Studies on compound I formation of the lignin peroxidase from Phanerochaete chrysosporium.
Identifieur interne : 001001 ( Main/Exploration ); précédent : 001000; suivant : 001002Studies on compound I formation of the lignin peroxidase from Phanerochaete chrysosporium.
Auteurs : A. Andrawis [États-Unis] ; K A Johnson ; M. TienSource :
- The Journal of biological chemistry [ 0021-9258 ] ; 1988.
Descripteurs français
- KwdFr :
- Chrysosporium (enzymologie), Concentration en ions d'hydrogène (MeSH), Concentration osmolaire (MeSH), Deuteromycota (enzymologie), Nitrates (métabolisme), Oxygénases (métabolisme), Peroxidases (MeSH), Peroxyde d'hydrogène (métabolisme), Spectrophotométrie atomique (MeSH), Séquence d'acides aminés (MeSH).
- MESH :
- enzymologie : Chrysosporium, Deuteromycota.
- métabolisme : Nitrates, Oxygénases, Peroxyde d'hydrogène.
- Concentration en ions d'hydrogène, Concentration osmolaire, Peroxidases, Spectrophotométrie atomique, Séquence d'acides aminés.
English descriptors
- KwdEn :
- MESH :
- chemical , metabolism : Hydrogen Peroxide, Nitrates, Oxygenases.
- enzymology : Chrysosporium, Mitosporic Fungi.
- Amino Acid Sequence, Hydrogen-Ion Concentration, Osmolar Concentration, Peroxidases, Spectrophotometry, Atomic.
Abstract
Ligninase, isolated from the wood-destroying fungus Phanerochaete chrysosporium, catalyzes the oxidation of lignin and lignin-related compounds. Ligninase reacts with H2O2 to form the classical peroxidase intermediates Compounds I and II. We have determined the activation energy of ligninase Compound I formation to be 5.9 kcal/mol. The effect of pH and ionic strength on the rate of ligninase Compound I formation was studied. In contrast to all other peroxidases, no pH effect was observed. This is despite homology of active-site amino acids residues (Tien, M., and Tu, C.-P. D. (1987) Nature 326, 520-523) which are proposed to affect the pH profile of Compound I formation. Ligninase Compound I formation can also be supported by organic peroxides. The second-order rate constants with the organic peroxides are lower, suggesting that H2O2 is the preferred substrate.
PubMed: 3335539
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence (MeSH)</term>
<term>Chrysosporium (enzymology)</term>
<term>Hydrogen Peroxide (metabolism)</term>
<term>Hydrogen-Ion Concentration (MeSH)</term>
<term>Mitosporic Fungi (enzymology)</term>
<term>Nitrates (metabolism)</term>
<term>Osmolar Concentration (MeSH)</term>
<term>Oxygenases (metabolism)</term>
<term>Peroxidases (MeSH)</term>
<term>Spectrophotometry, Atomic (MeSH)</term>
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<keywords scheme="KwdFr" xml:lang="fr"><term>Chrysosporium (enzymologie)</term>
<term>Concentration en ions d'hydrogène (MeSH)</term>
<term>Concentration osmolaire (MeSH)</term>
<term>Deuteromycota (enzymologie)</term>
<term>Nitrates (métabolisme)</term>
<term>Oxygénases (métabolisme)</term>
<term>Peroxidases (MeSH)</term>
<term>Peroxyde d'hydrogène (métabolisme)</term>
<term>Spectrophotométrie atomique (MeSH)</term>
<term>Séquence d'acides aminés (MeSH)</term>
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<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Hydrogen Peroxide</term>
<term>Nitrates</term>
<term>Oxygenases</term>
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<keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Chrysosporium</term>
<term>Deuteromycota</term>
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<keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Chrysosporium</term>
<term>Mitosporic Fungi</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Nitrates</term>
<term>Oxygénases</term>
<term>Peroxyde d'hydrogène</term>
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<keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term>
<term>Hydrogen-Ion Concentration</term>
<term>Osmolar Concentration</term>
<term>Peroxidases</term>
<term>Spectrophotometry, Atomic</term>
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<keywords scheme="MESH" xml:lang="fr"><term>Concentration en ions d'hydrogène</term>
<term>Concentration osmolaire</term>
<term>Peroxidases</term>
<term>Spectrophotométrie atomique</term>
<term>Séquence d'acides aminés</term>
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<front><div type="abstract" xml:lang="en">Ligninase, isolated from the wood-destroying fungus Phanerochaete chrysosporium, catalyzes the oxidation of lignin and lignin-related compounds. Ligninase reacts with H2O2 to form the classical peroxidase intermediates Compounds I and II. We have determined the activation energy of ligninase Compound I formation to be 5.9 kcal/mol. The effect of pH and ionic strength on the rate of ligninase Compound I formation was studied. In contrast to all other peroxidases, no pH effect was observed. This is despite homology of active-site amino acids residues (Tien, M., and Tu, C.-P. D. (1987) Nature 326, 520-523) which are proposed to affect the pH profile of Compound I formation. Ligninase Compound I formation can also be supported by organic peroxides. The second-order rate constants with the organic peroxides are lower, suggesting that H2O2 is the preferred substrate.</div>
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<Title>The Journal of biological chemistry</Title>
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<ArticleTitle>Studies on compound I formation of the lignin peroxidase from Phanerochaete chrysosporium.</ArticleTitle>
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<Abstract><AbstractText>Ligninase, isolated from the wood-destroying fungus Phanerochaete chrysosporium, catalyzes the oxidation of lignin and lignin-related compounds. Ligninase reacts with H2O2 to form the classical peroxidase intermediates Compounds I and II. We have determined the activation energy of ligninase Compound I formation to be 5.9 kcal/mol. The effect of pH and ionic strength on the rate of ligninase Compound I formation was studied. In contrast to all other peroxidases, no pH effect was observed. This is despite homology of active-site amino acids residues (Tien, M., and Tu, C.-P. D. (1987) Nature 326, 520-523) which are proposed to affect the pH profile of Compound I formation. Ligninase Compound I formation can also be supported by organic peroxides. The second-order rate constants with the organic peroxides are lower, suggesting that H2O2 is the preferred substrate.</AbstractText>
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