Research Topics
Species | Dale EdmondsonSummaryAffiliation: Emory University Country: USA Publications
Research Grants
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Detail Information
Publications
Structure-function relationships in flavoenzyme-dependent amine oxidations: a comparison of polyamine oxidase and monoamine oxidaseClaudia Binda
Department of Genetics and Microbiology, University of Pavia, 27100 Pavia, Italy
J Biol Chem 277:23973-6. 2002- New insights into the structures and functions of human monoamine oxidases A and BD 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... - Structural insights into the mechanism of amine oxidation by monoamine oxidases A and BDale 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... - Molecular and mechanistic properties of the membrane-bound mitochondrial monoamine oxidasesDale E Edmondson
Department of Biochemistry, Emory University, Atlanta, Georgia 30322, USA
Biochemistry 48:4220-30. 2009..This review summarizes the current structural and mechanistic information available that can be utilized in the development of future highly specific neuroprotectants and cardioprotectants... - Structural comparison of human monoamine oxidases A and B: mass spectrometry monitoring of cysteine reactivitiesFrantisek 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... - Functional role of the "aromatic cage" in human monoamine oxidase B: structures and catalytic properties of Tyr435 mutant proteinsMin 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... - Mutagenic probes of the role of Ser209 on the cavity shaping loop of human monoamine oxidase AJin Wang
Department of Biochemistry, Emory University, Atlanta, GA 30322, USA
FEBS J 276:4569-81. 2009.... - 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 formsAnup K Upadhyay
Department of Biochemistry, Emory University, Atlanta, Georgia 30322, USA
Biochemistry 47:526-36. 2008.... - Structural and mechanistic studies of mofegiline inhibition of recombinant human monoamine oxidase BErika M Milczek
Department of Chemistry, Emory University, 1510 Clifton Road, Atlanta, Georgia 30322, USA
J Med Chem 51:8019-26. 2008..A mechanism to explain these structural and spectral data is proposed... - The FAD binding sites of human monoamine oxidases A and BDale 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... - Characterization of detergent purified recombinant rat liver monoamine oxidase B expressed in Pichia pastorisAnup 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... - Demonstration of isoleucine 199 as a structural determinant for the selective inhibition of human monoamine oxidase B by specific reversible inhibitorsFrantisek Hubalek
Department of Biochemistry, Emory University, Atlanta, Georgia 30322, USA
J Biol Chem 280:15761-6. 2005.... - 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 spectroscopyAnup 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... - Expression of zebrafish (Danio rerio) monoamine oxidase (MAO) in Pichia pastoris: purification and comparison with human MAO A and MAO BBetül Kacar Arslan
Department of Biochemistry, Emory University, Rollins Research Bldg, 1510 Clifton Road, Atlanta, GA 30322, USA
Protein Expr Purif 70:290-7. 2010..The K(m) (O(2)) values determined for zMAO using either benzylamine or phenylethylamine as substrates ranges from 108(+/-5) to 140(+/-21)microM. The functional behavior of this teleost MAO relative to human MAO A and MAO B is discussed... - Development of spin-labeled pargyline analogues as specific inhibitors of human monoamine oxidases A and BAnup K Upadhyay
Department of Biochemistry, Emory University, Atlanta, Georgia 30322, USA
Biochemistry 48:3928-35. 2009..Recombinant MAOB is found to be situated on the cytosolic face of the outer membrane in Pichia mitochondria... - High-level expression and purification of rat monoamine oxidase A (MAO A) in Pichia pastoris: comparison with human MAO AJin Wang
Department of Biochemistry, Emory University, Rollins Research Center, 1510 Clifton Rd, Atlanta, GA 30322, USA
