| IED ID | IndEnz0010001152 |
| Enzyme Type ID | esterase001152 |
| Protein Name |
4-O-methyl-glucuronoyl methylesterase EC 3.1.1.117 Glucuronoyl esterase GE |
| Gene Name | SCHCODRAFT_238770 |
| Organism | Schizophyllum commune (strain H4-8 / FGSC 9210) (Split gill fungus) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Basidiomycota Agaricomycotina Agaricomycetes Agaricomycetidae Agaricales Schizophyllaceae Schizophyllum Schizophyllum commune (Split gill fungus) Schizophyllum commune (strain H4-8 / FGSC 9210) (Split gill fungus) |
| Enzyme Sequence | MKLSAALLAIAAFANVASAQDCDTPATVSGYSNSALPDPFTFNDGSPVTTAEDWECRRSQILALIQGYESGAAPPEPESVTGTASGNSLSVQVSYGGKSITFNNSITYPSGTAPAEGWPVIIAYEFPSLPIPSNVATLSFQNSAMGKQDSTSSRGQGLFYDLYGSSSNASAMTAWAWGVSRIIDAIESTPDAKLNPAAVGVTGCSRNGKGALMAGALEPRVALTLPQESGSGGDACWRLSRYEEQQGSQVQTATEIVGENCWFSAGFDQYVNNLDSLPYDHHLLAALVAPRGLISYANTDYVWLSGMSSFGCMTAAHAVYEALGVPENHGFEQVGGHSHCQWPSQLDGSLNAFINKFLLGQDVSTDYFESNNQFNGVTWSESQWINWETPTLN |
| Enzyme Length | 393 |
| Uniprot Accession Number | D8QLP9 |
| Absorption | |
| Active Site | ACT_SITE 205; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:G2QJR6; ACT_SITE 339; /note=Proton donor/acceptor; /evidence=ECO:0000250|UniProtKB:G2QJR6 |
| Activity Regulation | |
| Binding Site | BINDING 209; /note=Substrate; /evidence=ECO:0000250|UniProtKB:G2QJR6; BINDING 251; /note=Substrate; /evidence=ECO:0000250|UniProtKB:G2QJR6; BINDING 259; /note=Substrate; /evidence=ECO:0000250|UniProtKB:G2QJR6; BINDING 303; /note=Substrate; /evidence=ECO:0000250|UniProtKB:G2QJR6 |
| 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:16876163};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67453; Evidence={ECO:0000305|PubMed:16876163}; |
| 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:16876163}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 50 degrees Celsius. {ECO:0000269|PubMed:16876163}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7. {ECO:0000269|PubMed:16876163}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Binding site (4); Chain (1); Disulfide bond (3); Glycosylation (2); Modified residue (1); Motif (1); Signal peptide (1) |
| Keywords | Direct protein sequencing;Disulfide bond;Glycoprotein;Hydrolase;Lignin degradation;Pyrrolidone carboxylic acid;Reference proteome;Secreted;Serine esterase;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16876163}. |
| Modified Residue | MOD_RES 20; /note=Pyrrolidone carboxylic acid; /evidence=ECO:0000305|PubMed:17678650 |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..19; /evidence=ECO:0000305|PubMed:17678650 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | MOTIF 203..208; /note=GXSYXG catalytic site motif; /evidence=ECO:0000250|UniProtKB:G2QJR6 |
| Gene Encoded By | |
| Mass | 41,773 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.31 mM for 4-nitrophenyl 2-O-(methyl-4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranoside (purified enzyme) {ECO:0000269|PubMed:16876163}; KM=0.25 mM for 4-nitrophenyl 2-O-(methyl-4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranoside (recombinant enzyme) {ECO:0000269|PubMed:22844600}; Vmax=4.4 umol/min/mg enzyme toward 4-nitrophenyl 2-O-(methyl-4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranoside (purified enzyme) {ECO:0000269|PubMed:16876163}; Vmax=16.3 umol/min/mg enzyme toward 4-nitrophenyl 2-O-(methyl-4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranoside (recombinant enzyme) {ECO:0000269|PubMed:22844600}; |
| Metal Binding | |
| Rhea ID | RHEA:67452; RHEA:67453 |
| Cross Reference Brenda | 3.1.1.B11; |