for IndEnz0005000929
IED ID IndEnz0005000929
Enzyme Type ID lipase000929
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;