Detail Information for IndEnz0005000624
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