D E Edmondson

Summary

Affiliation: Emory University
Country: USA

Publications

  1. ncbi request reprint The FAD binding sites of human monoamine oxidases A and B
    Dale E Edmondson
    Department of Biochemistry and Chemistry, Rollins Research Center, Emory University School of Medicine, 1510 Clifton Road, Atlanta, GA 30322 3050, USA
    Neurotoxicology 25:63-72. 2004
  2. ncbi request reprint Structure and mechanism of monoamine oxidase
    D E Edmondson
    Department of Biochemistry and Chemistry, Emory University, Atlanta, Georgia 30322, USA
    Curr Med Chem 11:1983-93. 2004
  3. ncbi request reprint The covalent FAD of monoamine oxidase: structural and functional role and mechanism of the flavinylation reaction
    D E Edmondson
    Department of Biochemistry, Emory University School of Medicine, Atlanta, GA 30322, USA
    Antioxid Redox Signal 3:789-806. 2001
  4. ncbi request reprint Evidence for alternative binding modes in the interaction of benzylamine analogues with bovine liver monoamine oxidase B
    D E Edmondson
    Departments of Biochemistry and Chemistry, Emory University, Atlanta, GA 30322, USA
    Biochim Biophys Acta 1479:52-8. 2000
  5. ncbi request reprint Do monomeric vs dimeric forms of MAO-A make a difference? A direct comparison of the catalytic properties of rat and human MAO-A's
    J Wang
    Department of Biochemistry and Chemistry, Emory University, Atlanta, GA 30322, USA
    J Neural Transm 114:721-4. 2007
  6. ncbi request reprint Loss of serotonin oxidation as a component of the altered substrate specificity in the Y444F mutant of recombinant human liver MAO A
    R K Nandigama
    Department of Biochemistry, Emory University, Atlanta, Georgia 30322-3050, USA
    Biochemistry 40:14839-46. 2001
  7. ncbi request reprint New insights into the structures and functions of human monoamine oxidases A and B
    D E Edmondson
    Department of Biochemistry and Chemistry, Emory University, Atlanta, GA 30322, USA
    J Neural Transm 114:703-5. 2007
  8. ncbi request reprint High-level expression of human liver monoamine oxidase B in Pichia pastoris
    P Newton-Vinson
    Departments of Biochemistry and Chemistry, Emory University, Atlanta, Georgia 30322, USA
    Protein Expr Purif 20:334-45. 2000
  9. pmc Do MAO A and MAO B utilize the same mechanism for the C-H bond cleavage step in catalysis? Evidence suggesting differing mechanisms
    R Orru
    Department of Biochemistry, Emory University Rollins Research Center, 1510 Clifton Road, Atlanta, GA 30322, USA
    J Neural Transm 120:847-51. 2013
  10. ncbi request reprint Kinetic properties of recombinant MAO-A on incorporation into phospholipid nanodisks
    F Cruz
    Department of Biochemistry, School of Medicine, Emory University, Atlanta, GA 30322, USA
    J Neural Transm 114:699-702. 2007

