Detail Information for IndEnz0018000022
IED ID IndEnz0018000022
Enzyme Type ID peroxidase000022
Protein Name Versatile peroxidase VPL2
EC 1.11.1.16
Versatile liquid phase peroxidase 2
Gene Name vpl2
Organism Pleurotus eryngii (Boletus of the steppes)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Fungi Dikarya Basidiomycota Agaricomycotina Agaricomycetes Agaricomycetidae Agaricales Pleurotaceae Pleurotus Pleurotus eryngii (Boletus of the steppes)
Enzyme Sequence MSFKTLSALALALGAAVQFASAAVPLVQKRATCDDGRTTANAACCILFPILDDIQENLFDGAQCGEEVHESLRLTFHDAIGFSPTLGGGGADGSIIAFDTIETNFPANAGIDEIVSAQKPFVAKHNISAGDFIQFAGAVGVSNCPGGVRIPFFLGRPDAVAASPDHLVPEPFDSVDSILARMGDAGFSPVEVVWLLASHSIAAADKVDPSIPGTPFDSTPGVFDSQFFIETQLKGRLFPGTADNKGEAQSPLQGEIRLQSDHLLARDPQTACEWQSMVNNQPKIQNRFAATMSKMALLGQDKTKLIDCSDVIPTPPALVGAAHLPAGFSLSDVEQACAATPFPALTADPGPVTSVPPVPGS
Enzyme Length 361
Uniprot Accession Number O94753
Absorption
Active Site ACT_SITE 77; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00297, ECO:0000255|PROSITE-ProRule:PRU10012"; ACT_SITE 194; /note="Tryptophan radical intermediate"; /evidence="ECO:0000269|PubMed:16246366"
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=1-(4-hydroxy-3-methoxyphenyl)-2-(2-methoxyphenoxy)propane-1,3-diol + H2O2 = glycolaldehyde + guaiacol + H2O + vanillin; Xref=Rhea:RHEA:22396, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240, ChEBI:CHEBI:17071, ChEBI:CHEBI:18346, ChEBI:CHEBI:28591, ChEBI:CHEBI:53650; EC=1.11.1.16; Evidence={ECO:0000269|PubMed:12884090, ECO:0000269|PubMed:16246366, ECO:0000269|PubMed:9987124}; CATALYTIC ACTIVITY: Reaction=2 H(+) + H2O2 + 2 Mn(2+) = 2 H2O + 2 Mn(3+); Xref=Rhea:RHEA:22776, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16240, ChEBI:CHEBI:29035, ChEBI:CHEBI:29041; EC=1.11.1.16; Evidence={ECO:0000269|PubMed:12884090, ECO:0000269|PubMed:16246366, ECO:0000269|PubMed:9987124};
DNA Binding
EC Number 1.11.1.16
Enzyme Function FUNCTION: A versatile ligninolytic peroxidase that combines the substrate specificity characteristics of the two other ligninolytic peroxidases, manganese peroxidase and lignin peroxidase. {ECO:0000269|PubMed:9987124}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (2); Beta strand (10); Chain (1); Disulfide bond (4); Glycosylation (1); Helix (18); Metal binding (13); Mutagenesis (4); Propeptide (1); Region (1); Signal peptide (1); Site (1); Turn (6)
Keywords 3D-structure;Calcium;Direct protein sequencing;Disulfide bond;Glycoprotein;Heme;Hydrogen peroxide;Iron;Lignin degradation;Manganese;Metal-binding;Organic radical;Oxidoreductase;Peroxidase;Secreted;Signal;Zymogen
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Secreted {ECO:0000255|PROSITE-ProRule:PRU00297, ECO:0000269|PubMed:9987124}.
Modified Residue
Post Translational Modification
Signal Peptide SIGNAL 1..22; /evidence=ECO:0000255
Structure 3D X-ray crystallography (19)
Cross Reference PDB 2BOQ; 2VKA; 2W23; 3FJW; 3FKG; 3FM1; 3FM4; 3FM6; 3FMU; 4FCN; 4FCS; 4FDQ; 4FEF; 4G05; 5ABN; 5ABO; 5ABQ; 5FNB; 5FNE;
Mapped Pubmed ID 18201105; 19158088; 23071108; 26496708; 27118867;
Motif
Gene Encoded By
Mass 37,624
Kinetics BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=19 uM for manganese {ECO:0000269|PubMed:12884090}; KM=3000 uM for veratryl alcohol {ECO:0000269|PubMed:12884090}; KM=4 uM for reactive black 5 {ECO:0000269|PubMed:12884090}; KM=3 uM for 2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonate) (ABTS) {ECO:0000269|PubMed:12884090};
Metal Binding METAL 66; /note=Manganese; /evidence=ECO:0000269|PubMed:16246366; METAL 70; /note=Manganese; /evidence=ECO:0000250; METAL 78; /note=Calcium 1; METAL 90; /note=Calcium 1; via carbonyl oxygen; METAL 92; /note=Calcium 1; METAL 94; /note=Calcium 1; METAL 199; /note=Iron (heme b axial ligand); METAL 200; /note=Calcium 2; METAL 205; /note=Manganese; /evidence=ECO:0000269|PubMed:16246366; METAL 217; /note=Calcium 2; METAL 219; /note=Calcium 2; METAL 222; /note=Calcium 2; via carbonyl oxygen; METAL 224; /note=Calcium 2
Rhea ID RHEA:22396; RHEA:22776
Cross Reference Brenda 1.11.1.16;1.11.1.7;