Protein Expr Purif 70:211-7. 2010..Although approximately 90% identical in sequence to human MAO A, rat MAO A is a more efficient catalyst for amine neurotransmitter oxidation... - High-level expression of human liver monoamine oxidase A in Pichia pastoris: comparison with the enzyme expressed in Saccharomyces cerevisiaeMin 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... - Factors involved in the assembly of a functional molybdopyranopterin center in recombinant Comamonas acidovorans xanthine dehydrogenaseNikolai 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... - Phentermine inhibition of recombinant human liver monoamine oxidases A and BRavi 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... - Structural and mechanistic studies of arylalkylhydrazine inhibition of human monoamine oxidases A and BClaudia 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... - Plasmalogen assembly: a key flavoenzymeDale 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... - Structure of human monoamine oxidase B, a drug target for the treatment of neurological disordersClaudia 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... - Insights into the mode of inhibition of human mitochondrial monoamine oxidase B from high-resolution crystal structuresClaudia 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... - Ability of tetrahydrobiopterin analogues to support catalysis by inducible nitric oxide synthase: formation of a pterin radical is required for enzyme activityAmy 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... - Crystal structures of monoamine oxidase B in complex with four inhibitors of the N-propargylaminoindan classClaudia 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... - Crystal structure of human monoamine oxidase B, a drug target enzyme monotopically inserted into the mitochondrial outer membraneClaudia 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... - Three-dimensional structure of human monoamine oxidase A (MAO A): relation to the structures of rat MAO A and human MAO BLuigi 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... - Binding of rasagiline-related inhibitors to human monoamine oxidases: a kinetic and crystallographic analysisClaudia 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... - High-level expression and characterization of a highly functional Comamonas acidovorans xanthine dehydrogenase in Pseudomonas aeruginosaNikolai V Ivanov
Department of Chemistry, Atlanta, GA 30322, USA
Protein Expr Purif 37:72-82. 2004..A method is also described to evaluate the suitability of P. aeruginosa and other organisms as potential expression hosts for five different sources of xdh genes... - Oxygen isotope effects on electron transfer to O2 probed using chemically modified flavins bound to glucose oxidaseJustine P Roth
Department of Chemistry, University of California, Berkeley, California 94720, USA
J Am Chem Soc 126:15120-31. 2004.... - Structures of human monoamine oxidase B complexes with selective noncovalent inhibitors: safinamide and coumarin analogsClaudia 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... - Demonstration of peroxodiferric intermediate in M-ferritin ferroxidase reaction using rapid freeze-quench Mössbauer, resonance Raman, and XAS spectroscopiesCarsten Krebs
Department of Biochemistry and Molecular Biology, Pennsylvania State University, University Park, Pennsylvania 16802, USA
Methods Enzymol 354:436-54. 2002 - Human and rat monoamine oxidase-A are differentially inhibited by (S)-4-alkylthioamphetamine derivatives: insights from molecular modeling studiesAngelica 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...
Research Grants
- COVALENT FLAVIN COENZYME IN FLAVOENZYME CATALYSISDale Edmondson; Fiscal Year: 2001....
- COVALENT FLAVIN COENZYME IN FLAVOENZYME CATALYSISDale Edmondson; Fiscal Year: 2005..abstract_text> ..
- COVALENT FLAVIN COENZYME IN FLAVOENZYME CATALYSISDale Edmondson; Fiscal Year: 2009..The MAO B inhibitors would function as neuroprotective agents for the prevention of and treatment of age-related neurological disorders. The MAO A inhibitors could have clinical benefit as new types of anti-depressants. ..
- COVALENT FLAVIN COENZYMES IN FLAVOENZYME CATALYSISDale Edmondson; Fiscal Year: 1993..Anti- depressants used clinically are MAO A inhibitors while the clinical use of MAO B inhibitors is to potentiate L-Dopa therapy of patients with Parkinson's Disease...
- COVALENT FLAVIN COENZYMES IN FLAVOENZYME CATALYSISDale Edmondson; Fiscal Year: 1991..The results of these studies will be of importance in mitochondrial electron transport and in the elucidation of the mechanism of action of important enzyme systems such as succinate dehydrogenase and monoamine oxidase...
- COVALENT FLAVIN COENZYME IN FLAVOENZYME CATALYSISDale Edmondson; Fiscal Year: 2009..The MAO B inhibitors would function as neuroprotective agents for the prevention of and treatment of age-related neurological disorders. The MAO A inhibitors could have clinical benefit as new types of anti-depressants. ..