Collaborators

Detail Information

Publications37

  1. ncbi request reprint The FAD binding sites of human monoamine oxidases A and B
    Dale E Edmondson
    Department of Biochemistry and Chemistry, Rollins Research Center, Emory University School of Medicine, 1510 Clifton Road, Atlanta, GA 30322 3050, USA
    Neurotoxicology 25:63-72. 2004
    ..This structural information is then used to explain previous studies on flavin analog incorporation into either MAO B or into MAO A...
  2. ncbi request reprint Structure and mechanism of monoamine oxidase
    D E Edmondson
    Department of Biochemistry and Chemistry, Emory University, Atlanta, Georgia 30322, USA
    Curr Med Chem 11:1983-93. 2004
    ..The existing structural data on MAO B support previous QSAR results and are also supportive of a proposed polar nucleophilic mechanism for MAO A and B catalysis rather than the alternatively proposed single electron transfer mechanism...
  3. ncbi request reprint The covalent FAD of monoamine oxidase: structural and functional role and mechanism of the flavinylation reaction
    D E Edmondson
    Department of Biochemistry, Emory University School of Medicine, Atlanta, GA 30322, USA
    Antioxid Redox Signal 3:789-806. 2001
    ....
  4. ncbi request reprint Evidence for alternative binding modes in the interaction of benzylamine analogues with bovine liver monoamine oxidase B
    D E Edmondson
    Departments of Biochemistry and Chemistry, Emory University, Atlanta, GA 30322, USA
    Biochim Biophys Acta 1479:52-8. 2000
    ....
  5. ncbi request reprint Do monomeric vs dimeric forms of MAO-A make a difference? A direct comparison of the catalytic properties of rat and human MAO-A's
    J Wang
    Department of Biochemistry and Chemistry, Emory University, Atlanta, GA 30322, USA
    J Neural Transm 114:721-4. 2007
    ....
  6. ncbi request reprint Loss of serotonin oxidation as a component of the altered substrate specificity in the Y444F mutant of recombinant human liver MAO A
    R K Nandigama
    Department of Biochemistry, Emory University, Atlanta, Georgia 30322-3050, USA
    Biochemistry 40:14839-46. 2001
    ..The mechanism of C-H abstraction is therefore unaltered. The suggestion that polyamine oxidase and monoamine oxidase may have structural homology appears to be valid as regards Y444 in MAO A and Y439 in plant polyamine oxidase...
  7. ncbi request reprint New insights into the structures and functions of human monoamine oxidases A and B
    D E Edmondson
    Department of Biochemistry and Chemistry, Emory University, Atlanta, GA 30322, USA
    J Neural Transm 114:703-5. 2007
    ..Differences observed between human and rat MAO-A's raise questions regarding the appropriateness of the rat model in the development of MAO-A specific inhibitors as drugs for eventual human use...
  8. ncbi request reprint High-level expression of human liver monoamine oxidase B in Pichia pastoris
    P Newton-Vinson
    Departments of Biochemistry and Chemistry, Emory University, Atlanta, Georgia 30322, USA
    Protein Expr Purif 20:334-45. 2000
    ..These data demonstrate the successful heterologous expression of a functional, membrane-bound MAO B, which will permit a number of mutagenesis studies as structural and mechanistic probes not previously possible...
  9. pmc Do MAO A and MAO B utilize the same mechanism for the C-H bond cleavage step in catalysis? Evidence suggesting differing mechanisms
    R Orru
    Department of Biochemistry, Emory University Rollins Research Center, 1510 Clifton Road, Atlanta, GA 30322, USA
    J Neural Transm 120:847-51. 2013
    ..These results lead to the conclusion that the assumption that MAO A and MAO B follow identical mechanisms is incorrect...
  10. ncbi request reprint Kinetic properties of recombinant MAO-A on incorporation into phospholipid nanodisks
    F Cruz
    Department of Biochemistry, School of Medicine, Emory University, Atlanta, GA 30322, USA
    J Neural Transm 114:699-702. 2007
    ..Taken together, these data suggest that the membrane environment affects MAO-A catalytic properties for both substrates and reversible inhibitors...
  11. ncbi request reprint Oxidation-reduction potential studies on p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens
    G Williamson
    Department of Biochemistry, Emory University School of Medicine, Atlanta, GA 30322
    Biochim Biophys Acta 953:258-62. 1988
    ....
  12. pmc Insights into the mode of inhibition of human mitochondrial monoamine oxidase B from high-resolution crystal structures
    Claudia Binda
    Department of Genetics and Microbiology, University of Pavia, Via Abbiategrasso, 27100 Pavia, Italy
    Proc Natl Acad Sci U S A 100:9750-5. 2003
    ..Small conformational changes are observed on comparison of the different inhibitor-enzyme complexes. Future MAO-B drug design will need to consider "induced fit" contributions as an element in ligand-enzyme interactions...
  13. doi request reprint Structural and mechanistic studies of arylalkylhydrazine inhibition of human monoamine oxidases A and B
    Claudia Binda
    Department of Genetics and Microbiology, University of Pavia, Via Ferrata 1, Pavia 27100, Italy
    Biochemistry 47:5616-25. 2008
    ..The bound arylalkyl radical reacts with the N(5) of the flavin, while the dissociated diazene reacts nonspecifically with the enzyme through arylalkylradicals...
