Serveur d'exploration sur le phanerochaete

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Lignin peroxidase-negative mutant of the white-rot basidiomycete Phanerochaete chrysosporium.

Identifieur interne : 000F49 ( Main/Exploration ); précédent : 000F48; suivant : 000F50

Lignin peroxidase-negative mutant of the white-rot basidiomycete Phanerochaete chrysosporium.

Auteurs : K. Boominathan [États-Unis] ; S B Dass ; T A Randall ; R L Kelley ; C A Reddy

Source :

RBID : pubmed:2294087

Descripteurs français

English descriptors

Abstract

Phanerochaete chrysosporium produces two classes of extracellular heme proteins, designated lignin peroxidases and manganese peroxidases, that play a key role in lignin degradation. In this study we isolated and characterized a lignin peroxidase-negative mutant (lip mutant) that showed 16% of the ligninolytic activity (14C-labeled synthetic lignin----14CO2) exhibited by the wild type. The lip mutant did not produce detectable levels of lignin peroxidase, whereas the wild type, under identical conditions, produced 96 U of lignin peroxidase per liter. Both the wild type and the mutant produced comparable levels of manganese peroxidase and glucose oxidase, a key H2O2-generating secondary metabolic enzyme in P. chrysosporium. Fast protein liquid chromatographic analysis of the concentrated extracellular fluid of the lip mutant confirmed that it produced only heme proteins with manganese peroxidase activity but no detectable lignin peroxidase activity, whereas both lignin peroxidase and manganese peroxidase activities were produced by the wild type. The lip mutant appears to be a regulatory mutant that is defective in the production of all the lignin peroxidases.

DOI: 10.1128/jb.172.1.260-265.1990
PubMed: 2294087
PubMed Central: PMC208426


Affiliations:


