IED ID | IndEnz0018000510 |
Enzyme Type ID | peroxidase000510 |
Protein Name |
Ligninase LG2 EC 1.11.1.14 Diarylpropane peroxidase Lignin peroxidase |
Gene Name | GLG2 LIP2 |
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 | MAFKQLFAAITVALSLTAANAAVVKEKRATCANGKTVGDASCCAWFDVLDDIQANMFHGGQCGAEAHESIRLVFHDSIAISPAMEAKGKFGGGGADGSIMIFDTIETAFHPNIGLDEVVAMQKPFVQKHGVTPGDFIAFAGAVALSNCPGAPQMNFFTGRKPATQPAPDGLVPEPFHTVDQIIARVNDAGEFDELELVWMLSAHSVAAVNDVDPTVQGLPFDSTPGIFDSQFFVETQFRGTLFPGSGGNQGEVESGMAGEIRIQTDHTLARDSRTACEWQSFVGNQSKLVDDFQFIFLALTQLGQDPNAMTDCSDVIPLSKPIPGNGPFSFFPPGKSHSDIEQACAETPFPSLVTLPGPATSVARIPPHKA |
Enzyme Length | 371 |
Uniprot Accession Number | P49012 |
Absorption | |
Active Site | ACT_SITE 75; /note=Proton acceptor |
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:0000250|UniProtKB:P06181}; 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:0000250|UniProtKB:P06181}; |
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:0000250|UniProtKB:P06181}. |
Temperature Dependency | |
PH Dependency | |
Pathway | PATHWAY: Secondary metabolite metabolism; lignin degradation. |
nucleotide Binding | |
Features | Active site (1); Beta strand (9); Chain (1); Disulfide bond (4); Glycosylation (1); Helix (19); Metal binding (10); Modified residue (1); Propeptide (1); Signal peptide (1); Site (1); Turn (4) |
Keywords | 3D-structure;Calcium;Cleavage on pair of basic residues;Direct protein sequencing;Disulfide bond;Glycoprotein;Heme;Hydroxylation;Iron;Lignin degradation;Metal-binding;Oxidoreductase;Peroxidase;Signal;Zymogen |
Interact With | |
Induction | |
Subcellular Location | |
Modified Residue | MOD_RES 199; /note=3-hydroxytryptophan; /evidence=ECO:0000269|PubMed:10024453 |
Post Translational Modification | |
Signal Peptide | SIGNAL 1..21 |
Structure 3D | X-ray crystallography (2) |
Cross Reference PDB | 1LGA; 1LLP; |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 39,329 |
Kinetics | |
Metal Binding | METAL 76; /note=Calcium 1; METAL 94; /note=Calcium 1; via carbonyl oxygen; METAL 96; /note=Calcium 1; METAL 98; /note=Calcium 1; METAL 204; /note=Iron (heme b axial ligand); METAL 205; /note=Calcium 2; METAL 222; /note=Calcium 2; METAL 224; /note=Calcium 2; METAL 227; /note=Calcium 2; via carbonyl oxygen; METAL 229; /note=Calcium 2 |
Rhea ID | RHEA:48004; RHEA:30271 |
Cross Reference Brenda | 1.11.1.14; |