The heme-independent manganese-peroxidase activity depends on the presence of the C-terminal domain within the Streptomyces reticuli catalase-peroxidase CpeB

DC FieldValueLanguage
dc.contributor.authorZou, PJ
dc.contributor.authorSchrempf, H
dc.date.accessioned2021-12-23T16:04:30Z-
dc.date.available2021-12-23T16:04:30Z-
dc.date.issued2000
dc.identifier.issn00142956
dc.identifier.urihttps://osnascholar.ub.uni-osnabrueck.de/handle/unios/6457-
dc.description.abstractStreptomyces reticuli produces a heme-containing homodimeric enzyme (160 kDa), the catalase-peroxidase CpeB, which is processed to the enzyme CpeC during prolonged growth. CpeC contains four subunits of 60 kDa each that do not include the C-terminal portion of the progenitor subunits. A genetically engineered cpeB gene encodes a truncated subunit lacking 195 of the C-terminal amino acids; four of these subunits assemble to form the enzyme CpeD. Heme binds most strongly in CpeB, least in CpeD. The catalase-peroxidase CpeB and its apo-form (obtained after extraction of heme) catalyze the peroxidation of Mn(II) to Mn(III), independent of the presence or absence of the heme inhibitor KCN. CpeC and CpeD, in contrast, do not exhibit manganese-peroxidase activity. The data show for the first time that a bacterial catalase-peroxidase has a heme-independent manganese-peroxidase activity, which depends on the presence of the C-terminal domain.
dc.language.isoen
dc.publisherWILEY
dc.relation.ispartofEUROPEAN JOURNAL OF BIOCHEMISTRY
dc.subjectACTIVATION
dc.subjectBiochemistry & Molecular Biology
dc.subjectcatalase-peroxidase
dc.subjectCLONING
dc.subjectcpeB gene
dc.subjectCRYSTAL-STRUCTURE
dc.subjectESCHERICHIA-COLI
dc.subjectGENE
dc.subjectmanganese-peroxidase
dc.subjectMYCOBACTERIUM-TUBERCULOSIS
dc.subjectPHANEROCHAETE-CHRYSOSPORIUM
dc.subjectPURIFICATION
dc.subjectRESISTANCE
dc.subjectRESOLUTION
dc.subjectstreptomycetes
dc.titleThe heme-independent manganese-peroxidase activity depends on the presence of the C-terminal domain within the Streptomyces reticuli catalase-peroxidase CpeB
dc.typejournal article
dc.identifier.doi10.1046/j.1432-1327.2000.01259.x
dc.identifier.isiISI:000087209500002
dc.description.volume267
dc.description.issue10
dc.description.startpage2840
dc.description.endpage2849
dc.publisher.place111 RIVER ST, HOBOKEN 07030-5774, NJ USA
dcterms.isPartOf.abbreviationEur. J. Biochem.
dcterms.oaStatusBronze
crisitem.author.deptFB 05 - Biologie/Chemie-
crisitem.author.deptidfb05-
crisitem.author.parentorgUniversität Osnabrück-
crisitem.author.netidScHi752-
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