  14. ncbi request reprint Comparison of the structural properties of the active site cavities of human and rat monoamine oxidase A and B in their soluble and membrane-bound forms
    Anup K Upadhyay
    Department of Biochemistry, Emory University, Atlanta, Georgia 30322, USA
    Biochemistry 47:526-36. 2008
    ....
  15. pmc Structural insights into the mechanism of amine oxidation by monoamine oxidases A and B
    Dale E Edmondson
    Departments of Biochemistry and Chemistry, Emory University, 1510 Clifton Road, Atlanta, GA 30322, USA
    Arch Biochem Biophys 464:269-76. 2007
    ..These conclusions support the proposal that a polar nucleophilic mechanism for amine oxidation is the most consistent mechanistic scheme as compared with the single electron transfer mechanism...
  16. ncbi request reprint Plasmalogen assembly: a key flavoenzyme
    Dale E Edmondson
    Structure 15:639-41. 2007
    ..2007) in this issue of Structure provide new insights into how this peroxisomal flavoenzyme catalyzes a nonredox reaction in the conversion of an ester to an ether linkage in plasmologen biosynthesis...
  17. ncbi request reprint Structure of human monoamine oxidase B, a drug target for the treatment of neurological disorders
    Claudia Binda
    Department of Genetics and Microbiology, University of Pavia, Pavia, Italy
    Nat Struct Biol 9:22-6. 2002
    ..The structure provides a framework for probing the catalytic mechanism, understanding the differences between the B- and A-monoamine oxidase isoforms and designing specific inhibitors...
  18. ncbi request reprint Functional role of the "aromatic cage" in human monoamine oxidase B: structures and catalytic properties of Tyr435 mutant proteins
    Min Li
    Department of Biochemistry, Emory University, 1510 Clifton Road, Atlanta, Georgia 30322, USA
    Biochemistry 45:4775-84. 2006
    ..These results are consistent with a proposed polar nucleophilic mechanism for catalytic amine oxidation...
  19. pmc Three-dimensional structure of human monoamine oxidase A (MAO A): relation to the structures of rat MAO A and human MAO B
    Luigi De Colibus
    Department of Genetics and Microbiology, University of Pavia, via Abbiategrasso 207, 27100 Pavia, Italy
    Proc Natl Acad Sci U S A 102:12684-9. 2005
    ..M., Soldevila, M., Navarro, A., Kidd, K. K., Oliva, B. & Bertranpetit, J. (2004) Hum. Genet. 115, 377-386]. These considerations put into question the use of MAO A from nonhuman sources in drug development for use in humans...
  20. ncbi request reprint Structure-function relationships in flavoenzyme-dependent amine oxidations: a comparison of polyamine oxidase and monoamine oxidase
    Claudia Binda
    Department of Genetics and Microbiology, University of Pavia, 27100 Pavia, Italy
    J Biol Chem 277:23973-6. 2002
  21. ncbi request reprint Polystyrene microbridges used in sitting-drop crystallization release 1,4-diphenyl-2-butene, a novel inhibitor of human MAO B
    Frantisek Hubalek
    Department of Biochemistry, Emory University, Atlanta, Georgia, USA
    Acta Crystallogr D Biol Crystallogr 59:1874-6. 2003
    ..5 micro mol) per microbridge and functions as a competitive inhibitor of MAO B with a K(i) of 35 micro M. The presence of detergents in the crystallization solutions facilitates the extraction of this compound from the polymer medium...
  22. ncbi request reprint Crystal structures of monoamine oxidase B in complex with four inhibitors of the N-propargylaminoindan class
    Claudia Binda
    Department of Genetics and Microbiology, University of Pavia, via Abbiategrasso 207, Pavia, 27100 Italy
    J Med Chem 47:1767-74. 2004
    ..These structural studies may guide future drug design to improve selectivity and efficacy by introducing appropriate substituents on the rasagiline molecular scaffold...
  23. ncbi request reprint Ability of tetrahydrobiopterin analogues to support catalysis by inducible nitric oxide synthase: formation of a pterin radical is required for enzyme activity
    Amy R Hurshman
    Department of Medicinal Chemistry, University of Michigan, Ann Arbor, Michigan 48109 0606, USA
    Biochemistry 42:13287-303. 2003
    ..Although binding of H(4)B also stabilizes the NOS structure and active site, the most critical role of the pterin cofactor in NOS appears to be in electron transfer...
  24. ncbi request reprint Structural comparison of human monoamine oxidases A and B: mass spectrometry monitoring of cysteine reactivities
    Frantisek Hubalek
    Department of Biochemistry and the Microchemical and Proteomics Facility, Emory University School of Medicine, Atlanta, Georgia 30322, USA
    J Biol Chem 278:28612-8. 2003
    ..No evidence is found for the presence of disulfide bonds in either enzyme, contrary to a previous suggestion...
  25. ncbi request reprint Oxygen isotope effects on electron transfer to O2 probed using chemically modified flavins bound to glucose oxidase
    Justine P Roth
    Department of Chemistry, University of California, Berkeley, California 94720, USA
    J Am Chem Soc 126:15120-31. 2004
    ....
  26. pmc Characterization of detergent purified recombinant rat liver monoamine oxidase B expressed in Pichia pastoris
    Anup K Upadhyay
