Fungal aryl-alcohol oxidase: a peroxide-producing flavoenzyme involved in lignin degradation

Aryl-alcohol oxidase (AAO) is an extracellular flavoprotein providing the H 2 O 2 required by ligninolytic peroxidases for fungal degradation of lignin, the key step for carbon recycling in land ecosystems. O 2 activation by Pleurotus eryngii AAO takes place during the redox-cycling of p- methoxylat...

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Published inApplied microbiology and biotechnology Vol. 93; no. 4; pp. 1395 - 1410
Main Authors Hernández-Ortega, Aitor, Ferreira, Patricia, Martínez, Angel T.
Format Journal Article
LanguageEnglish
Published Berlin/Heidelberg Springer-Verlag 01.02.2012
Springer Nature B.V
Subjects
active sites
Alcohol
Alcohol Oxidoreductases
Alcohol Oxidoreductases - chemistry
Alcohol Oxidoreductases - genetics
Alcohol Oxidoreductases - metabolism
Alcohols
Aldehydes
Alternative energy sources
Analysis
Basidiomycetes
Biodegradation
Biomass
Biomedical and Life Sciences
Biorefineries
Biotechnology
Biotransformation
Carbon
Catalysis
catalytic activity
Cellulose
Chemicals
chemistry
Degradation
Ecosystems
Emission standards
enantiomers
Enzymes
enzymology
Flavoproteins
Flavoproteins - chemistry
Flavoproteins - genetics
Flavoproteins - metabolism
flavor
Fungi
Fungi - enzymology
genetics
Genomes
Hydrides
Hydrogen peroxide
isotopes
Life Sciences
Lignin
Lignin - metabolism
Lignocellulose
metabolism
Metabolites
Microbial Genetics and Genomics
Microbiology
Microorganisms
Mini-Review
Models, Biological
Models, Chemical
Models, Molecular
Oxidase
oxidation
peroxidases
Peroxides
Peroxides - metabolism
Phylogeny
Pleurotus
Pleurotus eryngii
Protein Conformation
protons
Recycling
Sequence Homology, Amino Acid
site-directed mutagenesis
Stereoselectivity
Studies
Stereoselectivity
Reaction mechanism
Lignin biodegradation
Fungal enzymes
GMC oxidoreductases
Aryl-alcohol oxidase
Online AccessGet full text

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Abstract Aryl-alcohol oxidase (AAO) is an extracellular flavoprotein providing the H 2 O 2 required by ligninolytic peroxidases for fungal degradation of lignin, the key step for carbon recycling in land ecosystems. O 2 activation by Pleurotus eryngii AAO takes place during the redox-cycling of p- methoxylated benzylic metabolites secreted by the fungus. Only Pleurotus AAO sequences were available for years, but the number strongly increased recently due to sequencing of different basidiomycete genomes, and a comparison of 112 GMC (glucose–methanol–choline oxidase) superfamily sequences including 40 AAOs is presented. As shown by kinetic isotope effects, alcohol oxidation by AAO is produced by hydride transfer to the flavin, and hydroxyl proton transfer to a base. Moreover, site-directed mutagenesis studies showed that His502 activates the alcohol substrate by proton abstraction, and this result was extended to other GMC oxidoreductases where the nature of the base was under discussion. However, in contrast with that proposed for GMC oxidoreductases, the two transfers are not stepwise but concerted. Alcohol docking at the buried AAO active site resulted in only one catalytically relevant position for concerted transfer, with the pro- R α-hydrogen at distance for hydride abstraction. The expected hydride-transfer stereoselectivity was demonstrated, for the first time in a GMC oxidoreductase, by using the (R) and (S) enantiomers of α-deuterated p -methoxybenzyl alcohol. Other largely unexplained aspects of AAO catalysis (such as the unexpected specificity on substituted aldehydes) can also be explained in the light of the recent results. Finally, the biotechnological interest of AAO in flavor production is extended by its potential in production of chiral compounds taking advantage from the above-described stereoselectivity.
