Glyoxal oxidases: their nature and properties.
Identifieur interne : 000168 ( Main/Exploration ); précédent : 000167; suivant : 000169Glyoxal oxidases: their nature and properties.
Auteurs : Marianne Daou [France] ; Craig B. Faulds [France]Source :
- World journal of microbiology & biotechnology [ 1573-0972 ] ; 2017.
Descripteurs français
- KwdFr :
- Alcohol oxidoreductases (métabolisme), Aldéhydes (métabolisme), Champignons (enzymologie), Dépollution biologique de l'environnement (MeSH), Lignine (métabolisme), Métabolisme glucidique (MeSH), Oxydoréduction (MeSH), Peroxyde d'hydrogène (métabolisme), Protéines fongiques (métabolisme), Protéines végétales (métabolisme), Vitis (enzymologie).
- MESH :
- enzymologie : Champignons, Vitis.
- métabolisme : Alcohol oxidoreductases, Aldéhydes, Lignine, Peroxyde d'hydrogène, Protéines fongiques, Protéines végétales.
- Dépollution biologique de l'environnement, Métabolisme glucidique, Oxydoréduction.
English descriptors
- KwdEn :
- Alcohol Oxidoreductases (metabolism), Aldehydes (metabolism), Biodegradation, Environmental (MeSH), Carbohydrate Metabolism (MeSH), Fungal Proteins (metabolism), Fungi (enzymology), Hydrogen Peroxide (metabolism), Lignin (metabolism), Oxidation-Reduction (MeSH), Plant Proteins (metabolism), Vitis (enzymology).
- MESH :
- chemical , metabolism : Alcohol Oxidoreductases, Aldehydes, Fungal Proteins, Hydrogen Peroxide, Lignin, Plant Proteins.
- enzymology : Fungi, Vitis.
- Biodegradation, Environmental, Carbohydrate Metabolism, Oxidation-Reduction.
Abstract
H2O2 has been found to be required for the activity of the main microbial enzymes responsible for lignin oxidative cleavage, peroxidases. Along with other small radicals, it is implicated in the early attack of plant biomass by fungi. Among the few extracellular H2O2-generating enzymes known are the glyoxal oxidases (GLOX). GLOX is a copper-containing enzyme, sharing high similarity at the level of active site structure and chemistry with galactose oxidase. Genes encoding GLOX enzymes are widely distributed among wood-degrading fungi especially white-rot degraders, plant pathogenic and symbiotic fungi. GLOX has also been identified in plants. Although widely distributed, only few examples of characterized GLOX exist. The first characterized fungal GLOX was isolated from Phanerochaete chrysosporium. The GLOX from Utilago maydis has a role in filamentous growth and pathogenicity. More recently, two other glyoxal oxidases from the fungus Pycnoporus cinnabarinus were also characterized. In plants, GLOX from Vitis pseudoreticulata was found to be implicated in grapevine defence mechanisms. Fungal GLOX were found to be activated by peroxidases in vitro suggesting a synergistic and regulatory relationship between these enzymes. The substrates oxidized by GLOX are mainly aldehydes generated during lignin and carbohydrates degradation. The reactions catalysed by this enzyme such as the oxidation of toxic molecules and the production of valuable compounds (organic acids) makes GLOX a promising target for biotechnological applications. This aspect on GLOX remains new and needs to be investigated.
DOI: 10.1007/s11274-017-2254-1
PubMed: 28390013
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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Faulds</name><affiliation wicri:level="3"><nlm:affiliation>Aix Marseille University, INRA, UMR1163 Biodiversité et Biotechnologie Fongiques (BBF), Marseille, France. craig.faulds@univ-amu.fr.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Aix Marseille University, INRA, UMR1163 Biodiversité et Biotechnologie Fongiques (BBF), Marseille</wicri:regionArea><placeName><region type="region">Provence-Alpes-Côte d'Azur</region><region type="old region">Provence-Alpes-Côte d'Azur</region><settlement type="city">Marseille</settlement></placeName></affiliation></author></analytic><series><title level="j">World journal of microbiology & biotechnology</title><idno type="eISSN">1573-0972</idno><imprint><date when="2017" type="published">2017</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Alcohol Oxidoreductases (metabolism)</term><term>Aldehydes (metabolism)</term><term>Biodegradation, Environmental (MeSH)</term><term>Carbohydrate Metabolism (MeSH)</term><term>Fungal Proteins (metabolism)</term><term>Fungi (enzymology)</term><term>Hydrogen Peroxide (metabolism)</term><term>Lignin (metabolism)</term><term>Oxidation-Reduction (MeSH)</term><term>Plant Proteins (metabolism)</term><term>Vitis (enzymology)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Alcohol oxidoreductases (métabolisme)</term><term>Aldéhydes (métabolisme)</term><term>Champignons (enzymologie)</term><term>Dépollution biologique de l'environnement (MeSH)</term><term>Lignine (métabolisme)</term><term>Métabolisme glucidique (MeSH)</term><term>Oxydoréduction (MeSH)</term><term>Peroxyde d'hydrogène (métabolisme)</term><term>Protéines fongiques (métabolisme)</term><term>Protéines végétales (métabolisme)</term><term>Vitis (enzymologie)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Alcohol Oxidoreductases</term><term>Aldehydes</term><term>Fungal Proteins</term><term>Hydrogen Peroxide</term><term>Lignin</term><term>Plant Proteins</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Champignons</term><term>Vitis</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Fungi</term><term>Vitis</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Alcohol oxidoreductases</term><term>Aldéhydes</term><term>Lignine</term><term>Peroxyde d'hydrogène</term><term>Protéines fongiques</term><term>Protéines