| IED ID | IndEnz0004000260 |
| Enzyme Type ID | xylanase000260 |
| Protein Name |
Feruloyl esterase B EC 3.1.1.73 Cinnamoyl esterase Ferulic acid esterase B FAEB |
| Gene Name | Fae1a MYCTH_96478 |
| Organism | Myceliophthora thermophila (strain ATCC 42464 / BCRC 31852 / DSM 1799) (Sporotrichum thermophile) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta sordariomyceta Sordariomycetes Sordariomycetidae Sordariales Chaetomiaceae Thermothelomyces Thermothelomyces thermophilus (Myceliophthora thermophila) Myceliophthora thermophila (strain ATCC 42464 / BCRC 31852 / DSM 1799) (Sporotrichum thermophile) |
| Enzyme Sequence | MLVRSFLGFAVLAATCLAASLQEVTEFGDNPTNIQMYIYVPDQLDTNPPVIVALHPCGGSAQQWFSGTQLPSYADDNGFILIYPSTPHMSNCWDIQNPDTLTHGQGGDALGIVSMVNYTLDKHSGDSSRVYAMGFSSGGMMTNQLAGSYPDVFEAGAVYSGVAFGCAAGAESATPFSPNQTCAQGLQKTAQEWGDFVRNAYAGYTGRRPRMQIFHGLEDTLVRPQCAEEALKQWSNVLGVELTQEVSGVPSPGWTQKIYGDGTQLQGFFGQGIGHQSTVNEQQLLQWFGLI |
| Enzyme Length | 291 |
| Uniprot Accession Number | G2QND5 |
| Absorption | |
| Active Site | ACT_SITE 136; /note=Charge relay system |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Feruloyl-polysaccharide + H(2)O = ferulate + polysaccharide.; EC=3.1.1.73; Evidence={ECO:0000269|PubMed:22012339}; |
| DNA Binding | |
| EC Number | 3.1.1.73 |
| Enzyme Function | FUNCTION: Feruloyl esterase which acts in synergy with xylanases in degradation of plant cell walls. Hydrolyzes the ester linkage of hydroxycinnamic acids (ferulic acid (FA) and p-coumaric acid) and diferulates present in plant cell walls. Is active on substrates containing ferulic acid ester linked to the C-5 and C-2 linkages of arabinofuranose, while it was found capable of de-esterifying acetylated glucuronoxylans. Efficiently releases ferulic acid (FA) from destarched wheat bran when incubated with an M3 xylanase. {ECO:0000269|PubMed:22012339}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 50 degrees Celsius. {ECO:0000269|PubMed:22012339}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0. {ECO:0000269|PubMed:22012339}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Glycosylation (2); Mutagenesis (1); Signal peptide (1) |
| Keywords | Carbohydrate metabolism;Glycoprotein;Hydrolase;Polysaccharide degradation;Reference proteome;Secreted;Serine esterase;Signal;Xylan degradation |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..18; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 31407106; |
| Motif | |
| Gene Encoded By | |
| Mass | 31,372 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.27 mM for methyl ferulate (MFA) {ECO:0000269|PubMed:22012339}; KM=0.26 mM for methyl p-coumarate (MpCA) {ECO:0000269|PubMed:22012339}; KM=0.18 mM for methyl caffeate (MCA) {ECO:0000269|PubMed:22012339}; KM=0.21 mM for methyl sinapate (MSA) {ECO:0000269|PubMed:22012339}; KM=2.29 mM for nitrophenyl-5-O-trans-feruloyl-alpha-L-arabinofuranoside {ECO:0000269|PubMed:22012339}; KM=2.79 mM for nitrophenyl-2-O-trans-feruloyl-alpha-L-arabinofuranoside {ECO:0000269|PubMed:22012339}; KM=2.33 mM for ethyl ferulate {ECO:0000269|PubMed:22012339}; KM=1.14 mM for n-propyl ferulate {ECO:0000269|PubMed:22012339}; KM=1.40 mM for iso-propyl ferulate {ECO:0000269|PubMed:22012339}; KM=0.74 mM for n-butyl ferulate {ECO:0000269|PubMed:22012339}; KM=0.65 mM for iso-butyl ferulate {ECO:0000269|PubMed:22012339}; KM=0.74 mM for 2-butyl ferulate {ECO:0000269|PubMed:22012339}; |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.1.1.73; |