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Article ; Online: Purification of MAO A and MAO B from Mammalian Tissue Sources.

Edmondson, Dale E

Methods in molecular biology (Clifton, N.J.)

2022 Volume 2558, Page(s) 1–10

Abstract: Procedures are described for the purification of the mitochondrial-bound enzymes human and bovine monoamine oxidases A and B (MAO A and B) from placental and liver tissue sources, respectively. Enzyme purification follows isolation of the mitochondria ... ...

Abstract	Procedures are described for the purification of the mitochondrial-bound enzymes human and bovine monoamine oxidases A and B (MAO A and B) from placental and liver tissue sources, respectively. Enzyme purification follows isolation of the mitochondria and preparation of outer membrane particles. The membrane-bound enzymes are solubilized by treatment of membranes with phospholipases and detergent extraction. Functional bovine MAO B is purified by polymer fractionation and differential centrifugation. Functional human MAO A is purified by ion-exchange DEAE-Sepharose chromatography.
MeSH term(s)	Animals ; Cattle ; Detergents ; Female ; Humans ; Mammals ; Mitochondria, Liver ; Monoamine Oxidase ; Phospholipases ; Placenta ; Polymers ; Pregnancy
Chemical Substances	Detergents ; Polymers ; Monoamine Oxidase (EC 1.4.3.4) ; Phospholipases (EC 3.1.-)
Language	English
Publishing date	2022-09-28
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ISSN	1940-6029
ISSN (online)	1940-6029
DOI	10.1007/978-1-0716-2643-6_1
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Article ; Online: Purification of Recombinant Eukaryotic MAO A and MAO B Utilizing the Pichia pastoris Expression System.

Edmondson, Dale E

Methods in molecular biology (Clifton, N.J.)

2022 Volume 2558, Page(s) 11–22

Abstract: Procedures are described for the heterologous expression and purification of the mitochondrial-bound enzymes human and rat monoamine oxidases A and B and zebrafish MAO in the yeast Pichia pastoris. Enzyme expression is under control of a methanol oxidase ...

Abstract	Procedures are described for the heterologous expression and purification of the mitochondrial-bound enzymes human and rat monoamine oxidases A and B and zebrafish MAO in the yeast Pichia pastoris. Enzyme expression is under control of a methanol oxidase promoter and similar procedures have been developed for the preparation of membrane particles and detergent solubilization of the functional enzymes. Similarities and differences are described in the procedures for purification of the respective enzymes using standard column chromatographic techniques to provide enzyme yields in the range of 100-300 mg from 1 L of cell culture.
MeSH term(s)	Animals ; Detergents/metabolism ; Detergents/pharmacology ; Eukaryota/metabolism ; Humans ; Monoamine Oxidase/genetics ; Pichia/genetics ; Pichia/metabolism ; Rats ; Recombinant Proteins/metabolism ; Saccharomycetales ; Zebrafish/metabolism
Chemical Substances	Detergents ; Recombinant Proteins ; Monoamine Oxidase (EC 1.4.3.4)
Language	English
Publishing date	2022-09-28
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ISSN	1940-6029
ISSN (online)	1940-6029
DOI	10.1007/978-1-0716-2643-6_2
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Article ; Online: Crystallization of Human Monoamine Oxidase B.

Binda, Claudia / Edmondson, Dale E / Mattevi, Andrea

Methods in molecular biology (Clifton, N.J.)

2022 Volume 2558, Page(s) 115–122

Abstract: The interest in monoamine oxidases A and B (MAO A and B) is due to their central role in regulating the balance of neurotransmitters, both in the central nervous system and in peripheral organs. As validated drug targets for depression and Parkinson's ... ...

Abstract	The interest in monoamine oxidases A and B (MAO A and B) is due to their central role in regulating the balance of neurotransmitters, both in the central nervous system and in peripheral organs. As validated drug targets for depression and Parkinson's disease, the elucidation of their crystal structures was an essential step to guide drug design investigations. The development of the heterologous expression system of MAO B in Pichia pastoris and the identification of the detergent, buffer, and precipitant conditions allowed to determine the first crystal structure of human MAO B in 2002. A detailed protocol to obtain reproducible MAO B crystals is described.
MeSH term(s)	Crystallization ; Detergents ; Drug Design ; Humans ; Monoamine Oxidase/genetics ; Monoamine Oxidase/metabolism ; Parkinson Disease
Chemical Substances	Detergents ; Monoamine Oxidase (EC 1.4.3.4)
Language	English
Publishing date	2022-09-28
Publishing country	United States
Document type	Journal Article
ISSN	1940-6029
ISSN (online)	1940-6029
DOI	10.1007/978-1-0716-2643-6_9
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Article: Monoamine Oxidases.

