| IED ID | IndEnz0018000619 |
| Enzyme Type ID | peroxidase000619 |
| Protein Name |
Ligninase B EC 1.11.1.14 Diarylpropane peroxidase Lignin peroxidase |
| Gene Name | LIPB |
| Organism | Phanerodontia chrysosporium (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) |
| Enzyme Sequence | MAFKQLFAAISLALSLSAANAAAVIEKRATCSNGKTVGDASCCAWFDVLDDIQQNLFHGGQCGAEAHESIRLVFHDSIAISPAMEAQGKFGGGGADGSIMIFDDIETAFHPNIGLDEIVKLQKPFVQKHGVTPGAFIAFAGAVALSNCPGAPQMNFFTGRAPATQPAPDGLVPEPFHTVDQIINRVNDAGEFDELELVWMLSAHSVAAVNDVDPTVQGLPFDSTPGIFDSQFFVETQLRGTAFPGSGGNQGEVESPLPGEIRIQSDHTIARDSRTACEWQSFVNNQSKLVDDFQFIFLALTQLGQDPNAMTDCSDVIPQSKPIPGNLPFSFFPAGKTIKDVEQACAETPFPTLTTLPGPETSVQRIPPPPGA |
| Enzyme Length | 372 |
| Uniprot Accession Number | P31838 |
| Absorption | |
| Active Site | ACT_SITE 75; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00297, ECO:0000255|PROSITE-ProRule:PRU10012" |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=1-(3,4-dimethoxyphenyl)-2-(2-methoxyphenoxy)propane-1,3-diol + H2O2 = 3,4-dimethoxybenzaldehyde + glycolaldehyde + guaiacol + H2O; Xref=Rhea:RHEA:48004, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240, ChEBI:CHEBI:17071, ChEBI:CHEBI:17098, ChEBI:CHEBI:28591, ChEBI:CHEBI:86963; EC=1.11.1.14; Evidence={ECO:0000269|PubMed:3240864}; CATALYTIC ACTIVITY: Reaction=2 (3,4-dimethoxyphenyl)methanol + H2O2 = 2 (3,4-dimethoxyphenyl)methanol radical + 2 H2O; Xref=Rhea:RHEA:30271, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240, ChEBI:CHEBI:62150, ChEBI:CHEBI:88143; EC=1.11.1.14; Evidence={ECO:0000269|PubMed:3240864}; |
| DNA Binding | |
| EC Number | 1.11.1.14 |
| Enzyme Function | FUNCTION: Depolymerization of lignin. Catalyzes the C(alpha)-C(beta) cleavage of the propyl side chains of lignin. {ECO:0000269|PubMed:3240864}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 2.3. {ECO:0000269|PubMed:3240864}; |
| Pathway | PATHWAY: Secondary metabolite metabolism; lignin degradation. |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Disulfide bond (4); Glycosylation (1); Metal binding (10); Propeptide (1); Region (1); Signal peptide (1); Site (1) |
| Keywords | Calcium;Cleavage on pair of basic residues;Direct protein sequencing;Disulfide bond;Glycoprotein;Heme;Hydrogen peroxide;Iron;Lignin degradation;Metal-binding;Oxidoreductase;Peroxidase;Signal;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..21; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 39,530 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=85 uM for H(2)O(2) {ECO:0000269|PubMed:3240864}; KM=83 uM for (3,4-dimethoxyphenyl)methanol {ECO:0000269|PubMed:3240864}; |
| Metal Binding | METAL 76; /note=Calcium 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00297; METAL 94; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000255|PROSITE-ProRule:PRU00297; METAL 96; /note=Calcium 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00297; METAL 98; /note=Calcium 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00297; METAL 204; /note=Iron (heme b axial ligand); /evidence=ECO:0000255|PROSITE-ProRule:PRU00297; METAL 205; /note=Calcium 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00297; METAL 222; /note=Calcium 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00297; METAL 224; /note=Calcium 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00297; METAL 227; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000255|PROSITE-ProRule:PRU00297; METAL 229; /note=Calcium 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00297 |
| Rhea ID | RHEA:48004; RHEA:30271 |
| Cross Reference Brenda |