Detail Information for IndEnz0010001146
IED ID IndEnz0010001146
Enzyme Type ID esterase001146
Protein Name 4-O-methyl-glucuronoyl methylesterase
EC 3.1.1.117
Glucuronoyl esterase
GE
Gene Name cip2 TRIREDRAFT_123940
Organism Hypocrea jecorina (strain QM6a) (Trichoderma reesei)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta sordariomyceta Sordariomycetes Hypocreomycetidae Hypocreales Hypocreaceae Trichoderma Hypocrea jecorina (Trichoderma reesei) Hypocrea jecorina (strain QM6a) (Trichoderma reesei)
Enzyme Sequence MASRFFALLLLAIPIQAQSPVWGQCGGIGWSGPTTCVGGATCVSYNPYYSQCIPSTQASSSIASTTLVTSFTTTTATRTSASTPPASSTGAGGATCSALPGSITLRSNAKLNDLFTMFNGDKVTTKDKFSCRQAEMSELIQRYELGTLPGRPSTLTASFSGNTLTINCGEAGKSISFTVTITYPSSGTAPYPAIIGYGGGSLPAPAGVAMINFNNDNIAAQVNTGSRGQGKFYDLYGSSHSAGAMTAWAWGVSRVIDALELVPGARIDTTKIGVTGCSRNGKGAMVAGAFEKRIVLTLPQESGAGGSACWRISDYLKSQGANIQTASEIIGEDPWFSTTFNSYVNQVPVLPFDHHSLAALIAPRGLFVIDNNIDWLGPQSCFGCMTAAHMAWQALGVSDHMGYSQIGAHAHCAFPSNQQSQLTAFVQKFLLGQSTNTAIFQSDFSANQSQWIDWTTPTLS
Enzyme Length 460
Uniprot Accession Number G0RV93
Absorption
Active Site ACT_SITE 278; /note=Nucleophile; /evidence=ECO:0000305|PubMed:21661060; ACT_SITE 411; /note=Proton donor/acceptor; /evidence=ECO:0000305|PubMed:21661060
Activity Regulation
Binding Site BINDING 282; /note=Substrate; /evidence=ECO:0000250|UniProtKB:G2QJR6; BINDING 324; /note=Substrate; /evidence=ECO:0000250|UniProtKB:G2QJR6; BINDING 332; /note=Substrate; /evidence=ECO:0000250|UniProtKB:G2QJR6; BINDING 375; /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:17678650};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67453; Evidence={ECO:0000305|PubMed:17678650};
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. Does not hydrolyze substrates of other carbohydrate esterases such as acetylxylan esterase, acetyl esterase and feruloyl esterase. {ECO:0000269|PubMed:12788920, ECO:0000269|PubMed:17678650}.
Temperature Dependency BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 40-60 degrees Celsius. {ECO:0000269|PubMed:17678650};
PH Dependency BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.5. {ECO:0000269|PubMed:17678650};
Pathway
nucleotide Binding
Features Active site (2); Beta strand (10); Binding site (4); Chain (1); Disulfide bond (3); Domain (1); Glycosylation (1); Helix (18); Modified residue (1); Motif (1); Signal peptide (1); Turn (3)
Keywords 3D-structure;Direct protein sequencing;Disulfide bond;Glycoprotein;Hydrolase;Lignin degradation;Pyrrolidone carboxylic acid;Reference proteome;Secreted;Serine esterase;Signal
Interact With
Induction INDUCTION: Induced in the presence of lactose or sophorose. {ECO:0000269|PubMed:12788920}.
Subcellular Location SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
Modified Residue MOD_RES 18; /note=Pyrrolidone carboxylic acid; /evidence=ECO:0000269|PubMed:17678650
Post Translational Modification
Signal Peptide SIGNAL 1..17; /evidence=ECO:0000305|PubMed:17678650
Structure 3D X-ray crystallography (1)
Cross Reference PDB 3PIC;
Mapped Pubmed ID -
Motif MOTIF 276..281; /note=GXSYXG catalytic site motif; /evidence=ECO:0000305|PubMed:21661060
Gene Encoded By
Mass 48,296
Kinetics BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.5 mM for 4-nitrophenyl 2-O-(methyl-4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranoside {ECO:0000269|PubMed:17678650}; Vmax=5.5 umol/min/mg enzyme toward 4-nitrophenyl 2-O-(methyl-4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranoside {ECO:0000269|PubMed:17678650};
Metal Binding
Rhea ID RHEA:67452; RHEA:67453
Cross Reference Brenda 3.1.1.B11;