Detail Information for IndEnz0018000510
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;