| IED ID | IndEnz0018001275 |
| Enzyme Type ID | peroxidase001275 |
| 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 p2o |
| Organism | Trametes pubescens (White-rot fungus) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Basidiomycota Agaricomycotina Agaricomycetes Agaricomycetes incertae sedis Polyporales Polyporaceae (bracket fungi) Trametes Trametes pubescens (White-rot fungus) |
| Enzyme Sequence | MSTSSSDPFYNFAKTSFKSAAAQKASATSLPPLPGPDQKVPGMDIKYDVVIVGSGPIGCTYARELVEAGYKVAMFDIGEIDSGLKIGAHKKNTVEYQKNIDKFVNVIQGQLMSVSVPVNKLVVDTLSPTSWQASTFFVRNGSNPEQDPLRNLSGQAVTRVVGGMSTHWTCATPRFDREQRPLLVKDDPDADDAIWDQLYTKAESYFKTGTDQFNESIRHNLVLNKLAEEYKGQRTFQQIPLAATRRNPTFVEWSSANTVFDLQNRPNIDAPEERFNLFPAVACERVMRNASNTAIESLHIRDLISGDRFAIQADVYVLTAGAVHNTQLLVNSGFGKLGRPDPANPPELLPFLGSYITEQSLVFCQTVMSTELIDSVKSDMTIIGNPGELGYSVSYMPGASTNKHPDWWNEKVQNHMMQHQEDPLPIPFEDPEPQVTTLFQPSHPWHTQIHRDAFSYGAVQQSIDSRLIVDWRFFGRTEPKEENKLWFSDKITDAYNMPQPTFDFRFPAGRTSQEAEDMMTDMCVMSAKIGGFLPGSLPQFMEPGLVLHLGGTHRMGFDEQEDNCCVDTDSRVFGFNNLFLGGCGNIPTAYGANPTLTAMSLAIKSCEYIKKNFTPSPFTPAQ |
| Enzyme Length | 622 |
| Uniprot Accession Number | Q5G234 |
| Absorption | |
| Active Site | ACT_SITE 548; /note=Proton acceptor; /evidence=ECO:0000250|UniProtKB:E4QP00; ACT_SITE 593; /evidence=ECO:0000250 |
| Activity Regulation | |
| Binding Site | BINDING 448; /note=Substrate; /evidence=ECO:0000250; BINDING 450; /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 (By similarity). {ECO:0000250, ECO:0000269|PubMed:16105703}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.5-6.5. {ECO:0000269|PubMed:16105703}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Binding site (2); Chain (1); Modified residue (1); Propeptide (1); Signal peptide (1) |
| Keywords | 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:0000250 |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..28; /evidence=ECO:0000250 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 69,214 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=133 mM for L-arabinose (at pH 6.5 and 30 degrees Celsius) {ECO:0000269|PubMed:16105703}; KM=9.91 mM for D-galactose (at pH 6.5 and 30 degrees Celsius) {ECO:0000269|PubMed:16105703}; KM=1.31 mM for D-glucose (at pH 6.5 and 30 degrees Celsius) {ECO:0000269|PubMed:16105703}; KM=157 mM for melibiose (at pH 6.5 and 30 degrees Celsius) {ECO:0000269|PubMed:16105703}; KM=123 mM for ribose (at pH 6.5 and 30 degrees Celsius) {ECO:0000269|PubMed:16105703}; KM=75.4 mM for L-sorbose (at pH 6.5 and 30 degrees Celsius) {ECO:0000269|PubMed:16105703}; KM=36.2 mM for D-xylose (at pH 6.5 and 30 degrees Celsius) {ECO:0000269|PubMed:16105703}; Vmax=0.08 umol/min/mg enzyme toward L-arabinose (at pH 6.5 and 30 degrees Celsius) {ECO:0000269|PubMed:16105703}; Vmax=1.52 umol/min/mg enzyme toward D-galactose (at pH 6.5 and 30 degrees Celsius) {ECO:0000269|PubMed:16105703}; Vmax=9.32 umol/min/mg enzyme toward D-glucose (at pH 6.5 and 30 degrees Celsius) {ECO:0000269|PubMed:16105703}; Vmax=1.30 umol/min/mg enzyme toward melibiose (at pH 6.5 and 30 degrees Celsius) {ECO:0000269|PubMed:16105703}; Vmax=0.01 umol/min/mg enzyme toward ribose (at pH 6.5 and 30 degrees Celsius) {ECO:0000269|PubMed:16105703}; Vmax=12.50 umol/min/mg enzyme toward L-sorbose (at pH 6.5 and 30 degrees Celsius) {ECO:0000269|PubMed:16105703}; Vmax=4.02 umol/min/mg enzyme toward D-xylose (at pH 6.5 and 30 degrees Celsius) {ECO:0000269|PubMed:16105703}; |
| Metal Binding | |
| Rhea ID | RHEA:10552 |
| Cross Reference Brenda | 1.1.3.10; |