| IED ID | IndEnz0005000624 |
| Enzyme Type ID | lipase000624 |
| Protein Name |
Mono- and diacylglycerol lipase MDGL EC 3.1.1.- |
| Gene Name | mdlA |
| Organism | Penicillium camembertii |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Aspergillaceae Penicillium Penicillium camembertii |
| Enzyme Sequence | MRLSFFTALSAVASLGYALPGKLQSRDVSTSELDQFEFWVQYAAASYYEADYTAQVGDKLSCSKGNCPEVEATGATVSYDFSDSTITDTAGYIAVDHTNSAVVLAFRGSYSVRNWVADATFVHTNPGLCDGCLAELGFWSSWKLVRDDIIKELKEVVAQNPNYELVVVGHSLGAAVATLAATDLRGKGYPSAKLYAYASPRVGNAALAKYITAQGNNFRFTHTNDPVPKLPLLSMGYVHVSPEYWITSPNNATVSTSDIKVIDGDVSFDGNTGTGLPLLTDFEAHIWYFVQVDAGKGPGLPFKRV |
| Enzyme Length | 305 |
| Uniprot Accession Number | P61870 |
| Absorption | |
| Active Site | ACT_SITE 171; /note=Nucleophile; /evidence=ECO:0000305|PubMed:7656005; ACT_SITE 225; /note=Charge relay system; /evidence=ECO:0000305|PubMed:7656005; ACT_SITE 285; /note=Charge relay system; /evidence=ECO:0000305|PubMed:7656005 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.1.1.- |
| Enzyme Function | FUNCTION: Hydrolyzes mono- and diacylglycerol but not triacylglycerol. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Disulfide bond (2); Glycosylation (1); Propeptide (1); Sequence conflict (1); Signal peptide (1) |
| Keywords | 3D-structure;Direct protein sequencing;Disulfide bond;Glycoprotein;Hydrolase;Lipid degradation;Lipid metabolism;Signal;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | PTM: Multiple forms of this lipase are due to the presence of different carbohydrates, which may contribute to the stability of this lipase but not to the enzyme activity. |
| Signal Peptide | SIGNAL 1..26; /evidence="ECO:0000269|PubMed:1879699, ECO:0000269|PubMed:8458423" |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 1TIA; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 32,948 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |