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Release of the FAD domain from cellobiose oxidase by proteases from cellulolytic cultures of Phanerochaete chrysosporium.
Department of Biochemistry, University of Georgia, Athens 30602-7229.
Evidence has previously suggested that cellobiose:quinone oxidoreductase (CBQ) in cellulolytic cultures of Phanerochaete chrysosporium might be produced from cellobiose oxidase (CBO) by proteolytic cleavage. This study demonstrates that the ratio of CBO activity to (CBO + CBQ) activity declines with decreasing culture pH, while protease activity increases. Furthermore, we demonstrate that endogenous P. chrysosporium proteases can only cleave CBO when the enzyme is bound to cellulose. This is the first demonstration that the proteases produced in cellulolytic cultures of P. chrysosporium can release the FAD domain from CBO.
PMID: 8392950 [PubMed - indexed for MEDLINE]
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Cited by 6 PubMed Central articles
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Cellobiose Dehydrogenase, an Active Agent in Cellulose Depolymerization.
Mansfield SD, De Jong E, Saddler JN.
Appl Environ Microbiol. 1997 Oct; 63(10):3804-3809.
[Appl Environ Microbiol. 1997]
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Purification and Characterization of Cellobiose Dehydrogenases from the White Rot Fungus Trametes versicolor.
Roy BP, Dumonceaux T, Koukoulas AA, Archibald FS.
Appl Environ Microbiol. 1996 Dec; 62(12):4417-4427.
[Appl Environ Microbiol. 1996]
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Characterization of carbohydrate-binding cytochrome b562 from the white-rot fungus Phanerochaete chrysosporium.
Yoshida M, Igarashi K, Wada M, Kaneko S, Suzuki N, Matsumura H, Nakamura N, Ohno H, Samejima M.
Appl Environ Microbiol. 2005 Aug; 71(8):4548-55.
[Appl Environ Microbiol. 2005]
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