| IED ID | IndEnz0018000846 |
| Enzyme Type ID | peroxidase000846 |
| Protein Name |
Pyranose 2-oxidase P2Ox POD POx PROD Pyranose oxidase EC 1.1.3.10 FAD-oxidoreductase Glucose 2-oxidase Pyranose:oxygen 2-oxidoreductase |
| Gene Name | p2ox poxB |
| Organism | Phlebiopsis gigantea (White-rot fungus) (Peniophora gigantea) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Basidiomycota Agaricomycotina Agaricomycetes Agaricomycetes incertae sedis Polyporales Phanerochaetaceae Phlebiopsis Phlebiopsis gigantea (White-rot fungus) (Peniophora gigantea) |
| Enzyme Sequence | MSASSSDPFHSFAKTSFTSKAAKRATAHSLPPLPGPGDLPPGMNVEYDVAIVGSGPIGSTYARELVEAGFNVAMFEIGEIDSGLKIGSHKKNTVEYQKNIDKFVNVIQGQLMPVSVPVNTMVVDTLSPASWQASTFFVRNGANPEQDPLRNLSGQAVTRVVGGMSTHWTCATPRFEKLQRPLLVKNDPVADDAEWDRLYKKAESYFKTGTTQFAESIRHNLVLKKLQEEYKGVRDFQQIPLAATRQSPTFVEWSSAHTVFDLENRPNKDAPKQRFNLFPAVACTSVRRNDANSEIIGLDVRDLHGGKSITIKAKVYILTAGAVHNAQLLAASGFGQLGRPDPAKPLPSLLPYLGTHITEQTLVFCQTVMSTELINSVTADMTIVGKPGDPDYSVTYTSGSPNNKHPDWWNEKVKKHMMDHQEDPLPIPFEDPEPQVTTLFKASHPWHTQIHRDAFSYGAVQQSIDSRLIVDWRFFGRTEPKEENKLWFSDKITDAYNLPQPTFDFRFPGGREAEDMMTDMCVMSAKIGGFLPGSYPQFMEPGLVLHLGGTHRMGFDEKADKCCVDTDSRVFGFKNLFLGGCGNIPTAYAANPTLTAMSLAIKSCEYIKKNFEPSPNPVKHHN |
| Enzyme Length | 622 |
| Uniprot Accession Number | Q6UG02 |
| Absorption | |
| Active Site | ACT_SITE 546; /note=Proton acceptor; /evidence=ECO:0000250|UniProtKB:E4QP00; ACT_SITE 591; /evidence=ECO:0000250 |
| Activity Regulation | |
| Binding Site | BINDING 449; /note=Substrate; /evidence=ECO:0000250; BINDING 451; /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. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 44 degrees Celsius. Active from 30 to 55 degrees Celsius. Thermostable for 30 minutes up to 50 degrees Celsius. {ECO:0000269|PubMed:15660220, ECO:0000269|PubMed:8319689}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 4.5-6.0. Active from pH 4 to 7.5. Stable from pH 4 to 11. {ECO:0000269|PubMed:15660220, ECO:0000269|PubMed:8319689}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Binding site (2); Chain (1); Modified residue (1); Mutagenesis (3); Propeptide (1); Signal peptide (1) |
| Keywords | Direct protein sequencing;FAD;Flavoprotein;Oxidoreductase;Periplasm;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Periplasm {ECO:0000250}. Note=Hyphal periplasmic space. {ECO:0000250}. |
| Modified Residue | MOD_RES 167; /note=Tele-8alpha-FAD histidine; /evidence=ECO:0000305 |
| Post Translational Modification | PTM: Not glycosylated. |
| Signal Peptide | SIGNAL 1..28; /evidence=ECO:0000250 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 68,902 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.65 mM for O(2) {ECO:0000269|PubMed:15660220, ECO:0000269|PubMed:8319689}; KM=1.1 mM for D-glucose {ECO:0000269|PubMed:15660220, ECO:0000269|PubMed:8319689}; KM=11.3 mM for 2-deoxy-D-glucose {ECO:0000269|PubMed:15660220, ECO:0000269|PubMed:8319689}; KM=289 mM for methyl-beta-D-glucoside {ECO:0000269|PubMed:15660220, ECO:0000269|PubMed:8319689}; KM=29.4 mM for D-xylose {ECO:0000269|PubMed:15660220, ECO:0000269|PubMed:8319689}; KM=50 mM for L-sorbose {ECO:0000269|PubMed:15660220, ECO:0000269|PubMed:8319689}; KM=8.2 mM for D-galactose {ECO:0000269|PubMed:15660220, ECO:0000269|PubMed:8319689}; KM=55.7 mM for D-allose {ECO:0000269|PubMed:15660220, ECO:0000269|PubMed:8319689}; Vmax=10.4 umol/min/mg enzyme with D-glucose as substrate {ECO:0000269|PubMed:15660220, ECO:0000269|PubMed:8319689}; Vmax=4.5 umol/min/mg enzyme with 2-deoxy-D-glucose as substrate {ECO:0000269|PubMed:15660220, ECO:0000269|PubMed:8319689}; Vmax=2.9 umol/min/mg enzyme with methyl-beta-D-glucoside as substrate {ECO:0000269|PubMed:15660220, ECO:0000269|PubMed:8319689}; Vmax=4.3 umol/min/mg enzyme with D-xylose as substrate {ECO:0000269|PubMed:15660220, ECO:0000269|PubMed:8319689}; Vmax=7.9 umol/min/mg enzyme with L-sorbose as substrate {ECO:0000269|PubMed:15660220, ECO:0000269|PubMed:8319689}; Vmax=0.5 umol/min/mg enzyme with D-galactose as substrate {ECO:0000269|PubMed:15660220, ECO:0000269|PubMed:8319689}; Vmax=3.7 umol/min/mg enzyme with D-allose as substrate {ECO:0000269|PubMed:15660220, ECO:0000269|PubMed:8319689}; |
| Metal Binding | |
| Rhea ID | RHEA:10552 |
| Cross Reference Brenda | 1.1.3.10; |