| IED ID | IndEnz0010001142 |
| Enzyme Type ID | esterase001142 |
| Protein Name |
4-O-methyl-glucuronoyl methylesterase 2 EC 3.1.1.117 Glucuronoyl esterase 2 GE2 |
| Gene Name | e_gw1.11.1537.1 fgenesh1_pg.C_scaffold_11000167 |
| Organism | Phanerochaete chrysosporium (strain RP-78 / ATCC MYA-4764 / FGSC 9002) (White-rot fungus) (Sporotrichum pruinosum) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Basidiomycota Agaricomycotina Agaricomycetes Agaricomycetes incertae sedis Polyporales Phanerochaetaceae Phanerodontia Phanerodontia chrysosporium (White-rot fungus) (Sporotrichum pruinosum) Phanerochaete chrysosporium (strain RP-78 / ATCC MYA-4764 / FGSC 9002) (White-rot fungus) (Sporotrichum pruinosum) |
| Enzyme Sequence | MAFSWLSFVLLALPVLALARPSEHEARSLFCSTPSNIPFNDDKLPDPFKFNDGSPVRSFADWDCRRQQLSALIQGYEAGTLPPRPPVVTSTFTKSGTTGNLTVTAGFPGKTITFSSPITFPTGTAPFGGWPLVIAYGGVSIPIPDGIAVLTYDNSAMAEQNDQSSRGVGLFFDVYGANATASSMTAWVWGLSRIIDSLEVTPAAHINTAKIAVTGCSRNGKGALMAGAFEERIALTIPQESGSGGDTCWRLSKFEQDSGDVVQQATEIVQENVWFSTNFDNYVFNISLLPYDHHELAALVAPRPLISYENTDFEWLSPLSGFGCMTAAHTVWEAMGIPDKHGFVQVGNHSHCDFPSSLNPTLFAFFDKFLLGKEANTSIFETNGLFNGTEWVASQWINWTTPRFTLL |
| Enzyme Length | 407 |
| Uniprot Accession Number | P0CT88 |
| Absorption | |
| Active Site | ACT_SITE 217; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:G2QJR6; ACT_SITE 351; /note=Proton donor/acceptor; /evidence=ECO:0000250|UniProtKB:G2QJR6 |
| Activity Regulation | |
| Binding Site | BINDING 221; /note=Substrate; /evidence=ECO:0000250|UniProtKB:G2QJR6; BINDING 263; /note=Substrate; /evidence=ECO:0000250|UniProtKB:G2QJR6; BINDING 271; /note=Substrate; /evidence=ECO:0000250|UniProtKB:G2QJR6; BINDING 315; /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:18854978, ECO:0000269|PubMed:19897892};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67453; Evidence={ECO:0000305|PubMed:18854978, ECO:0000305|PubMed:19897892}; |
| 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:18854978, ECO:0000269|PubMed:19897892}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 45-55 degrees Celsius. {ECO:0000269|PubMed:19897892}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.0-6.0. {ECO:0000269|PubMed:19897892}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Binding site (4); Chain (1); Disulfide bond (3); Glycosylation (7); Motif (1); Signal peptide (1) |
| Keywords | Disulfide bond;Glycoprotein;Hydrolase;Lignin degradation;Secreted;Serine esterase;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18854978}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..19; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | MOTIF 215..220; /note=GXSYXG catalytic site motif; /evidence=ECO:0000250|UniProtKB:G2QJR6 |
| Gene Encoded By | |
| Mass | 44,294 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.82 mM for 4-nitrophenyl 2-O-(methyl-4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranoside {ECO:0000269|PubMed:19897892}; Vmax=88.4 umol/min/mg enzyme toward 4-nitrophenyl 2-O-(methyl-4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranoside {ECO:0000269|PubMed:19897892}; |
| Metal Binding | |
| Rhea ID | RHEA:67452; RHEA:67453 |
| Cross Reference Brenda | 3.1.1.B11; |