    Department of Biochemistry, Emory University School of Medicine, 1510 Clifton Road NE, Atlanta, GA 30322, USA
    Protein Expr Purif 59:349-56. 2008
    ..Kinetic parameters obtained for purified rMAOB are compared with those reported earlier for recombinant human liver MAOB expressed in P. pastoris...
  27. doi request reprint Determination of the oligomeric states of human and rat monoamine oxidases in the outer mitochondrial membrane and octyl beta-D-glucopyranoside micelles using pulsed dipolar electron spin resonance spectroscopy
    Anup K Upadhyay
    Department of Biochemistry, Emory University, 1510 Clifton Road, Atlanta, Georgia 30322, USA
    Biochemistry 47:1554-66. 2008
    ..The general applicability of the PDS technique to structural studies of membrane proteins in their native membrane environments and detergent purified forms is discussed...
  28. ncbi request reprint Structures of human monoamine oxidase B complexes with selective noncovalent inhibitors: safinamide and coumarin analogs
    Claudia Binda
    Department of Genetics and Microbiology, University of Pavia, Via Ferrata 1, Pavia, 27100 Italy
    J Med Chem 50:5848-52. 2007
    ..1-0.5 microM range that are 30-700-fold lower than those observed with MAO A. The inhibitors bind noncovalently to MAO B, occupying both the entrance and the substrate cavities and showing a similarly oriented benzyloxy substituent...
  29. ncbi request reprint Factors involved in the assembly of a functional molybdopyranopterin center in recombinant Comamonas acidovorans xanthine dehydrogenase
    Nikolai V Ivanov
    Department of Chemistry, Emory University, Atlanta, GA 30322, USA
    Eur J Biochem 270:4744-54. 2003
    ..Therefore, the assembly of a functional Mo-pyranopterin center in XDH requires the presence of a functional xdhC gene product. The purified, recombinant XDH shows spectral and kinetic properties identical to those of the native enzyme...
  30. pmc Human and rat monoamine oxidase-A are differentially inhibited by (S)-4-alkylthioamphetamine derivatives: insights from molecular modeling studies
    Angelica Fierro
    Faculty of Chemistry and Biology, University of Santiago de Chile, Alameda, Santiago, Chile
    Bioorg Med Chem 15:5198-206. 2007
    ..These findings further support the concept that MAO inhibitory activity of novel compounds, determined with enzymes from diverse mammalian species, should be considered with caution if human MAO is the final target to be addressed...
  31. ncbi request reprint Inactivation of purified human recombinant monoamine oxidases A and B by rasagiline and its analogues
    Frantisek Hubalek
    Department of Biochemistry, Emory University, 1510 Clifton Road, Atlanta, Georgia 30322, USA
    J Med Chem 47:1760-6. 2004
    ..et al. J. Med. Chem. 2004, 47, 1767-1774...
  32. ncbi request reprint High-level expression of human liver monoamine oxidase A in Pichia pastoris: comparison with the enzyme expressed in Saccharomyces cerevisiae
    Min Li
    Department of Biochemistry, Emory University, Atlanta, Georgia 30322 3050, USA
    Protein Expr Purif 24:152-62. 2002
    ..pastoris compared with the published S. cerevisiae system in higher expression level (329 mg/L) and in a higher level of homogeneity of the isolated enzyme...
  33. ncbi request reprint Phentermine inhibition of recombinant human liver monoamine oxidases A and B
    Ravi K Nandigama
    Department of Biochemistry, Emory University School of Medicine, Rollins Research Building, 1510 Clifton Road, Atlanta, GA 30322 3050, USA
    Biochem Pharmacol 63:865-9. 2002
    ..These data suggest that phentermine inhibition of human MAO A (or of MAO B) is too weak to be of pharmacological relevance...
  34. pmc Binding of rasagiline-related inhibitors to human monoamine oxidases: a kinetic and crystallographic analysis
    Claudia Binda
    Department of Genetics and Microbiology, University of Pavia, via Abbiategrasso 207, Pavia 27100 Italy
    J Med Chem 48:8148-54. 2005
    ..The crystal structure of N-methyl-1(R)-aminoindan bound to MAO B shows that its aminoindan ring adopts a different orientation compared to that of rasagiline...
  35. ncbi request reprint Demonstration of peroxodiferric intermediate in M-ferritin ferroxidase reaction using rapid freeze-quench Mössbauer, resonance Raman, and XAS spectroscopies
    Carsten Krebs
    Department of Biochemistry and Molecular Biology, Pennsylvania State University, University Park, Pennsylvania 16802, USA
    Methods Enzymol 354:436-54. 2002
  36. ncbi request reprint Demonstration of isoleucine 199 as a structural determinant for the selective inhibition of human monoamine oxidase B by specific reversible inhibitors
    Frantisek Hubalek
    Department of Biochemistry, Emory University, Atlanta, Georgia 30322, USA
    J Biol Chem 280:15761-6. 2005
    ....
  37. ncbi request reprint Crystal structure of human monoamine oxidase B, a drug target enzyme monotopically inserted into the mitochondrial outer membrane
    Claudia Binda
    Department of Genetics and Microbiology, University of Pavia, via Abbiategrasso 207, 27100 Pavia, Italy
    FEBS Lett 564:225-8. 2004
    ..One of these loops (residues 99-112) also functions in opening and closing the MAO B active site cavity, which suggests that the membrane may have a role in controlling substrate binding...