Molecular and Mechanistic Properties of the Membrane-Bound Mitochondrial Monoamine Oxidases+
Identifieur interne : 000182 ( Pmc/Checkpoint ); précédent : 000181; suivant : 000183Molecular and Mechanistic Properties of the Membrane-Bound Mitochondrial Monoamine Oxidases+
Auteurs : Dale Edmondson [États-Unis] ; Claudia Binda [Italie] ; Jin Wang [États-Unis] ; Anup Upadhyay [États-Unis] ; Andrea Mattevi [Italie]Source :
- Biochemistry [ 0006-2960 ] ; 2009.
Abstract
The last decade has brought major advances in our knowledge of the structures and mechanisms of MAO A and MAO B, which are pharmacological targets for specific inhibitors. In both enzymes, crystallographic and biochemical data show their respective C-terminal transmembrane helices anchor the enzymes to the outer mitochondrial membrane. Pulsed EPR data show both enzymes are dimeric in their membrane-bound forms with agreement between distances measured in their crystalline forms. Distances measure between active-site directed spin labels in membrane preparations show excellent agreement with those estimated from crystallographic data. Our knowledge of requirements for development of specific reversible MAO B inhibitors is in a fairly mature status. Less is known regarding the structural requirements for highly specific reversible MAO A inhibitors. In spite of their 70% sequence identity and similarities of Cα-folds, the two enzymes exhibit significant functional and structural differences that can be exploited in the ultimate goal of the development of highly specific inhibitors. This review summarizes the current structural and mechanistic information available that can be utilized in the development of future highly specific neuroprotectants and cardioprotectants.
Url:
DOI: 10.1021/bi900413g
PubMed: 19371079
PubMed Central: 2710584
Affiliations:
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<front><div type="abstract" xml:lang="en"><p id="P1">The last decade has brought major advances in our knowledge of the structures and mechanisms of MAO A and MAO B, which are pharmacological targets for specific inhibitors. In both enzymes, crystallographic and biochemical data show their respective C-terminal transmembrane helices anchor the enzymes to the outer mitochondrial membrane. Pulsed EPR data show both enzymes are dimeric in their membrane-bound forms with agreement between distances measured in their crystalline forms. Distances measure between active-site directed spin labels in membrane preparations show excellent agreement with those estimated from crystallographic data. Our knowledge of requirements for development of specific reversible MAO B inhibitors is in a fairly mature status. Less is known regarding the structural requirements for highly specific reversible MAO A inhibitors. In spite of their 70% sequence identity and similarities of Cα-folds, the two enzymes exhibit significant functional and structural differences that can be exploited in the ultimate goal of the development of highly specific inhibitors. This review summarizes the current structural and mechanistic information available that can be utilized in the development of future highly specific neuroprotectants and cardioprotectants.</p>
</div>
</front>
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<pmc article-type="research-article" xml:lang="EN"><pmc-comment>The publisher of this article does not allow downloading of the full text in XML form.</pmc-comment>
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<front><journal-meta><journal-id journal-id-type="nlm-journal-id">0370623</journal-id>
<journal-id journal-id-type="pubmed-jr-id">1028</journal-id>
<journal-id journal-id-type="nlm-ta">Biochemistry</journal-id>
<journal-title>Biochemistry</journal-title>
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<issn pub-type="epub">1520-4995</issn>
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<title-group><article-title>Molecular and Mechanistic Properties of the Membrane-Bound Mitochondrial Monoamine Oxidases<xref ref-type="fn" rid="FN1">+</xref>
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<contrib-group><contrib contrib-type="author"><name><surname>Edmondson</surname>
<given-names>Dale E.</given-names>
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<xref ref-type="aff" rid="A1">‡</xref>
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<contrib contrib-type="author"><name><surname>Binda</surname>
<given-names>Claudia</given-names>
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<xref ref-type="aff" rid="A2">§</xref>
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<contrib contrib-type="author"><name><surname>Wang</surname>
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<xref ref-type="aff" rid="A1">‡</xref>
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<contrib contrib-type="author"><name><surname>Upadhyay</surname>
<given-names>Anup K.</given-names>
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<xref ref-type="aff" rid="A1">‡</xref>
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<contrib contrib-type="author"><name><surname>Mattevi</surname>
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<xref ref-type="aff" rid="A2">§</xref>
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<aff id="A1"><label>‡</label>
Departments of Biochemistry and Chemistry, Emory University, Atlanta, Georgia 30322</aff>
<aff id="A2"><label>§</label>
Department of Genetics and Microbiology, University of Pavia, via Ferrata 1, Pavia, 27100 Italy</aff>
<author-notes><corresp id="cor1">Correspondence should be addressed to: Dr. Dale E. Edmondson, Department of Biochemistry, Emory University, 1510 Clifton Rd., Atlanta, GA 30322, Phone: 404-727-5972, Fax: 404-727-2738. Email: <email>deedmon@emory.edu</email>
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<pub-date pub-type="nihms-submitted"><day>24</day>
<month>4</month>
<year>2009</year>
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<pub-date pub-type="ppub"><day>26</day>
<month>5</month>
<year>2009</year>
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<pub-date pub-type="pmc-release"><day>26</day>
<month>5</month>
<year>2010</year>
</pub-date>
<volume>48</volume>
<issue>20</issue>
<fpage>4220</fpage>
<lpage>4230</lpage>
<abstract><p id="P1">The last decade has brought major advances in our knowledge of the structures and mechanisms of MAO A and MAO B, which are pharmacological targets for specific inhibitors. In both enzymes, crystallographic and biochemical data show their respective C-terminal transmembrane helices anchor the enzymes to the outer mitochondrial membrane. Pulsed EPR data show both enzymes are dimeric in their membrane-bound forms with agreement between distances measured in their crystalline forms. Distances measure between active-site directed spin labels in membrane preparations show excellent agreement with those estimated from crystallographic data. Our knowledge of requirements for development of specific reversible MAO B inhibitors is in a fairly mature status. Less is known regarding the structural requirements for highly specific reversible MAO A inhibitors. In spite of their 70% sequence identity and similarities of Cα-folds, the two enzymes exhibit significant functional and structural differences that can be exploited in the ultimate goal of the development of highly specific inhibitors. This review summarizes the current structural and mechanistic information available that can be utilized in the development of future highly specific neuroprotectants and cardioprotectants.</p>
</abstract>
<contract-num rid="GM1">R01 GM029433-26</contract-num>
<contract-sponsor id="GM1">National Institute of General Medical Sciences : NIGMS</contract-sponsor>
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