Detail Information for IndEnz0010001400
IED ID IndEnz0010001400
Enzyme Type ID esterase001400
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;