AbstractList Aryl-alcohol oxidase (AAO) is an extracellular flavoprotein providing the H2O2 required by ligninolytic peroxidases for fungal degradation of lignin, the key step for carbon recycling in land ecosystems. O2 activation by Pleurotus eryngii AAO takes place during the redox-cycling of p-methoxylated benzylic metabolites secreted by the fungus. Only Pleurotus AAO sequences were available for years, but the number strongly increased recently due to sequencing of different basidiomycete genomes, and a comparison of 112 GMC (glucose-methanol-choline oxidase) superfamily sequences including 40 AAOs is presented. As shown by kinetic isotope effects, alcohol oxidation by AAO is produced by hydride transfer to the flavin, and hydroxyl proton transfer to a base. Moreover, site-directed mutagenesis studies showed that His502 activates the alcohol substrate by proton abstraction, and this result was extended to other GMC oxidoreductases where the nature of the base was under discussion. However, in contrast with that proposed for GMC oxidoreductases, the two transfers are not stepwise but concerted. Alcohol docking at the buried AAO active site resulted in only one catalytically relevant position for concerted transfer, with the pro-R α-hydrogen at distance for hydride abstraction. The expected hydride-transfer stereoselectivity was demonstrated, for the first time in a GMC oxidoreductase, by using the (R) and (S) enantiomers of α-deuterated p-methoxybenzyl alcohol. Other largely unexplained aspects of AAO catalysis (such as the unexpected specificity on substituted aldehydes) can also be explained in the light of the recent results. Finally, the biotechnological interest of AAO in flavor production is extended by its potential in production of chiral compounds taking advantage from the above-described stereoselectivity.[PUBLICATION ABSTRACT]
Aryl-alcohol oxidase (AAO) is an extracellular flavoprotein providing the H₂O₂ required by ligninolytic peroxidases for fungal degradation of lignin, the key step for carbon recycling in land ecosystems. O₂ activation by Pleurotus eryngii AAO takes place during the redox-cycling of p-methoxylated benzylic metabolites secreted by the fungus. Only Pleurotus AAO sequences were available for years, but the number strongly increased recently due to sequencing of different basidiomycete genomes, and a comparison of 112 GMC (glucose–methanol–choline oxidase) superfamily sequences including 40 AAOs is presented. As shown by kinetic isotope effects, alcohol oxidation by AAO is produced by hydride transfer to the flavin, and hydroxyl proton transfer to a base. Moreover, site-directed mutagenesis studies showed that His502 activates the alcohol substrate by proton abstraction, and this result was extended to other GMC oxidoreductases where the nature of the base was under discussion. However, in contrast with that proposed for GMC oxidoreductases, the two transfers are not stepwise but concerted. Alcohol docking at the buried AAO active site resulted in only one catalytically relevant position for concerted transfer, with the pro-R α-hydrogen at distance for hydride abstraction. The expected hydride-transfer stereoselectivity was demonstrated, for the first time in a GMC oxidoreductase, by using the (R) and (S) enantiomers of α-deuterated p-methoxybenzyl alcohol. Other largely unexplained aspects of AAO catalysis (such as the unexpected specificity on substituted aldehydes) can also be explained in the light of the recent results. Finally, the biotechnological interest of AAO in flavor production is extended by its potential in production of chiral compounds taking advantage from the above-described stereoselectivity.
Aryl-alcohol oxidase (AAO) is an extracellular flavoprotein providing the H sub(2)O sub(2) required by ligninolytic peroxidases for fungal degradation of lignin, the key step for carbon recycling in land ecosystems. O sub(2) activation by Pleurotus eryngii AAO takes place during the redox-cycling of p-methoxylated benzylic metabolites secreted by the fungus. Only Pleurotus AAO sequences were available for years, but the number strongly increased recently due to sequencing of different basidiomycete genomes, and a comparison of 112 GMC (glucose-methanol-choline oxidase) superfamily sequences including 40 AAOs is presented. As shown by kinetic isotope effects, alcohol oxidation by AAO is produced by hydride transfer to the flavin, and hydroxyl proton transfer to a base. Moreover, site-directed mutagenesis studies showed that His502 activates the alcohol substrate by proton abstraction, and this result was extended to other GMC oxidoreductases where the nature of the base was under discussion. However, in contrast with that proposed for GMC oxidoreductases, the two transfers are not stepwise but concerted. Alcohol docking at the buried AAO active site resulted in only one catalytically relevant position for concerted transfer, with the pro-R alpha -hydrogen at distance for hydride abstraction. The expected hydride-transfer stereoselectivity was demonstrated, for the first time in a GMC oxidoreductase, by using the (R) and (S) enantiomers of alpha -deuterated p-methoxybenzyl alcohol. Other largely unexplained aspects of AAO catalysis (such as the unexpected specificity on substituted aldehydes) can also be explained in the light of the recent results. Finally, the biotechnological interest of AAO in flavor production is extended by its potential in production of chiral compounds taking advantage from the above-described stereoselectivity.