Edmondson, Dale E / Binda, Claudia

Sub-cellular biochemistry

2018 Volume 87, Page(s) 117–139

Abstract: Monoamine oxidases A and B (MAO A and B) are mammalian flavoenzymes bound to the outer mitochondrial membrane. They were discovered almost a century ago and they have been the subject of many biochemical, structural and pharmacological investigations due ...

Abstract	Monoamine oxidases A and B (MAO A and B) are mammalian flavoenzymes bound to the outer mitochondrial membrane. They were discovered almost a century ago and they have been the subject of many biochemical, structural and pharmacological investigations due to their central role in neurotransmitter metabolism. Currently, the treatment of Parkinson's disease involves the use of selective MAO B inhibitors such as rasagiline and safinamide. MAO inhibition was shown to exert a general neuroprotective effect as a result of the reduction of oxidative stress produced by these enzymes, which seems to be relevant also in non-neuronal contexts. MAOs were successfully expressed as recombinant proteins in Pichia pastoris, which allowed a thorough biochemical and structural characterization. These enzymes are characterized by a globular water-soluble main body that is anchored to the mitochondrial membrane through a C-terminal α-helix, similar to other bitopic membrane proteins. In both MAO A and MAO B the enzyme active site consists of a hydrophobic cavity lined by residues that are conserved in the two isozymes, except for few details that determine substrate and inhibitor specificity. In particular, human MAO B features a dual-cavity active site whose conformation depends on the size of the bound ligand. This article provides a comprehensive and historical review of MAOs and the state-of-the-art of these enzymes as membrane drug targets.
MeSH term(s)	Animals ; Catalytic Domain ; Humans ; Monoamine Oxidase/chemistry ; Monoamine Oxidase/metabolism ; Monoamine Oxidase Inhibitors/chemistry ; Monoamine Oxidase Inhibitors/therapeutic use ; Oxidative Stress/drug effects ; Parkinson Disease/drug therapy ; Parkinson Disease/enzymology ; Parkinson Disease/pathology ; Protein Structure, Secondary
Chemical Substances	Monoamine Oxidase Inhibitors ; Monoamine Oxidase (EC 1.4.3.4) ; monoamine oxidase A, human (EC 1.4.3.4.)
Language	English
Publishing date	2018-02-20
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ISSN	0306-0225 ; 0096-8757
ISSN	0306-0225 ; 0096-8757
DOI	10.1007/978-981-10-7757-9_5
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Article ; Online: Hydrogen peroxide produced by mitochondrial monoamine oxidase catalysis: biological implications.

Edmondson, Dale E

Current pharmaceutical design

2013 Volume 20, Issue 2, Page(s) 155–160

Abstract: The biological roles of mitochondrial-produced reactive oxygen species continue to receive intensive investigation since one of the products (H₂O₂) has important cellular signaling roles as well as contributing to apoptotic responses. In general, the ... ...

Abstract	The biological roles of mitochondrial-produced reactive oxygen species continue to receive intensive investigation since one of the products (H₂O₂) has important cellular signaling roles as well as contributing to apoptotic responses. In general, the source of mitochondrial reactive oxygen species is thought to be the superoxide anion produced from Complex I and Complex III components of the electron transport chain. Superoxide anion readily dismutates to H₂O₂ with subsequent transformation to the hydroxyl radical by Fenton chemistry. An overlooked source of H₂O₂ in the mitochondrion is its production as a catalytic reaction product from the outer membrane enzymes: monoamine oxidases A and B. The literature is reviewed to document identified degenerative reactions attributed to H₂O₂ produced by MAO A and by MAO B catalysis. Available information on the topologies of these enzymes in the mitochondrial outer membrane is also discussed with relevance to H₂O₂ production and involvement in cell signaling functions as well as degenerative effects.
MeSH term(s)	Apoptosis/physiology ; Electron Transport/physiology ; Humans ; Hydrogen Peroxide/metabolism ; Mitochondria/metabolism ; Mitochondrial Membranes/metabolism ; Monoamine Oxidase/metabolism ; Reactive Oxygen Species/metabolism ; Signal Transduction/physiology ; Superoxides/metabolism
Chemical Substances	Reactive Oxygen Species ; Superoxides (11062-77-4) ; Hydrogen Peroxide (BBX060AN9V) ; Monoamine Oxidase (EC 1.4.3.4)
Language	English
Publishing date	2013-04-07
Publishing country	United Arab Emirates
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Review
ZDB-ID	1304236-1
ISSN	1873-4286 ; 1381-6128
ISSN (online)	1873-4286
ISSN	1381-6128
DOI	10.2174/13816128113190990406
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Article: Plasmalogen assembly: a key flavoenzyme.

