| IED ID | IndEnz0018000006 |
| Enzyme Type ID | peroxidase000006 |
| Protein Name |
Multifunctional dye peroxidase DyP2 EC 1.11.1.16 EC 1.11.1.19 EC 1.11.1.7 Dye decolorizing peroxidase 2 DyP2 Manganese peroxidase |
| Gene Name | dyp2 |
| Organism | Amycolatopsis sp. (strain ATCC 39116 / 75iv2) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Actinobacteria Actinomycetia (high G+C Gram-positive bacteria) Pseudonocardiales Pseudonocardiaceae Amycolatopsis unclassified Amycolatopsis Amycolatopsis sp. (strain ATCC 39116 / 75iv2) |
| Enzyme Sequence | MPVDLSTTLSWKSATGEAATMLDELQPNILKAHVRDRLTVLFLGFGDAAEARTFLNGLSGLMKSARTHLQEVEAHKLTKAVGTPYLGVGLTAHGYATLGVTAPADPSFTAGAKAAVEKLADPAVTEWEGHYQQTIDAVLLLGDATAGPVRTLRRQVEALRPASVTVVGEESGLGLANANGDGIEHFGYVDGRSQPLFLTEDVDAERDTTDGVNDWDPSAPLEQVLVPDPAAPDPTVHFGSYFVFRKLEQNVRLFKEAERDLAHDLGLRGEDRERAGAMLVGRFEDGTPLTAQSAPGSHHPVGNDFSYDSDKLGQKCPFHAHIRKTNPRGSGGAEAPEEERKHLMARRGQTYGRRHDDPNADLPPRLRPAKDVGLLFMAFNSNLGNQFEFTQQIWANNPAFPFPPDGSQPGLDPVIGQGARAPQKYAPEWGHNNVAEATDPIPQAVTMKGGEYFFMPSLAFLRSL |
| Enzyme Length | 464 |
| Uniprot Accession Number | K7N5M8 |
| Absorption | |
| Active Site | ACT_SITE 203; /note=Proton acceptor; /evidence=ECO:0000250|UniProtKB:Q47KB1 |
| 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:23054399}; 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:23054399}; CATALYTIC ACTIVITY: Reaction=2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2 H2O; Xref=Rhea:RHEA:56136, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240, ChEBI:CHEBI:139520, ChEBI:CHEBI:139521; EC=1.11.1.7; Evidence={ECO:0000269|PubMed:23054399}; CATALYTIC ACTIVITY: Reaction=2 H2O2 + Reactive Blue 5 = 2,2'-disulfonyl azobenzene + 3-[(4-amino-6-chloro-1,3,5-triazin-2-yl)amino]benzenesulfonate + 2 H(+) + 2 H2O + phthalate; Xref=Rhea:RHEA:28086, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16240, ChEBI:CHEBI:17563, ChEBI:CHEBI:63950, ChEBI:CHEBI:63955, ChEBI:CHEBI:64278; EC=1.11.1.19; Evidence={ECO:0000269|PubMed:23054399}; |
| DNA Binding | |
| EC Number | 1.11.1.16; 1.11.1.19; 1.11.1.7 |
| Enzyme Function | FUNCTION: Displays both high peroxidase and manganese peroxidase activity. Is likely involved in lignin degradation. Also has a Mn-dependent oxidase mode of action that expands its substrate scope in vitro; is thus able to catalyze the O(2)- and Mn-dependent oxidative decarboxylation of 4-methoxymandelate to anisaldehyde. {ECO:0000269|PubMed:23054399}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 4.5 for the H(2)O(2)-dependent oxidation of Reactive Blue 5, and 5.0 for the O(2)-dependent oxidation of 4-methoxymandelate. {ECO:0000269|PubMed:23054399}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Beta strand (13); Chain (1); Helix (21); Metal binding (4); Turn (7) |
| Keywords | 3D-structure;Heme;Iron;Manganese;Metal-binding;Oxidoreductase;Peroxidase;Secreted |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:23054399}. Note=Although no signal sequence is found, the secretory machinery for actinomycetes is not fully characterized, and the low pH optimum for DyP2 along with the observation that many DyPs have been isolated from the secreted protein fraction imply that DyP2 could be secreted and still possibly play a role in extracellular oxidation chemistry (PubMed:23054399). |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 4G2C; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 50,225 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=13 uM for ABTS {ECO:0000269|PubMed:23054399}; KM=48 uM for Reactive Blue 5 {ECO:0000269|PubMed:23054399}; KM=2.4 uM for Reactive Black 5 {ECO:0000269|PubMed:23054399}; KM=1.2 mM for 2,4-dichlorophenol {ECO:0000269|PubMed:23054399}; KM=210 uM for Mn(2+) (when assaying manganese peroxidase activity) {ECO:0000269|PubMed:23054399}; KM=760 uM for Mn(2+) (when assaying 4-methoxymandelate oxidase activity) {ECO:0000269|PubMed:23054399}; Note=kcat is 87 sec(-1) for peroxidase activity with ABTS as substrate. kcat is 34 sec(-1) for peroxidase activity with Reactive Blue 5 as substrate. kcat is 0.38 sec(-1) for peroxidase activity with Reactive Black 5 as substrate. kcat is 68 sec(-1) for peroxidase activity with 2,4-dichlorophenol as substrate. kcat is 24 sec(-1) for manganese peroxidase activity.; |
| Metal Binding | METAL 258; /note="Manganese"; /evidence="ECO:0000269|PubMed:23054399"; METAL 273; /note="Manganese"; /evidence="ECO:0000269|PubMed:23054399"; METAL 284; /note="Manganese"; /evidence="ECO:0000269|PubMed:23054399"; METAL 321; /note="Iron (heme axial ligand); via tele nitrogen"; /evidence="ECO:0000269|PubMed:23054399, ECO:0007744|PDB:4G2C" |
| Rhea ID | RHEA:22396; RHEA:22776; RHEA:56136; RHEA:28086 |
| Cross Reference Brenda | 1.11.1.19; |