PhanerochaeteV1, Main, Exploration, bibRecord, 000E06

Lignin-degrading peroxidases of Phanerochaete chrysosporium.

Identifieur interne : 000E06 ( Main/Exploration ); précédent : 000E05; suivant : 000E07

Lignin-degrading peroxidases of Phanerochaete chrysosporium.

Auteurs : D. Cai [États-Unis] ; M. Tien

Source :

Journal of biotechnology [ 0168-1656 ] ; 1993.

RBID : pubmed:7763834

Descripteurs français

KwdFr :
- Basidiomycota (enzymologie), Cinétique (MeSH), Données de séquences moléculaires (MeSH), Hème (composition chimique), Lignine (métabolisme), Peroxidases (composition chimique), Peroxidases (métabolisme), Sites de fixation (MeSH), Séquence d'acides aminés (MeSH).
MESH :
- composition chimique : Hème, Peroxidases.
- enzymologie : Basidiomycota.
- métabolisme : Lignine, Peroxidases.
- Cinétique, Données de séquences moléculaires, Sites de fixation, Séquence d'acides aminés.

English descriptors

KwdEn :
- Amino Acid Sequence (MeSH), Basidiomycota (enzymology), Binding Sites (MeSH), Heme (chemistry), Kinetics (MeSH), Lignin (metabolism), Molecular Sequence Data (MeSH), Peroxidases (chemistry), Peroxidases (metabolism).
MESH :
- chemical , chemistry : Heme, Peroxidases.
- enzymology : Basidiomycota.
- chemical , metabolism : Lignin, Peroxidases.
- Amino Acid Sequence, Binding Sites, Kinetics, Molecular Sequence Data.

Abstract

Lignin and manganese peroxidases are secreted by the basidiomycete Phanerochaete chrysosporium during secondary metabolism. These enzymes play major roles in lignin degradation. The active site amino acid sequence of these lignin-degrading peroxidases is similar to that of horseradish peroxidase (HRP) and cytochrome c peroxidase (CcP). The mechanism by which they oxidize substrates also appears to be the similar. pH has a similar effect on lignin peroxidase compound I formation as on HRP or CcP; however, the pKa controlling compound I formation for lignin peroxidase appears to be much lower. Lignin-degrading peroxidases are able to catalyze the oxidation of substrates with high redox potential. This unique ability is consistent with a heme active site of low electron density, which is indicated by high redox potential.

DOI: 10.1016/0168-1656(93)90029-m
PubMed: 7763834

Affiliations:

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Le document en format XML

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<keywords scheme="KwdFr" xml:lang="fr"><term>Basidiomycota (enzymologie)</term>
<term>Cinétique (MeSH)</term>
<term>Données de séquences moléculaires (MeSH)</term>
<term>Hème (composition chimique)</term>
<term>Lignine (métabolisme)</term>
<term>Peroxidases (composition chimique)</term>
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<term>Séquence d'acides aminés</term>
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<front><div type="abstract" xml:lang="en">Lignin and manganese peroxidases are secreted by the basidiomycete Phanerochaete chrysosporium during secondary metabolism. These enzymes play major roles in lignin degradation. The active site amino acid sequence of these lignin-degrading peroxidases is similar to that of horseradish peroxidase (HRP) and cytochrome c peroxidase (CcP). The mechanism by which they oxidize substrates also appears to be the similar. pH has a similar effect on lignin peroxidase compound I formation as on HRP or CcP; however, the pKa controlling compound I formation for lignin peroxidase appears to be much lower. Lignin-degrading peroxidases are able to catalyze the oxidation of substrates with high redox potential. This unique ability is consistent with a heme active site of low electron density, which is indicated by high redox potential.</div>
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<Month>09</Month>
<Day>02</Day>
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<DateRevised><Year>2019</Year>
<Month>09</Month>
<Day>13</Day>
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<Title>Journal of biotechnology</Title>
<ISOAbbreviation>J Biotechnol</ISOAbbreviation>
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<ArticleTitle>Lignin-degrading peroxidases of Phanerochaete chrysosporium.</ArticleTitle>
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<Abstract><AbstractText>Lignin and manganese peroxidases are secreted by the basidiomycete Phanerochaete chrysosporium during secondary metabolism. These enzymes play major roles in lignin degradation. The active site amino acid sequence of these lignin-degrading peroxidases is similar to that of horseradish peroxidase (HRP) and cytochrome c peroxidase (CcP). The mechanism by which they oxidize substrates also appears to be the similar. pH has a similar effect on lignin peroxidase compound I formation as on HRP or CcP; however, the pKa controlling compound I formation for lignin peroxidase appears to be much lower. Lignin-degrading peroxidases are able to catalyze the oxidation of substrates with high redox potential. This unique ability is consistent with a heme active site of low electron density, which is indicated by high redox potential.</AbstractText>
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Lignin-degrading peroxidases of Phanerochaete chrysosporium.

Lignin-degrading peroxidases of Phanerochaete chrysosporium.

Source :

Descripteurs français

English descriptors

Abstract

Links toward previous steps (curation, corpus...)

Le document en format XML

Pour manipuler ce document sous Unix (Dilib)

Pour mettre un lien sur cette page dans le réseau Wicri

Pour générer des pages wiki