| IED ID | IndEnz0005000476 |
| Enzyme Type ID | lipase000476 |
| Protein Name |
Feruloyl esterase A EC 3.1.1.73 Ferulic acid esterase A FAEA Feruloylesterase |
| Gene Name | faeA |
| Organism | Aspergillus awamori (Black koji mold) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Aspergillaceae Aspergillus Aspergillus awamori (Black koji mold) |
| Enzyme Sequence | MKQFSAKHALAVVVTAGHALAASTQGISEDLYTRLVEMATISQAAYADLCNIPSTIIKGEKIYNSQTDINGWILRDDSSKEIITVFRGTGSDTNLQLDTNYTLTPFDTLPQCNGCEVHGGYYIGWVSVQDQVESLVKQQVSQYPDYALTVTGHSLGASLAALTAAQLSATYDNIRLYTFGEPRSGNQAFASYMNDAFQASSPDTTQYFRVTHANDGIPNLPPVEQGYAHGGVEYWSVDPYSAQNTFVCTGDEVQCCEAQGGQGVNNAHTTYFGMTSGACTW |
| Enzyme Length | 281 |
| Uniprot Accession Number | Q9P979 |
| Absorption | |
| Active Site | ACT_SITE 154; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:O42807; ACT_SITE 215; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:O42807; ACT_SITE 268; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:O42807 |
| Activity Regulation | |
| Binding Site | BINDING 98; /note=Substrate; /evidence=ECO:0000250|UniProtKB:O42807; BINDING 101; /note=Substrate; /evidence=ECO:0000250|UniProtKB:O42807; BINDING 268; /note=Substrate; /evidence=ECO:0000250|UniProtKB:O42807 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Feruloyl-polysaccharide + H(2)O = ferulate + polysaccharide.; EC=3.1.1.73; Evidence={ECO:0000269|PubMed:15716038}; |
| DNA Binding | |
| EC Number | 3.1.1.73 |
| Enzyme Function | FUNCTION: Involved in the degradation of plant cell walls. Hydrolyzes the feruloyl-arabinose ester bond in arabinoxylans, and the feruloyl-galactose ester bond in pectin. Active against methyl ferulate, methyl sinapate, methyl caffeate, and alpha-naphthyl esters with chains containing 2 to 8 carbons (C2-C8). Inactive against alpha-naphthyl esters with longer chains (C10 or more). {ECO:0000269|PubMed:15716038}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.0. {ECO:0000269|PubMed:15716038}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Binding site (3); Chain (1); Disulfide bond (3); Glycosylation (1); Mutagenesis (5); Signal peptide (1) |
| Keywords | Carbohydrate metabolism;Disulfide bond;Glycoprotein;Hydrolase;Polysaccharide degradation;Secreted;Serine esterase;Signal;Xylan degradation |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:O42807}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..21; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 30,401 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.33 mM for alpha-naphthylbutyrate {ECO:0000269|PubMed:15716038}; KM=0.079 mM for alpha-naphthylcaprylate {ECO:0000269|PubMed:15716038}; |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.1.1.73; |