Edmondson, Dale E

Structure (London, England : 1993)

2007 Volume 15, Issue 6, Page(s) 639–641

Abstract: The structural properties of alkyldihydroxyacetonephosphate synthase (ADPS) described by Razeto et al. (2007) in this issue of Structure provide new insights into how this peroxisomal flavoenzyme catalyzes a nonredox reaction in the conversion of an ... ...

Abstract	The structural properties of alkyldihydroxyacetonephosphate synthase (ADPS) described by Razeto et al. (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.
MeSH term(s)	Alkyl and Aryl Transferases/chemistry ; Alkyl and Aryl Transferases/genetics ; Alkyl and Aryl Transferases/metabolism ; Amino Acid Substitution ; Binding Sites ; Catalysis ; Dimerization ; Flavin-Adenine Dinucleotide/chemistry ; Flavin-Adenine Dinucleotide/metabolism ; Histidine/metabolism ; Humans ; Models, Biological ; Peroxisomes/enzymology ; Peroxisomes/metabolism ; Phenylalanine/metabolism ; Phospholipid Ethers/metabolism ; Protein Binding ; Substrate Specificity
Chemical Substances	Phospholipid Ethers ; Flavin-Adenine Dinucleotide (146-14-5) ; Phenylalanine (47E5O17Y3R) ; Histidine (4QD397987E) ; Alkyl and Aryl Transferases (EC 2.5.-) ; alkylglycerone-phosphate synthase (EC 2.5.1.26)
Language	English
Publishing date	2007-06
Publishing country	United States
Document type	Comment ; News
ZDB-ID	1213087-4
ISSN	1878-4186 ; 0969-2126
ISSN (online)	1878-4186
ISSN	0969-2126
DOI	10.1016/j.str.2007.05.003
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Zs.A 4141: Show issues

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Article ; Online: Topological probes of monoamine oxidases A and B in rat liver mitochondria: inhibition by TEMPO-substituted pargyline analogues and inactivation by proteolysis.

Wang, Jin / Edmondson, Dale E

Biochemistry

2011 Volume 50, Issue 13, Page(s) 2499–2505

Abstract: ... on differing faces of the mitochondrial outer membrane [Upadhyay, A., and Edmondson, D. E. (2009) Biochemistry ...

Abstract	TEMPO-substituted pargyline analogues differentially inhibit recombinant human monoamine oxidase A (MAO A) and B (MAO B) in intact yeast mitochondria, suggesting these membrane-bound enzymes are located on differing faces of the mitochondrial outer membrane [Upadhyay, A., and Edmondson, D. E. (2009) Biochemistry 48, 3928]. This approach is extended to the recombinant rat enzymes and to rat liver mitochondria. The differential specificities exhibited for human MAO A and MAO B by the m- and p-amido TEMPO pargylines are not as absolute with the rat enzymes. Similar patterns of reactivity are observed for rat MAO A and B in mitochondrial outer membrane preparations expressed in Pichia pastoris or isolated from rat liver. In intact yeast mitochondria, recombinant rat MAO B is inhibited by the pargyline analogue whereas MAO A activity shows no inhibition. Intact rat liver mitochondria exhibit an inhibition pattern opposite to that observed in yeast where MAO A is inhibited and MAO B activity is unaffected. Protease inactivation studies show specificity in that MAO A is sensitive to trypsin whereas MAO B is sensitive to β-chymotrypsin. In intact mitochondrial preparations, MAO A is readily inactivated in rat liver but not in yeast upon trypsin treatment and MAO B is readily inactivated by β-chymotrypsin in yeast but not in rat liver. These data show MAO A is oriented on the cytosolic face and MAO B is situated on the surface facing the intermembrane space of the mitochondrial outer membrane in rat liver. The differential mitochondrial outer membrane topology of MAO A and MAO B is relevant to their inhibition by drugs designed to be cardioprotectants or neuroprotectants.
MeSH term(s)	Animals ; Chymotrypsin/metabolism ; Humans ; Hydrolysis ; Kinetics ; Mitochondria, Liver/drug effects ; Mitochondria, Liver/enzymology ; Mitochondrial Membranes/drug effects ; Mitochondrial Membranes/enzymology ; Mitochondrial Membranes/metabolism ; Monoamine Oxidase/metabolism ; Monoamine Oxidase Inhibitors/chemistry ; Monoamine Oxidase Inhibitors/pharmacology ; Pargyline/analogs & derivatives ; Pargyline/chemistry ; Pargyline/pharmacology ; Pichia/drug effects ; Pichia/metabolism ; Piperidines/chemistry ; Rats ; Recombinant Proteins/antagonists & inhibitors ; Recombinant Proteins/metabolism ; Species Specificity ; Spin Labels ; Substrate Specificity ; Trypsin/metabolism
Chemical Substances	2,2,6,6-tetramethyl-1-piperidine ; Monoamine Oxidase Inhibitors ; Piperidines ; Recombinant Proteins ; Spin Labels ; Pargyline (9MV14S8G3E) ; Monoamine Oxidase (EC 1.4.3.4) ; Chymotrypsin (EC 3.4.21.1) ; Trypsin (EC 3.4.21.4)
Language	English
Publishing date	2011-03-07
Publishing country	United States
Document type	Comparative Study ; Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	1108-3
ISSN	1520-4995 ; 0006-2960
ISSN (online)	1520-4995
ISSN	0006-2960
DOI	10.1021/bi101722b
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Article ; Online: ²H kinetic isotope effects and pH dependence of catalysis as mechanistic probes of rat monoamine oxidase A: comparisons with the human enzyme.

