Detail Information for IndEnz0010001148
IED ID IndEnz0010001148
Enzyme Type ID esterase001148
Protein Name 4-O-methyl-glucuronoyl methylesterase
EC 3.1.1.117
Glucuronoyl esterase
GE
Gene Name Cip2 ce15-1 NCU09445
Organism Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta sordariomyceta Sordariomycetes Sordariomycetidae Sordariales Sordariaceae Neurospora Neurospora crassa Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
Enzyme Sequence MVHLTPALLLASAAFAAAAPASQIFERQCSVAGNYPTAAVSKLPDPFTTAAGQKITTKADFDCRKAEISKILQQYELGTYPGKPDKVEGSLSGNTLTVRITVGSQTVSFSASIKKPSSGSGPFPAIIGIGGISIPIPSTVATITFPNDDFAQQSGTSSRGRGKFYTLFGSSHSAGALIAWAWGVDRLVDALEQVQSTSGIDPKRLGVTGCSRNGKGAFVAGALVDRIALTIPQESGAGGAACWRISDSEKSAGKNIQTASQIVTENVWFSPAFNAYTRQTTNIPADHHMLAALTVPRGLIAFENDIDWLGPVSTTACMQAGRLIYKAYGVSNHMGFSLVGGHGHCQFPSSQQSELTSYINYFLLKAGTAPGAVERSSAKVDLKSWAPWDVPALS
Enzyme Length 394
Uniprot Accession Number Q7S1X0
Absorption
Active Site ACT_SITE 211; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:G2QJR6; ACT_SITE 344; /note=Proton donor/acceptor; /evidence=ECO:0000250|UniProtKB:G2QJR6
Activity Regulation
Binding Site BINDING 215; /note=Substrate; /evidence=ECO:0000250|UniProtKB:G2QJR6; BINDING 257; /note=Substrate; /evidence=ECO:0000250|UniProtKB:G2QJR6; BINDING 265; /note=Substrate; /evidence=ECO:0000250|UniProtKB:G2QJR6; BINDING 308; /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:27600355};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67453; Evidence={ECO:0000305|PubMed:27600355};
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:27600355}.
Temperature Dependency BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 40-50 degrees Celsius. {ECO:0000269|PubMed:27600355};
PH Dependency BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7. Stable from pH 4 to pH 7. {ECO:0000269|PubMed:27600355};
Pathway
nucleotide Binding
Features Active site (2); Binding site (4); Chain (1); Disulfide bond (3); Motif (1); Signal peptide (1)
Keywords Disulfide bond;Hydrolase;Lignin degradation;Reference proteome;Secreted;Serine esterase;Signal
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:G0RV93}.
Modified Residue
Post Translational Modification
Signal Peptide SIGNAL 1..18; /evidence=ECO:0000255
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif MOTIF 209..214; /note=GXSYXG catalytic site motif; /evidence=ECO:0000250|UniProtKB:G2QJR6
Gene Encoded By
Mass 41,351
Kinetics BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=15 mM for 3-(4-methoxyphenyl) propyl methyl 4-O-methyl-alpha-D-glucopyranosiduronate {ECO:0000269|PubMed:27600355}; Note=kcat is 16.8 sec(-1) with 3-(4-methoxyphenyl) propyl methyl 4-O-methyl-alpha-D-glucopyranosiduronate. {ECO:0000269|PubMed:27600355};
Metal Binding
Rhea ID RHEA:67452; RHEA:67453
Cross Reference Brenda 3.1.1.B11;