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[1]
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NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 10-30; 66-96; 98-150; 182-191; 202-216; 223-229; 236-272; 275-282; 421-444; 458-472 AND 479-517, AND INDUCTION.
STRAIN=ATCC 24725 / CBS 481.73 / CCRC 36200 / NRRL 6361 / VKM-F-1767;
DOI=10.1128/AEM.70.10.5794-5800.2004; PubMed=15466516 [NCBI, ExPASy, EBI, Israel, Japan]
de Koker T.H.,
Mozuch M.D.,
Cullen D.,
Gaskell J.,
Kersten P.J.;
"Isolation and purification of pyranose 2-oxidase from Phanerochaete chrysosporium and characterization of gene structure and regulation.";
Appl. Environ. Microbiol. 70:5794-5800(2004).
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[2]
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PROTEIN SEQUENCE OF 66-96 AND 366-388, BIOPHYSICOCHEMICAL PROPERTIES, FAD-BINDING, AND TETRAMERIZATION.
DOI=10.1007/s002530050964; PubMed=9210340 [NCBI, ExPASy, EBI, Israel, Japan]
Artolozaga M.J.,
Kubatova E.,
Volc J.,
Kalisz H.M.;
"Pyranose 2-oxidase from Phanerochaete chrysosporium -- further biochemical characterisation.";
Appl. Microbiol. Biotechnol. 47:508-514(1997).
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[3]
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FUNCTION.
Volc J.,
Kubatova E.,
Sedmera P.,
Daniel G.,
Gabriel J.;
"Pyranose oxidase and pyranosone dehydratase: enzymes responsible for conversion of D-glucose to cortalcerone by the basidiomycete Phanerochaete chrysosporium.";
Arch. Microbiol. 156:297-301(1991).
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[4]
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SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND INDUCTION.
PubMed=16348809 [NCBI, ExPASy, EBI, Israel, Japan]
Daniel G.,
Volc J.,
Kubatova E.,
Nilsson T.;
"Ultrastructural and immunocytochemical studies on the H(2)O(2)-producing enzyme pyranose oxidase in Phanerochaete chrysosporium grown under liquid culture conditions.";
Appl. Environ. Microbiol. 58:3667-3676(1992).
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[5]
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FUNCTION.
DOI=10.1007/s002030050348; PubMed=8661938 [NCBI, ExPASy, EBI, Israel, Japan]
Volc J.,
Kubatova E.,
Daniel G.,
Prikrylova V.;
"Only C-2 specific glucose oxidase activity is expressed in ligninolytic cultures of the white rot fungus Phanerochaete chrysosporium.";
Arch. Microbiol. 165:421-424(1996).
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- 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.
- CATALYTIC ACTIVITY: D-glucose + O2 = 2-dehydro-D-glucose + H2O2.
- COFACTOR: Binds 1 FAD covalently per subunit.
- ENZYME REGULATION: Inhibited by HgCl(2).
- BIOPHYSICOCHEMICAL PROPERTIES:
| Kinetic parameters: |
KM=83.2 µM for O2; | | KM=1.43 mM for D-glucose; | | KM=1.53 mM for alpha-D-glucose; | | KM=0.97 mM for beta-D-glucose; | | KM=55 mM for 2-deoxy-D-glucose; | | KM=25 mM for D-xylose; | | KM=108 mM for L-sorbose; | | Vmax=26.64 µM/min/mg enzyme towards O(2); | | pH dependence: |
Optimum pH is 8.0-8.5. Active from pH 4.5 to 10. Stable from pH 4 to 11; | | Temperature dependence: |
Optimum temperature is 55 degrees Celsius. Thermostable for 2 hours up to 70 degrees Celsius; | |
- SUBUNIT: Homotetramer.
- SUBCELLULAR LOCATION: Periplasm. Note=Hyphal periplasmic space.
- DEVELOPMENTAL STAGE: During autolysis, associated with extracellular slime surrounding lysed hyphae.
- INDUCTION: Induced by carbon starvation.
- PTM: Not glycosylated.
- SIMILARITY: Belongs to the GMC oxidoreductase family.
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Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms.
Distributed under the Creative Commons Attribution-NoDerivs License.
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| Length: 621 AA [This is the length of the unprocessed precursor] |
Molecular weight: 69298 Da [This is the MW of the unprocessed precursor] |
CRC64: 08A1C1264D824A4C [This is a checksum on the sequence] |
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10 20 30 40 50 60
MFLDTTPFRA DEPYDVFIAG SGPIGATFAK LCVDANLRVC MVEIGAADSF TSKPMKGDPN
70 80 90 100 110 120
APRSVQFGPG QVPIPGYHKK NEIEYQKDID RFVNVIKGAL STCSIPTSNN HIATLDPSVV
130 140 150 160 170 180
SNSLDKPFIS LGKNPAQNPF VNLGAEAVTR GVGGMSTHWT CATPEFFAPA DFNAPHRERP
190 200 210 220 230 240
KLSTDAAEDA RIWKDLYAQA KEIIGTSTTE FDHSIRHNLV LRKYNDIFQK ENVIREFSPL
250 260 270 280 290 300
PLACHRLTDP DYVEWHATDR ILEELFTDPV KRGRFTLLTN HRCTKLVFKH YRPGEENEVD
310 320 330 340 350 360
YALVEDLLPH MQNPGNPASV KKIYARSYVV ACGAVATAQV LANSHIPPDD VVIPFPGGEK
370 380 390 400 410 420
GSGGGERDAT IPTPLMPMLG KYITEQPMTF CQVVLDSSLM EVVRNPPWPG LDWWKEKVAR
430 440 450 460 470 480
HVEAFPNDPI PIPFRDPEPQ VTIKFTEEHP WHVQIHRDAF SYGAVAENMD TRVIVDYRFF
490 500 510 520 530 540
GYTEPQEANE LVFQQHYRDA YDMPQPTFKF TMSQDDRARA RRMMDDMCNI ALKIGGYLPG
550 560 570 580 590 600
SEPQFMTPGL ALHLAGTTRC GLDTQKTVGN THCKVHNFNN LYVGGNGVIE TGFAANPTLT
610 620
SICYAIRASN DIIAKFGRHR G
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Q6QWR1 in FASTA format |
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