| IED ID | IndEnz0018000881 |
| Enzyme Type ID | peroxidase000881 |
| Protein Name |
Pyranose 2-oxidase P2O P2Ox POD POx PROD Pyranose oxidase EC 1.1.3.10 FAD-oxidoreductase Glucose 2-oxidase Pyranose:oxygen 2-oxidoreductase |
| Gene Name | p2ox pox |
| 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 | MFLDTTPFRADEPYDVFIAGSGPIGATFAKLCVDANLRVCMVEIGAADSFTSKPMKGDPNAPRSVQFGPGQVPIPGYHKKNEIEYQKDIDRFVNVIKGALSTCSIPTSNNHIATLDPSVVSNSLDKPFISLGKNPAQNPFVNLGAEAVTRGVGGMSTHWTCATPEFFAPADFNAPHRERPKLSTDAAEDARIWKDLYAQAKEIIGTSTTEFDHSIRHNLVLRKYNDIFQKENVIREFSPLPLACHRLTDPDYVEWHATDRILEELFTDPVKRGRFTLLTNHRCTKLVFKHYRPGEENEVDYALVEDLLPHMQNPGNPASVKKIYARSYVVACGAVATAQVLANSHIPPDDVVIPFPGGEKGSGGGERDATIPTPLMPMLGKYITEQPMTFCQVVLDSSLMEVVRNPPWPGLDWWKEKVARHVEAFPNDPIPIPFRDPEPQVTIKFTEEHPWHVQIHRDAFSYGAVAENMDTRVIVDYRFFGYTEPQEANELVFQQHYRDAYDMPQPTFKFTMSQDDRARARRMMDDMCNIALKIGGYLPGSEPQFMTPGLALHLAGTTRCGLDTQKTVGNTHCKVHNFNNLYVGGNGVIETGFAANPTLTSICYAIRASNDIIAKFGRHRG |
| Enzyme Length | 621 |
| Uniprot Accession Number | Q6QWR1 |
| Absorption | |
| Active Site | ACT_SITE 553; /note=Proton acceptor; /evidence=ECO:0000250|UniProtKB:E4QP00; ACT_SITE 596; /evidence=ECO:0000250 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by HgCl(2). |
| Binding Site | BINDING 454; /note=Substrate; /evidence=ECO:0000250; BINDING 456; /note=Substrate; /evidence=ECO:0000250 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=D-glucose + O2 = 2-dehydro-D-glucose + H2O2; Xref=Rhea:RHEA:10552, ChEBI:CHEBI:4167, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:16609; EC=1.1.3.10; |
| DNA Binding | |
| EC Number | 1.1.3.10 |
| Enzyme Function | FUNCTION: Catalyzes the oxidation of various aldopyranoses and disaccharides on carbon-2 to the corresponding 2-keto sugars concomitant with the reduction of O(2) to H(2)O(2). Plays an important role in lignin degradation of wood rot fungi by supplying the essential cosubstrate H(2)O(2) for the ligninolytic peroxidases, lignin peroxidase and manganese-dependent peroxidase. The preferred substrate is D-glucose which is converted to 2-dehydro-D-glucose, an intermediate of a secondary metabolic pathway leading to the antibiotic cortalcerone. Acts also on D-xylose, together with D-glucose the major sugars derived from wood, on L-sorbose, D-galactose and 1,5-anhydroglucitol, a diagnostic marker of diabetes mellitus. {ECO:0000269|PubMed:8661938, ECO:0000269|Ref.3}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 55 degrees Celsius. Thermostable for 2 hours up to 70 degrees Celsius. {ECO:0000269|PubMed:9210340}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0-8.5. Active from pH 4.5 to 10. Stable from pH 4 to 11. {ECO:0000269|PubMed:9210340}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Beta strand (30); Binding site (2); Chain (1); Helix (20); Modified residue (1); Propeptide (1); Sequence conflict (2); Turn (5) |
| Keywords | 3D-structure;Direct protein sequencing;FAD;Flavoprotein;Oxidoreductase;Periplasm |
| Interact With | |
| Induction | INDUCTION: Induced by carbon starvation. {ECO:0000269|PubMed:15466516, ECO:0000269|PubMed:16348809}. |
| Subcellular Location | SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:16348809}. Note=Hyphal periplasmic space. |
| Modified Residue | MOD_RES 158; /note=Tele-8alpha-FAD histidine; /evidence=ECO:0000250 |
| Post Translational Modification | PTM: Not glycosylated. |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (3) |
| Cross Reference PDB | 4MIF; 4MIG; 4MIH; |
| Mapped Pubmed ID | 24282677; |
| Motif | |
| Gene Encoded By | |
| Mass | 69,298 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=83.2 uM for O(2) {ECO:0000269|PubMed:9210340}; KM=1.43 mM for D-glucose {ECO:0000269|PubMed:9210340}; KM=1.53 mM for alpha-D-glucose {ECO:0000269|PubMed:9210340}; KM=0.97 mM for beta-D-glucose {ECO:0000269|PubMed:9210340}; KM=55 mM for 2-deoxy-D-glucose {ECO:0000269|PubMed:9210340}; KM=25 mM for D-xylose {ECO:0000269|PubMed:9210340}; KM=108 mM for L-sorbose {ECO:0000269|PubMed:9210340}; Vmax=26.64 uM/min/mg enzyme towards O(2) {ECO:0000269|PubMed:9210340}; |
| Metal Binding | |
| Rhea ID | RHEA:10552 |
| Cross Reference Brenda | 1.1.3.10; |