| IED ID | IndEnz0010000656 |
| Enzyme Type ID | esterase000656 |
| Protein Name |
Lipase A EC 3.1.1.3 EC 3.1.1.72 Acetylxylan esterase |
| Gene Name | lipA fgenesh2_kg.3_#_445_#_Contig6955 |
| Organism | Sodiomyces alcalophilus (Acremonium alcalophilum) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta sordariomyceta Sordariomycetes Hypocreomycetidae Glomerellales Plectosphaerellaceae Sodiomyces Sodiomyces alcalophilus (Acremonium alcalophilum) |
| Enzyme Sequence | MRLAPQKPLLLSTVLHLLLSIWMLGFASLAGATVQEPLAASDTPKPVSAALFSSIERLSRLVDITYCVGNTGVWKPFACASRCNEFPTLTLERTWRTGILMSDSCGLIAVDHGTPRHDAGEGKDDPLAEKAIIVAFRGTYSLTNTIIDLSTIPQEYVPYPSPDDGGNEPPREPSHRCDNCTVHSGFLASWRHARKVVLPELKVLRQKYPEYPIRLVGHSLGGAVAMLAALEMRVSLGWRDTVVTTFGEPRVGNRQLCDYLNAVFELNLGDEMDPAEREYRRVTHADDPVPLLPPAEWGYSSHGGEFFISKKDLPPSVEDVLVCHGDHDENCIARGKSSAVSVPAGDYDDALSTLEEQDVMLADALPWIPARLKLWELFFAHRDYFWRLGLCVPGGDPANWGRKGGEGAAESISAEG |
| Enzyme Length | 416 |
| Uniprot Accession Number | P0CT91 |
| Absorption | |
| Active Site | ACT_SITE 219; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:O59952; ACT_SITE 287; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:O59952; ACT_SITE 381; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:O59952 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Deacetylation of xylans and xylo-oligosaccharides.; EC=3.1.1.72; Evidence={ECO:0000269|PubMed:23915965}; 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; Evidence={ECO:0000269|PubMed:23915965}; |
| DNA Binding | |
| EC Number | 3.1.1.3; 3.1.1.72 |
| Enzyme Function | FUNCTION: Lipolytic enzyme that possesses both lipase and acetylxylan esterase activity. Active towards p-nitrophenol esters of various carbon chain length with preference for medium-chain fatty acids (C-8). Also highly active on the acetylated compounds xylose tetra-acetate and oat spelt xylan. {ECO:0000269|PubMed:23915965}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 40 degrees Celsius. Thermostable from 20 to 50 degrees Celsius. {ECO:0000269|PubMed:23915965}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0. {ECO:0000269|PubMed:23915965}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Disulfide bond (2); Glycosylation (1); Signal peptide (1) |
| Keywords | Carbohydrate metabolism;Disulfide bond;Glycoprotein;Hydrolase;Lipid degradation;Lipid metabolism;Polysaccharide degradation;Secreted;Serine esterase;Signal;Xylan degradation |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000305}. |
| Modified Residue | |
| Post Translational Modification | PTM: Glycosylated. {ECO:0000269|PubMed:23915965}. |
| Signal Peptide | SIGNAL 1..32; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 45,645 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.15 mM for p-nitrophenol acetate {ECO:0000269|PubMed:23915965}; KM=0.16 mM for p-nitrophenol butyrate {ECO:0000269|PubMed:23915965}; KM=0.10 mM for p-nitrophenol caprylate {ECO:0000269|PubMed:23915965}; KM=0.07 mM for p-nitrophenol myristate {ECO:0000269|PubMed:23915965}; KM=0.10 mM for p-nitrophenol palmitate {ECO:0000269|PubMed:23915965}; Vmax=0.24 umol/min/mg enzyme toward p-nitrophenol acetate {ECO:0000269|PubMed:23915965}; Vmax=4.73 umol/min/mg enzyme toward p-nitrophenol butyrate {ECO:0000269|PubMed:23915965}; Vmax=9.45 umol/min/mg enzyme toward p-nitrophenol caprylate {ECO:0000269|PubMed:23915965}; Vmax=3.42 umol/min/mg enzyme toward p-nitrophenol myristate {ECO:0000269|PubMed:23915965}; Vmax=1.84 umol/min/mg enzyme toward p-nitrophenol palmitate {ECO:0000269|PubMed:23915965}; |
| Metal Binding | |
| Rhea ID | RHEA:12044 |
| Cross Reference Brenda |