Aryl-alcohol oxidase (AAO) is an extracellular flavoprotein providing the H(2)O(2) required by ligninolytic peroxidases for fungal degradation of lignin, the key step for carbon recycling in land ecosystems. O(2) activation by Pleurotus eryngii AAO takes place during the redox-cycling of p-methoxylated benzylic metabolites secreted by the fungus. Only Pleurotus AAO sequences were available for years, but the number strongly increased recently due to sequencing of different basidiomycete genomes, and a comparison of 112 GMC (glucose-methanol-choline oxidase) superfamily sequences including 40 AAOs is presented. As shown by kinetic isotope effects, alcohol oxidation by AAO is produced by hydride transfer to the flavin, and hydroxyl proton transfer to a base. Moreover, site-directed mutagenesis studies showed that His502 activates the alcohol substrate by proton abstraction, and this result was extended to other GMC oxidoreductases where the nature of the base was under discussion. However, in contrast with that proposed for GMC oxidoreductases, the two transfers are not stepwise but concerted. Alcohol docking at the buried AAO active site resulted in only one catalytically relevant position for concerted transfer, with the pro-R α-hydrogen at distance for hydride abstraction. The expected hydride-transfer stereoselectivity was demonstrated, for the first time in a GMC oxidoreductase, by using the (R) and (S) enantiomers of α-deuterated p-methoxybenzyl alcohol. Other largely unexplained aspects of AAO catalysis (such as the unexpected specificity on substituted aldehydes) can also be explained in the light of the recent results. Finally, the biotechnological interest of AAO in flavor production is extended by its potential in production of chiral compounds taking advantage from the above-described stereoselectivity.
Aryl-alcohol oxidase (AAO) is an extracellular flavoprotein providing the H(2)O(2) required by ligninolytic peroxidases for fungal degradation of lignin, the key step for carbon recycling in land ecosystems. O(2) activation by Pleurotus eryngii AAO takes place during the redox-cycling of p-methoxylated benzylic metabolites secreted by the fungus. Only Pleurotus AAO sequences were available for years, but the number strongly increased recently due to sequencing of different basidiomycete genomes, and a comparison of 112 GMC (glucose-methanol-choline oxidase) superfamily sequences including 40 AAOs is presented. As shown by kinetic isotope effects, alcohol oxidation by AAO is produced by hydride transfer to the flavin, and hydroxyl proton transfer to a base. Moreover, site-directed mutagenesis studies showed that His502 activates the alcohol substrate by proton abstraction, and this result was extended to other GMC oxidoreductases where the nature of the base was under discussion. However, in contrast with that proposed for GMC oxidoreductases, the two transfers are not stepwise but concerted. Alcohol docking at the buried AAO active site resulted in only one catalytically relevant position for concerted transfer, with the pro-R α-hydrogen at distance for hydride abstraction. The expected hydride-transfer stereoselectivity was demonstrated, for the first time in a GMC oxidoreductase, by using the (R) and (S) enantiomers of α-deuterated p-methoxybenzyl alcohol. Other largely unexplained aspects of AAO catalysis (such as the unexpected specificity on substituted aldehydes) can also be explained in the light of the recent results. Finally, the biotechnological interest of AAO in flavor production is extended by its potential in production of chiral compounds taking advantage from the above-described stereoselectivity.Aryl-alcohol oxidase (AAO) is an extracellular flavoprotein providing the H(2)O(2) required by ligninolytic peroxidases for fungal degradation of lignin, the key step for carbon recycling in land ecosystems. O(2) activation by Pleurotus eryngii AAO takes place during the redox-cycling of p-methoxylated benzylic metabolites secreted by the fungus. Only Pleurotus AAO sequences were available for years, but the number strongly increased recently due to sequencing of different basidiomycete genomes, and a comparison of 112 GMC (glucose-methanol-choline oxidase) superfamily sequences including 40 AAOs is presented. As shown by kinetic isotope effects, alcohol oxidation by AAO is produced by hydride transfer to the flavin, and hydroxyl proton transfer to a base. Moreover, site-directed mutagenesis studies showed that His502 activates the alcohol substrate by proton abstraction, and this result was extended to other GMC oxidoreductases where the nature of the base was under discussion. However, in contrast with that proposed for GMC oxidoreductases, the two transfers are not stepwise but concerted. Alcohol docking at the buried AAO active site resulted in only one catalytically relevant position for concerted transfer, with the pro-R α-hydrogen at distance for hydride abstraction. The expected hydride-transfer stereoselectivity was demonstrated, for the first time in a GMC oxidoreductase, by using the (R) and (S) enantiomers of α-deuterated p-methoxybenzyl alcohol. Other largely unexplained aspects of AAO catalysis (such as the unexpected specificity on substituted aldehydes) can also be explained in the light of the recent results. Finally, the biotechnological interest of AAO in flavor production is extended by its potential in production of chiral compounds taking advantage from the above-described stereoselectivity.
