| IED ID | IndEnz0010000978 |
| Enzyme Type ID | esterase000978 |
| Protein Name |
Lovastatin esterase PcEST EC 3.1.1.- |
| Gene Name | PcEST Pc15g00720 PCH_Pc15g00720 |
| Organism | Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255) (Penicillium chrysogenum) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Aspergillaceae Penicillium Penicillium chrysogenum species complex Penicillium rubens Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255) (Penicillium chrysogenum) |
| Enzyme Sequence | MDTTFQAAIDTGKINGAVVCATDAQGHFVYNKATGERTLLSGEKQPQQLDDVLYLASATKLITTIAALQCVEDGLLSLDGDLSSIAPELAAKYVLTGFTDDESPLDDPPARPITLKMLLTHSSGTSYHFLDPSIAKWRAQYANPENEKPRLVEEMFTYPLSFQPGTGWMYGPGLDWAGRVVERVTGGTLMEFMQKRIFDPLGITDSQFYPVTREDLRARLVDLNPSDPGALGSAVIGGGGEMNLRGRGAFGGHGLFLTGLDFVKILRSLLANDGMLLKPAAVDNMFQQHLGPEAAASHRAALASPLGPFFRVGTDPETKVGYGLGGLLTLEDVDGWYGERTLTWGGGLTLTWFIDRKNNLCGVGAIQAVLPVDGDLMADLKQTFRHDIYRKYSAWKGQQ |
| Enzyme Length | 399 |
| Uniprot Accession Number | B6H6L7 |
| Absorption | |
| Active Site | ACT_SITE 57; /note=Nucleophile; /evidence=ECO:0000269|PubMed:31839596; ACT_SITE 60; /note=Proton acceptor; /evidence=ECO:0000269|PubMed:31839596; ACT_SITE 170; /note=Proton acceptor; /evidence=ECO:0000269|PubMed:31839596 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=H2O + lovastatin = (S)-2-methylbutanoate + H(+) + monacolin J; Xref=Rhea:RHEA:62748, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:40303, ChEBI:CHEBI:79034, ChEBI:CHEBI:145932; Evidence={ECO:0000269|PubMed:28619444};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62749; Evidence={ECO:0000269|PubMed:28619444}; CATALYTIC ACTIVITY: Reaction=H2O + pravastatin lactone = (S)-2-methylbutanoate + H(+) + pravastatin diol lactone; Xref=Rhea:RHEA:62752, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:145931, ChEBI:CHEBI:145932, ChEBI:CHEBI:145933; Evidence={ECO:0000269|PubMed:28619444};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62753; Evidence={ECO:0000269|PubMed:28619444}; CATALYTIC ACTIVITY: Reaction=H2O + mevastatin = (S)-2-methylbutanoate + compactin diol lactone + H(+); Xref=Rhea:RHEA:62744, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:34652, ChEBI:CHEBI:34848, ChEBI:CHEBI:145932; Evidence={ECO:0000269|PubMed:28619444};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62745; Evidence={ECO:0000269|PubMed:28619444}; |
| DNA Binding | |
| EC Number | 3.1.1.- |
| Enzyme Function | FUNCTION: Esterase that can hydrolyze the side chain of lovastatin to produce monacolin J (PubMed:28619444, PubMed:31839596). Is also able to hydrolyze the side chains of mevastatin and pravastatin, but not simvastatin (PubMed:28619444). {ECO:0000269|PubMed:28619444, ECO:0000269|PubMed:31839596}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Beta strand (16); Chain (1); Helix (17); Mutagenesis (7); Turn (6) |
| Keywords | 3D-structure;Hydrolase;Reference proteome |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (4) |
| Cross Reference PDB | 6KJC; 6KJD; 6KJE; 6KJF; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 43,292 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=39.4 uM for lovastatin (at 37 degrees Celsius) {ECO:0000269|PubMed:28619444}; KM=5.46 uM for lovastatin (at 30 degrees Celsius) {ECO:0000269|PubMed:31839596}; |
| Metal Binding | |
| Rhea ID | RHEA:62748; RHEA:62749; RHEA:62752; RHEA:62753; RHEA:62744; RHEA:62745 |
| Cross Reference Brenda |