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Le document en format XML

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<div type="abstract" xml:lang="en">Phanerochaete chrysosporium produces two classes of extracellular heme proteins, designated lignin peroxidases and manganese peroxidases, that play a key role in lignin degradation. In this study we isolated and characterized a lignin peroxidase-negative mutant (lip mutant) that showed 16% of the ligninolytic activity (14C-labeled synthetic lignin----14CO2) exhibited by the wild type. The lip mutant did not produce detectable levels of lignin peroxidase, whereas the wild type, under identical conditions, produced 96 U of lignin peroxidase per liter. Both the wild type and the mutant produced comparable levels of manganese peroxidase and glucose oxidase, a key H2O2-generating secondary metabolic enzyme in P. chrysosporium. Fast protein liquid chromatographic analysis of the concentrated extracellular fluid of the lip mutant confirmed that it produced only heme proteins with manganese peroxidase activity but no detectable lignin peroxidase activity, whereas both lignin peroxidase and manganese peroxidase activities were produced by the wild type. The lip mutant appears to be a regulatory mutant that is defective in the production of all the lignin peroxidases.</div>
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<Reference>
<Citation>J Bacteriol. 1985 May;162(2):641-4</Citation>
<ArticleIdList>
<ArticleId IdType="pubmed">3921527</ArticleId>
</ArticleIdList>
</Reference>
<Reference>
<Citation>Arch Biochem Biophys. 1986 Feb 1;244(2):750-65</Citation>
<ArticleIdList>
<ArticleId IdType="pubmed">3080953</ArticleId>
</ArticleIdList>
</Reference>
<Reference>
<Citation>Nature. 1987 Apr 2-8;326(6112):520-3</Citation>
<ArticleIdList>
<ArticleId IdType="pubmed">3561490</ArticleId>
</ArticleIdList>
</Reference>
<Reference>
<Citation>Biochemistry. 1988 Jul 12;27(14):5365-70</Citation>
<ArticleIdList>
<ArticleId IdType="pubmed">3167051</ArticleId>
</ArticleIdList>
</Reference>
<Reference>
<Citation>Gene. 1988 Dec 15;73(1):77-85</Citation>
<ArticleIdList>
<ArticleId IdType="pubmed">2907500</ArticleId>
</ArticleIdList>
</Reference>
<Reference>
<Citation>Crit Rev Microbiol. 1987;15(2):141-68</Citation>
<ArticleIdList>
<ArticleId IdType="pubmed">3322681</ArticleId>
</ArticleIdList>
</Reference>
<Reference>
<Citation>Biochem J. 1988 Oct 15;255(2):445-50</Citation>
<ArticleIdList>
<ArticleId IdType="pubmed">3060110</ArticleId>
</ArticleIdList>
</Reference>
<Reference>
<Citation>Nucleic Acids Res. 1988 Feb 11;16(3):1219</Citation>
<ArticleIdList>
<ArticleId IdType="pubmed">3344218</ArticleId>
</ArticleIdList>
</Reference>
<Reference>
<Citation>Biochem Biophys Res Commun. 1986 Jun 13;137(2):649-56</Citation>
<ArticleIdList>
<ArticleId IdType="pubmed">3755339</ArticleId>
</ArticleIdList>
</Reference>
<Reference>
<Citation>Appl Environ Microbiol. 1989 Jan;55(1):154-8</Citation>
<ArticleIdList>
<ArticleId IdType="pubmed">2705768</ArticleId>
</ArticleIdList>
</Reference>
<Reference>
<Citation>Proc Natl Acad Sci U S A. 1984 Apr;81(8):2280-4</Citation>
<ArticleIdList>
<ArticleId IdType="pubmed">16593451</ArticleId>
</ArticleIdList>
</Reference>
<Reference>
<Citation>J Biol Chem. 1982 Oct 10;257(19):11455-62</Citation>
<ArticleIdList>
<ArticleId IdType="pubmed">6288685</ArticleId>
</ArticleIdList>
</Reference>
<Reference>
<Citation>Gene. 1988 Oct 15;70(1):127-37</Citation>
<ArticleIdList>
<ArticleId IdType="pubmed">3240864</ArticleId>
</ArticleIdList>
</Reference>
<Reference>
<Citation>Biochem Biophys Res Commun. 1985 Aug 30;131(1):436-41</Citation>
<ArticleIdList>
<ArticleId IdType="pubmed">4038305</ArticleId>
</ArticleIdList>
</Reference>
<Reference>
<Citation>Arch Biochem Biophys. 1985 Aug 15;241(1):304-14</Citation>
<ArticleIdList>
<ArticleId IdType="pubmed">4026322</ArticleId>
</ArticleIdList>
</Reference>
<Reference>
<Citation>Gene. 1987;60(1):93-102</Citation>
<ArticleIdList>
<ArticleId IdType="pubmed">3440521</ArticleId>
</ArticleIdList>
</Reference>
<Reference>
<Citation>Arch Biochem Biophys. 1984 Nov 1;234(2):353-62</Citation>
<ArticleIdList>
<ArticleId IdType="pubmed">6497376</ArticleId>
</ArticleIdList>
</Reference>
<Reference>
<Citation>J Biol Chem. 1989 Mar 25;264(9):5036-40</Citation>
<ArticleIdList>
<ArticleId IdType="pubmed">2925681</ArticleId>
</ArticleIdList>
</Reference>
<Reference>
<Citation>J Biol Chem. 1987 Jan 5;262(1):419-24</Citation>
<ArticleIdList>
<ArticleId IdType="pubmed">2432065</ArticleId>
</ArticleIdList>
</Reference>
<Reference>
<Citation>J Bacteriol. 1987 May;169(5):2195-201</Citation>
<ArticleIdList>
<ArticleId IdType="pubmed">3553159</ArticleId>
</ArticleIdList>
</Reference>
<Reference>
<Citation>Appl Environ Microbiol. 1986 Aug;52(2):251-4</Citation>
<ArticleIdList>
<ArticleId IdType="pubmed">16347125</ArticleId>
</ArticleIdList>
</Reference>
<Reference>
<Citation>Appl Environ Microbiol. 1985 Nov;50(5):1274-8</Citation>
<ArticleIdList>
<ArticleId IdType="pubmed">16346932</ArticleId>
</ArticleIdList>
</Reference>
<Reference>
<Citation>Mol Cell Biol. 1989 Jun;9(6):2743-7</Citation>
<ArticleIdList>
<ArticleId IdType="pubmed">2761543</ArticleId>
</ArticleIdList>
</Reference>
<Reference>
<Citation>Annu Rev Microbiol. 1987;41:465-505</Citation>
<ArticleIdList>
<ArticleId IdType="pubmed">3318677</ArticleId>
</ArticleIdList>
</Reference>
<Reference>
<Citation>Biochem Biophys Res Commun. 1988 Sep 15;155(2):626-33</Citation>
<ArticleIdList>
<ArticleId IdType="pubmed">2844176</ArticleId>
</ArticleIdList>
</Reference>
<Reference>
<Citation>Immunology. 1986 Jun;58(2):257-62</Citation>
<ArticleIdList>
<ArticleId IdType="pubmed">2423445</ArticleId>
</ArticleIdList>
</Reference>
<Reference>
<Citation>Arch Biochem Biophys. 1985 Nov 1;242(2):329-41</Citation>
<ArticleIdList>
<ArticleId IdType="pubmed">4062285</ArticleId>
</ArticleIdList>
</Reference>
<Reference>
<Citation>Appl Environ Microbiol. 1983 Jun;45(6):1741-7</Citation>
<ArticleIdList>
<ArticleId IdType="pubmed">16346307</ArticleId>
</ArticleIdList>
</Reference>
<Reference>
<Citation>J Bacteriol. 1986 Apr;166(1):269-74</Citation>
<ArticleIdList>
<ArticleId IdType="pubmed">3957868</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
</PubmedData>
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