Aryl-alcohol oxidase (AAO) is an extracellular flavoprotein providing the H 2 O 2 required by ligninolytic peroxidases for fungal degradation of lignin, the key step for carbon recycling in land ecosystems. O 2 activation by Pleurotus eryngii AAO takes place during the redox-cycling of p- methoxylated benzylic metabolites secreted by the fungus. Only Pleurotus AAO sequences were available for years, but the number strongly increased recently due to sequencing of different basidiomycete genomes, and a comparison of 112 GMC (glucose–methanol–choline oxidase) superfamily sequences including 40 AAOs is presented. As shown by kinetic isotope effects, alcohol oxidation by AAO is produced by hydride transfer to the flavin, and hydroxyl proton transfer to a base. Moreover, site-directed mutagenesis studies showed that His502 activates the alcohol substrate by proton abstraction, and this result was extended to other GMC oxidoreductases where the nature of the base was under discussion. However, in contrast with that proposed for GMC oxidoreductases, the two transfers are not stepwise but concerted. Alcohol docking at the buried AAO active site resulted in only one catalytically relevant position for concerted transfer, with the pro- R α-hydrogen at distance for hydride abstraction. The expected hydride-transfer stereoselectivity was demonstrated, for the first time in a GMC oxidoreductase, by using the (R) and (S) enantiomers of α-deuterated p -methoxybenzyl alcohol. Other largely unexplained aspects of AAO catalysis (such as the unexpected specificity on substituted aldehydes) can also be explained in the light of the recent results. Finally, the biotechnological interest of AAO in flavor production is extended by its potential in production of chiral compounds taking advantage from the above-described stereoselectivity.
Author Hernández-Ortega, Aitor
Ferreira, Patricia
Martínez, Angel T.
Author_xml – sequence: 1
  givenname: Aitor
  surname: Hernández-Ortega
  fullname: Hernández-Ortega, Aitor
  organization: Centro de Investigaciones Biológicas, Consejo Superior de Investigaciones Científicas (CSIC)
– sequence: 2
  givenname: Patricia
  surname: Ferreira
  fullname: Ferreira, Patricia
  organization: Departamento de Bioquímica y Biología Molecular y Celular and Instituto de Biocomputación y Fisica de los Sistemas Complejos, Universidad de Zaragoza
– sequence: 3
  givenname: Angel T.
  surname: Martínez
  fullname: Martínez, Angel T.
