| IED ID | IndEnz0005000153 |
| Enzyme Type ID | lipase000153 |
| Protein Name |
Lipase 2 EC 3.1.1.3 GCL II Lipase II |
| Gene Name | LIP2 |
| Organism | Geotrichum candidum (Oospora lactis) (Dipodascus geotrichum) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Saccharomycotina (true yeasts) Saccharomycetes Saccharomycetales Dipodascaceae Geotrichum Geotrichum candidum (Oospora lactis) (Dipodascus geotrichum) |
| Enzyme Sequence | MVSKSLFLAAAVNLAGVLAQAPRPSLNGNEVISGVLEGKVDTFKGIPFADPPLNDLRFKHPQPFTGSYQGLKANDFSPACMQLDPGNSLTLLDKALGLAKVIPEEFRGPLYDMAKGTVSMNEDCLYLNVFRPAGTKPDAKLPVMVWIYGGAFVYGSSAAYPGNSYVKESINMGQPVVFVSINYRTGPFGFLGGDAITAEGNTNAGLHDQRKGLEWVSDNIANFGGDPDKVMIFGESAGAMSVAHQLIAYGGDNTYNGKKLFHSAILQSGGPLPYHDSSSVGPDISYNRFAQYAGCDTSASANDTLECLRSKSSSVLHDAQNSYDLKDLFGLLPQFLGFGPRPDGNIIPDAAYELFRSGRYAKVPYISGNQEDEGTAFAPVALNATTTPHVKKWLQYIFYDASEASIDRVLSLYPQTLSVGSPFRTGILNALTPQFKRVAAILSDMLFQSPRRVMLSATKDVNRWTYLSTHLHNLVPFLGTFHGNELIFQFNVNIGPANSYLRYFISFANHHDPNVGTNLLQWDQYTDEGKEMLEIHMTDNVMRTDDYRIEGISNFETDVNLYG |
| Enzyme Length | 563 |
| Uniprot Accession Number | P22394 |
| Absorption | |
| Active Site | ACT_SITE 236; /note=Acyl-ester intermediate; ACT_SITE 373; /note=Charge relay system; ACT_SITE 482; /note=Charge relay system |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=a triacylglycerol + H2O = a diacylglycerol + a fatty acid + H(+); Xref=Rhea:RHEA:12044, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17855, ChEBI:CHEBI:18035, ChEBI:CHEBI:28868; EC=3.1.1.3; |
| DNA Binding | |
| EC Number | 3.1.1.3 |
| Enzyme Function | FUNCTION: Hydrolyzes all ester bonds in triglyceride and displays a high affinity for triolein. For unsaturated substrates having long fatty acyl chains (C18:2 cis-9, cis-12 and C18:3 cis-9, cis-12, cis-15) GCL I shows higher specific activity than GCL II, whereas GCL II shows higher specific activity against saturated substrates having short fatty acid chains (C8, C10, C12 and C14). |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Beta strand (20); Chain (1); Disulfide bond (2); Glycosylation (2); Helix (27); Modified residue (1); Natural variant (6); Sequence conflict (5); Signal peptide (1); Turn (9) |
| Keywords | 3D-structure;Direct protein sequencing;Disulfide bond;Glycoprotein;Hydrolase;Lipid degradation;Lipid metabolism;Pyrrolidone carboxylic acid;Secreted;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted. |
| Modified Residue | MOD_RES 20; /note=Pyrrolidone carboxylic acid; /evidence=ECO:0000269|PubMed:2341377 |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..19; /evidence=ECO:0000269|PubMed:2341377 |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 1THG; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 61,617 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:12044 |
| Cross Reference Brenda |