Evolution, expression, and substrate specificities of aldehyde oxidase enzymes in eukaryotes.
Identifieur interne : 000135 ( Main/Exploration ); précédent : 000134; suivant : 000136Evolution, expression, and substrate specificities of aldehyde oxidase enzymes in eukaryotes.
Auteurs : Mineko Terao [Italie] ; Enrico Garattini [Italie] ; Maria João Romão [Portugal] ; Silke Leimkühler [Allemagne]Source :
- The Journal of biological chemistry [ 1083-351X ] ; 2020.
Abstract
Aldehyde oxidases (AOXs) are a small group of enzymes belonging to the larger family of molybdo-flavoenzymes, along with the well-characterized xanthine oxidoreductase. The two major types of reactions that are catalyzed by AOXs are the hydroxylation of heterocycles and the oxidation of aldehydes to their corresponding carboxylic acids. Different animal species have different complements of AOX genes. The two extremes are represented in humans and rodents; whereas the human genome contains a single active gene (AOX1), those of rodents, such as mice, are endowed with four genes (Aox1-4), clustering on the same chromosome, each encoding a functionally distinct AOX enzyme. It still remains enigmatic why some species have numerous AOX enzymes, whereas others harbor only one functional enzyme. At present, little is known about the physiological relevance of AOX enzymes in humans and their additional forms in other mammals. These enzymes are expressed in the liver and play an important role in the metabolisms of drugs and other xenobiotics. In this review, we discuss the expression, tissue-specific roles, and substrate specificities of the different mammalian AOX enzymes and highlight insights into their physiological roles.
DOI: 10.1074/jbc.REV119.007741
PubMed: 32144208
PubMed Central: PMC7170512
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of Biochemistry and Biology, University of Potsdam, Karl-Liebknecht-Str. 24-25, 14476 Potsdam</wicri:regionArea><placeName><region type="land" nuts="2">Brandebourg</region><settlement type="city">Potsdam</settlement></placeName><orgName type="university">Université de Potsdam</orgName></affiliation></author></analytic><series><title level="j">The Journal of biological chemistry</title><idno type="eISSN">1083-351X</idno><imprint><date when="2020" type="published">2020</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Aldehyde oxidases (AOXs) are a small group of enzymes belonging to the larger family of molybdo-flavoenzymes, along with the well-characterized xanthine oxidoreductase. The two major types of reactions that are catalyzed by AOXs are the hydroxylation of heterocycles and the oxidation of aldehydes to their corresponding carboxylic acids. Different animal species have different complements of <i>AOX</i> genes. The two extremes are represented in humans and rodents; whereas the human genome contains a single active gene (<i>AOX1</i>), those of rodents, such as mice, are endowed with four genes (<i>Aox1-4</i>), clustering on the same chromosome, each encoding a functionally distinct AOX enzyme. It still remains enigmatic why some species have numerous AOX enzymes, whereas others harbor only one functional enzyme. At present, little is known about the physiological relevance of AOX enzymes in humans and their additional forms in other mammals. These enzymes are expressed in the liver and play an important role in the metabolisms of drugs and other xenobiotics. In this review, we discuss the expression, tissue-specific roles, and substrate specificities of the different mammalian AOX enzymes and highlight insights into their physiological roles.</div></front></TEI><pubmed><MedlineCitation Status="In-Data-Review" Owner="NLM"><PMID Version="1">32144208</PMID><DateRevised><Year>2020</Year><Month>04</Month><Day>24</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1083-351X</ISSN><JournalIssue CitedMedium="Internet"><Volume>295</Volume><Issue>16</Issue><PubDate><Year>2020</Year><Month>Apr</Month><Day>17</Day></PubDate></JournalIssue><Title>The Journal of biological chemistry</Title><ISOAbbreviation>J Biol Chem</ISOAbbreviation></Journal><ArticleTitle>Evolution, expression, and substrate specificities of aldehyde oxidase enzymes in eukaryotes.</ArticleTitle><Pagination><MedlinePgn>5377-5389</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1074/jbc.REV119.007741</ELocationID><Abstract><AbstractText>Aldehyde oxidases (AOXs) are a small group of enzymes belonging to the larger family of molybdo-flavoenzymes, along with the well-characterized xanthine oxidoreductase. The two major types of reactions that are catalyzed by AOXs are the hydroxylation of heterocycles and the oxidation of aldehydes to their corresponding carboxylic acids. Different animal species have different complements of <i>AOX</i> genes. The two extremes are represented in humans and rodents; whereas the human genome contains a single active gene (<i>AOX1</i>), those of rodents, such as mice, are endowed with four genes (<i>Aox1-4</i>), clustering on the same chromosome, each encoding a functionally distinct AOX enzyme. It still remains enigmatic why some species have numerous AOX enzymes, whereas others harbor only one functional enzyme. At present, little is known about the physiological relevance of AOX enzymes in humans and their additional forms in other mammals. These enzymes are expressed in the liver and play an important role in the metabolisms of drugs and other xenobiotics. In this review, we discuss the expression, tissue-specific roles, and substrate specificities of the different mammalian AOX enzymes and highlight insights into their physiological roles.</AbstractText><CopyrightInformation>© 2020 Terao et al.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Terao</LastName><ForeName>Mineko</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Laboratory of Molecular Biology, Istituto di Ricerche Farmacologiche Mario Negri IRCCS, via La Masa 19, 20156 Milano, Italy.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Garattini</LastName><ForeName>Enrico</ForeName><Initials>E</Initials><AffiliationInfo><Affiliation>Laboratory of Molecular Biology, Istituto di Ricerche Farmacologiche Mario Negri IRCCS, via La Masa 19, 20156 Milano, Italy.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Romão</LastName><ForeName>Maria João</ForeName><Initials>MJ</Initials><AffiliationInfo><Affiliation>UCIBIO-Applied Biomolecular Sciences Unit, Departamento de Química, Faculdade de Ciências e Tecnologia, Universidade NOVA de Lisboa, 2829-516 Caparica, Portugal.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Leimkühler</LastName><ForeName>Silke</ForeName><Initials>S</Initials><Identifier Source="ORCID">https://orcid.org/0000-0003-3238-2122</Identifier><AffiliationInfo><Affiliation>Department of Molecular Enzymology, Institute of Biochemistry and Biology, University of Potsdam, Karl-Liebknecht-Str. 24-25, 14476 Potsdam, Germany sleim@uni-potsdam.de.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><DataBankList 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last="Terao">Mineko Terao</name></noRegion><name sortKey="Garattini, Enrico" sort="Garattini, Enrico" uniqKey="Garattini E" first="Enrico" last="Garattini">Enrico Garattini</name></country><country name="Portugal"><noRegion><name sortKey="Romao, Maria Joao" sort="Romao, Maria Joao" uniqKey="Romao M" first="Maria João" last="Romão">Maria João Romão</name></noRegion></country><country name="Allemagne"><region name="Brandebourg"><name sortKey="Leimkuhler, Silke" sort="Leimkuhler, Silke" uniqKey="Leimkuhler S" first="Silke" last="Leimkühler">Silke Leimkühler</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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