végétales</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Biodegradation, Environmental</term><term>Carbohydrate Metabolism</term><term>Oxidation-Reduction</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Dépollution biologique de l'environnement</term><term>Métabolisme glucidique</term><term>Oxydoréduction</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">H<sub>2</sub>O<sub>2</sub> has been found to be required for the activity of the main microbial enzymes responsible for lignin oxidative cleavage, peroxidases. Along with other small radicals, it is implicated in the early attack of plant biomass by fungi. Among the few extracellular H<sub>2</sub>O<sub>2</sub>-generating enzymes known are the glyoxal oxidases (GLOX). GLOX is a copper-containing enzyme, sharing high similarity at the level of active site structure and chemistry with galactose oxidase. Genes encoding GLOX enzymes are widely distributed among wood-degrading fungi especially white-rot degraders, plant pathogenic and symbiotic fungi. GLOX has also been identified in plants. Although widely distributed, only few examples of characterized GLOX exist. The first characterized fungal GLOX was isolated from Phanerochaete chrysosporium. The GLOX from Utilago maydis has a role in filamentous growth and pathogenicity. More recently, two other glyoxal oxidases from the fungus Pycnoporus cinnabarinus were also characterized. In plants, GLOX from Vitis pseudoreticulata was found to be implicated in grapevine defence mechanisms. Fungal GLOX were found to be activated by peroxidases in vitro suggesting a synergistic and regulatory relationship between these enzymes. The substrates oxidized by GLOX are mainly aldehydes generated during lignin and carbohydrates degradation. The reactions catalysed by this enzyme such as the oxidation of toxic molecules and the production of valuable compounds (organic acids) makes GLOX a promising target for biotechnological applications. This aspect on GLOX remains new and needs to be investigated.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">28390013</PMID><DateCompleted><Year>2017</Year><Month>04</Month><Day>19</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1573-0972</ISSN><JournalIssue CitedMedium="Internet"><Volume>33</Volume><Issue>5</Issue><PubDate><Year>2017</Year><Month>May</Month></PubDate></JournalIssue><Title>World journal of microbiology & biotechnology</Title><ISOAbbreviation>World J Microbiol Biotechnol</ISOAbbreviation></Journal><ArticleTitle>Glyoxal oxidases: their nature and properties.</ArticleTitle><Pagination><MedlinePgn>87</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1007/s11274-017-2254-1</ELocationID><Abstract><AbstractText>H<sub>2</sub>O<sub>2</sub> has been found to be required for the activity of the main microbial enzymes responsible for lignin oxidative cleavage, peroxidases. Along with other small radicals, it is implicated in the early attack of plant biomass by fungi. Among the few extracellular H<sub>2</sub>O<sub>2</sub>-generating enzymes known are the glyoxal oxidases (GLOX). GLOX is a copper-containing enzyme, sharing high similarity at the level of active site structure and chemistry with galactose oxidase. Genes encoding GLOX enzymes are widely distributed among wood-degrading fungi especially white-rot degraders, plant pathogenic and symbiotic fungi. GLOX has also been identified in plants. Although widely distributed, only few examples of characterized GLOX exist. The first characterized fungal GLOX was isolated from Phanerochaete chrysosporium. The GLOX from Utilago maydis has a role in filamentous growth and pathogenicity. More recently, two other glyoxal oxidases from the fungus Pycnoporus cinnabarinus were also characterized. In plants, GLOX from Vitis pseudoreticulata was found to be implicated in grapevine defence mechanisms. Fungal GLOX were found to be activated by peroxidases in vitro suggesting a synergistic and regulatory relationship between these enzymes. The substrates oxidized by GLOX are mainly aldehydes generated during lignin and carbohydrates degradation. The reactions catalysed by this enzyme such as the oxidation of toxic molecules and the production of valuable compounds (organic acids) makes GLOX a promising target for biotechnological applications. This aspect on GLOX remains new and needs to be investigated.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Daou</LastName><ForeName>Marianne</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Aix Marseille University, INRA, UMR1163 Biodiversité et Biotechnologie Fongiques (BBF), Marseille, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Faulds</LastName><ForeName>Craig B</ForeName><Initials>CB</Initials><AffiliationInfo><Affiliation>Aix Marseille University, INRA, UMR1163 Biodiversité et Biotechnologie Fongiques (BBF), Marseille, France. craig.faulds@univ-amu.fr.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D016454">Review</PublicationType></PublicationTypeList><ArticleDate 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IdType="pubmed">15578222</ArticleId></ArticleIdList></Reference></ReferenceList></PubmedData></pubmed><affiliations><list><country><li>France</li></country><region><li>Provence-Alpes-Côte d'Azur</li></region><settlement><li>Marseille</li></settlement></list><tree><country name="France"><region name="Provence-Alpes-Côte d'Azur"><name sortKey="Daou, Marianne" sort="Daou, Marianne" uniqKey="Daou M" first="Marianne" last="Daou">Marianne Daou</name></region><name sortKey="Faulds, Craig B" sort="Faulds, Craig B" uniqKey="Faulds C" first="Craig B" last="Faulds">Craig B. 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