  email: ATMartinez@cib.csic.es
  organization: Centro de Investigaciones Biológicas, Consejo Superior de Investigaciones Científicas (CSIC)
BackLink https://www.ncbi.nlm.nih.gov/pubmed/22249717$$D View this record in MEDLINE/PubMed
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ID FETCH-LOGICAL-p308t-b0cad2745b1bed042c68a5d359e20c64ebe092fa55a0664eda65a01e6754c6cd3
IEDL.DBID U2A
ISSN 0175-7598
1432-0614
IngestDate Thu Jul 10 21:15:17 EDT 2025
Fri Jul 11 10:22:23 EDT 2025
Fri Jul 11 05:37:27 EDT 2025
Fri Jul 11 01:12:59 EDT 2025
Wed Aug 13 09:38:46 EDT 2025
Mon Jul 21 06:03:34 EDT 2025
Fri Feb 21 02:37:13 EST 2025
IsPeerReviewed true
IsScholarly true
Issue 4
Keywords Stereoselectivity
Reaction mechanism
Lignin biodegradation
Fungal enzymes
GMC oxidoreductases
Aryl-alcohol oxidase
Language English
LinkModel DirectLink
MergedId FETCHMERGED-LOGICAL-p308t-b0cad2745b1bed042c68a5d359e20c64ebe092fa55a0664eda65a01e6754c6cd3
Notes ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 14
content type line 23
ObjectType-Review-3
PMID 22249717
PQID 920372725
PQPubID 54065
PageCount 16
ParticipantIDs proquest_miscellaneous_954640424
proquest_miscellaneous_921721710
proquest_miscellaneous_1753522373
proquest_miscellaneous_1449948955
proquest_journals_920372725
pubmed_primary_22249717
springer_journals_10_1007_s00253_011_3836_8
PublicationCentury 2000
PublicationDate 20120200
2012-Feb
20120201
PublicationDateYYYYMMDD 2012-02-01
PublicationDate_xml – month: 2
  year: 2012
  text: 20120200
PublicationDecade 2010
PublicationPlace Berlin/Heidelberg
PublicationPlace_xml – name: Berlin/Heidelberg
– name: Germany
– name: Heidelberg
PublicationTitle Applied microbiology and biotechnology
PublicationTitleAbbrev Appl Microbiol Biotechnol
PublicationTitleAlternate Appl Microbiol Biotechnol
PublicationYear 2012
Publisher Springer-Verlag
Springer Nature B.V
Publisher_xml – name: Springer-Verlag
– name: Springer Nature B.V
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Snippet Aryl-alcohol oxidase (AAO) is an extracellular flavoprotein providing the H 2 O 2 required by ligninolytic peroxidases for fungal degradation of lignin, the...
Aryl-alcohol oxidase (AAO) is an extracellular flavoprotein providing the H(2)O(2) required by ligninolytic peroxidases for fungal degradation of lignin, the...
Aryl-alcohol oxidase (AAO) is an extracellular flavoprotein providing the H2O2 required by ligninolytic peroxidases for fungal degradation of lignin, the key...
Aryl-alcohol oxidase (AAO) is an extracellular flavoprotein providing the H₂O₂ required by ligninolytic peroxidases for fungal degradation of lignin, the key...
Aryl-alcohol oxidase (AAO) is an extracellular flavoprotein providing the H sub(2)O sub(2) required by ligninolytic peroxidases for fungal degradation of...
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StartPage 1395
SubjectTerms active sites
Alcohol
Alcohol Oxidoreductases
Alcohol Oxidoreductases - chemistry
Alcohol Oxidoreductases - genetics
Alcohol Oxidoreductases - metabolism
Alcohols
Aldehydes
Alternative energy sources
Analysis
Basidiomycetes
Biodegradation
Biomass
Biomedical and Life Sciences
Biorefineries
Biotechnology
Biotransformation
Carbon
Catalysis
catalytic activity
Cellulose
Chemicals
chemistry
Degradation
Ecosystems
Emission standards
enantiomers
Enzymes
enzymology
Flavoproteins
Flavoproteins - chemistry
Flavoproteins - genetics
Flavoproteins - metabolism
flavor
Fungi
Fungi - enzymology
genetics
Genomes
Hydrides
Hydrogen peroxide
isotopes
Life Sciences
Lignin
Lignin - metabolism
Lignocellulose
metabolism
Metabolites
Microbial Genetics and Genomics
Microbiology
Microorganisms
Mini-Review
Models, Biological
Models, Chemical
Models, Molecular
Oxidase
oxidation
peroxidases
Peroxides
Peroxides - metabolism
Phylogeny
Pleurotus
Pleurotus eryngii
Protein Conformation
protons
Recycling
Sequence Homology, Amino Acid
site-directed mutagenesis
Stereoselectivity
Studies
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Title Fungal aryl-alcohol oxidase: a peroxide-producing flavoenzyme involved in lignin degradation
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