Detail Information for IndEnz0018000790
IED ID IndEnz0018000790
Enzyme Type ID peroxidase000790
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
Organism Trametes hirsuta (White-rot fungus) (Coriolus hirsutus)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Fungi Dikarya Basidiomycota Agaricomycotina Agaricomycetes Agaricomycetes incertae sedis Polyporales Polyporaceae (bracket fungi) Trametes Trametes hirsuta (White-rot fungus) (Coriolus hirsutus)
Enzyme Sequence MSASSSDPFHSFAKTSFTSKAAKRATAHSLPPLPGPGDLPPGMNVEYDVAIVGSGPIGCTYARELVEAGFNVAMFEIGEIDSGLKIGSHKKNTVEYQKNIDKFVNVIQGQLMPVSVPVNTMVVDTLSPASWQASTFFVRNGANPEQDPLRNLSGQAVTRVVGGMSTHWTCATPRFEKLQRPLLVKNDSKADDAEWDRLYKKAESYFKTGTTQFAESIRHNLVLKKLQEEYKGVRDFQQIPLAATRQSPTFVEWSSAHTVFDLENRPNKDAPKQRFNLFPAVACTNVRRDNANSEIVGLDVRDLHGGKSITIKAKVYILTAGAVHNAQLLAASGFGQLGRPDPAKPLPSLLPYLGTHITEQTLVFCQTVMSTELINSVTADMTIVGKPGHPDYSVTYTPGNPNNKHPDWWNEKVKKHMMDHQEDPLPIPFEDPEPQVTTLFQATHPWHTQIHRDAFSYGAVQQSIDSRLIVDWRFFGRTEPKEENKLWFSDKITDAYNLRQPTFDFRFPGGREAEDMMTDMCVMSAKIGGFLPGSYPQFMEPGLVLHLGGTHRMGFDEKADKCCVDTDSRVFGFKNLFLGGCGNIPTAYAANPTLTAMSLAIKSCEYIKKNFEPSPNPVKHHN
Enzyme Length 622
Uniprot Accession Number P59097
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 30-50 degrees Celsius. Active and thermostable for 30 minutes up to 55 degrees Celsius. {ECO:0000269|Ref.1};
PH Dependency BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6. Active and stable from pH 3 to 9. {ECO:0000269|Ref.1};
Pathway
nucleotide Binding
Features Active site (2); Binding site (2); Chain (1); Modified residue (1); Propeptide (1); Sequence conflict (2); 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: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 69,082
Kinetics
Metal Binding
Rhea ID RHEA:10552
Cross Reference Brenda