| IED ID | IndEnz0010001141 |
| Enzyme Type ID | esterase001141 |
| Protein Name |
4-O-methyl-glucuronoyl methylesterase EC 3.1.1.117 Glucuronoyl esterase 2 GE2 |
| Gene Name | ge2 MYCTH_55568 |
| 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 | MVHLTSALLVAGAAFAAAAPMNHIFERQDTCSVSDNYPTVNSAKLPDPFTTASGEKVTTKDQFECRRAEINKILQQYELGEYPGPPDSVEASLSGNSITVRVTVGSKSISFSASIRKPSGAGPFPAIIGIGGASIPIPSNVATITFNNDEFGAQMGSGSRGQGKFYDLFGRDHSAGSLTAWAWGVDRLIDGLEQVGAQASGIDTKRLGVTGCSRNGKGAFITGALVDRIALTIPQESGAGGAACWRISDQQKAAGANIQTAAQIITENPWFSRNFDPHVNSITSVPQDHHLLAALIVPRGLAVFENNIDWLGPVSTTGCMAAGRLIYKAYGVPNNMGFSLVGGHNHCQFPSSQNQDLNSYINYFLLGQGSPSGVEHSDVNVNVAEWAPWGAGAPTLA |
| Enzyme Length | 397 |
| Uniprot Accession Number | G2QJR6 |
| Absorption | |
| Active Site | ACT_SITE 213; /note="Nucleophile"; /evidence="ECO:0000269|PubMed:20473662, ECO:0000305|PubMed:23275164"; ACT_SITE 346; /note="Proton donor/acceptor"; /evidence="ECO:0000305|PubMed:23275164" |
| Activity Regulation | |
| Binding Site | BINDING 217; /note=Substrate; /evidence=ECO:0000269|PubMed:23275164; BINDING 259; /note=Substrate; /evidence=ECO:0000269|PubMed:23275164; BINDING 267; /note=Substrate; /evidence=ECO:0000269|PubMed:23275164; BINDING 310; /note=Substrate; /evidence=ECO:0000269|PubMed:23275164 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=a 4-O-methyl-alpha-D-glucuronosyl ester derivative + H2O = 4-O-methyl-alpha-D-glucuronate derivative + an alcohol + H(+); Xref=Rhea:RHEA:67452, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30879, ChEBI:CHEBI:171667, ChEBI:CHEBI:171668; EC=3.1.1.117; Evidence={ECO:0000269|PubMed:20473662};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67453; Evidence={ECO:0000305|PubMed:20473662}; |
| DNA Binding | |
| EC Number | 3.1.1.117 |
| Enzyme Function | FUNCTION: Glucuronoyl esterase which may play a significant role in biomass degradation, as it is considered to disconnect hemicellulose from lignin through the hydrolysis of the ester bond between 4-O-methyl-D-glucuronic acid residues of glucuronoxylans and aromatic alcohols of lignin. {ECO:0000269|PubMed:20473662}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 55 degrees Celsius. {ECO:0000269|PubMed:20473662}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0. {ECO:0000269|PubMed:20473662}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Beta strand (11); Binding site (4); Chain (1); Disulfide bond (3); Helix (18); Motif (1); Mutagenesis (1); Signal peptide (1); Turn (4) |
| Keywords | 3D-structure;Disulfide bond;Hydrolase;Lignin degradation;Reference proteome;Secreted;Serine esterase;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000305}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..18; /evidence=ECO:0000255 |
| Structure 3D | X-ray crystallography (3) |
| Cross Reference PDB | 4G4G; 4G4I; 4G4J; |
| Mapped Pubmed ID | - |
| Motif | MOTIF 211..216; /note=GXSYXG catalytic site motif; /evidence=ECO:0000305|PubMed:20473662 |
| Gene Encoded By | |
| Mass | 41,752 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=3.63 mM for trans-3-phenyl-2-propen-1-yl D-glucopyranosyluronate {ECO:0000269|PubMed:24531271}; KM=7.24 mM for 3-phenyl-1-propyl D-glucopyranosyluronate {ECO:0000269|PubMed:24531271}; Note=kcat is 115.9 min(-1) with trans-3-phenyl-2-propen-1-yl D-glucopyranosyluronate and 166.4 with 3-phenyl-1-propyl D-glucopyranosyluronate as substrate. {ECO:0000269|PubMed:24531271}; |
| Metal Binding | |
| Rhea ID | RHEA:67452; RHEA:67453 |
| Cross Reference Brenda | 3.1.1.B11; |