Wang, Jin / Edmondson, Dale E

Biochemistry

2011 Volume 50, Issue 35, Page(s) 7710–7717

Abstract: Monoamine oxidase A (MAO A) is a mitochondrial outer membrane-bound flavoenzyme important in the regulation of serotonin and dopamine levels. Because the rat is extensively used as an animal model in drug studies, it is important to understand how rat ... ...

Abstract	Monoamine oxidase A (MAO A) is a mitochondrial outer membrane-bound flavoenzyme important in the regulation of serotonin and dopamine levels. Because the rat is extensively used as an animal model in drug studies, it is important to understand how rat MAO A behaves in comparison with the more extensively studied human enzyme. For many reversible inhibitors, rat MAO A exhibits K(i) values similar to those of human MAO A. The pH profile of k(cat) for rat MAO A shows a pK(a) of 8.2 ± 0.1 for the benzylamine ES complex and pK(a) values of 7.5 ± 0.1 and 7.6 ± 0.1 for the ES complexes with p-CF(3)-(1)H- and p-CF(3)-(2)H-benzylamine, respectively. In contrast to the human enzyme, the rat enzyme exhibits a single pK(a) value (8.3 ± 0.1) with k(cat)/K(m) for benzylamine versus pH and pK(a) values of 7.8 ± 0.1 and 8.1 ± 0.2 for the ascending limbs, respectively, of k(cat)/K(m) versus pH profiles for p-CF(3)-(1)H- and p-CF(3)-(2)H-benzylamine and 9.3 ± 0.1 and 9.1 ± 0.2 for the descending limbs, respectively. The oxidation of para-substituted benzylamine substrate analogues by rat MAO A has large deuterium kinetic isotope effects on k(cat) and on k(cat)/K(m). These effects are pH-independent and range from 7 to 14, demonstrating a rate-limiting α-C-H bond cleavage step in catalysis. Quantitative structure-activity correlations of log k(cat) with the electronic substituent parameter (σ) at pH 7.5 and 9.0 show a dominant contribution with positive ρ values (1.2-1.3) and a pH-independent negative contribution from the steric term. Quantitative structure-activity relationship analysis of the binding affinities of the para-substituted benzylamine analogues for rat MAO A shows an increased van der Waals volume (V(w)) increases the affinity of the deprotonated amine for the enzyme. These results demonstrate that rat MAO A exhibits functional properties similar but not identical with those of the human enzyme and provide additional support for C-H bond cleavage via a polar nucleophilic mechanism.
MeSH term(s)	Animals ; Catalysis ; Deuterium/chemistry ; Deuterium/pharmacokinetics ; Humans ; Hydrogen/pharmacokinetics ; Hydrogen-Ion Concentration ; Isotopes/pharmacokinetics ; Monoamine Oxidase/chemistry ; Monoamine Oxidase/metabolism ; Protein Binding/physiology ; Quantitative Structure-Activity Relationship ; Rats ; Species Specificity
Chemical Substances	Isotopes ; Hydrogen (7YNJ3PO35Z) ; Deuterium (AR09D82C7G) ; Monoamine Oxidase (EC 1.4.3.4)
Language	English
Publishing date	2011-08-16
Publishing country	United States
Document type	Comparative Study ; Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	1108-3
ISSN	1520-4995 ; 0006-2960
ISSN (online)	1520-4995
ISSN	0006-2960
DOI	10.1021/bi200951z
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Zs.A 217: Show issues

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Article ; Online: Expression of zebrafish (Danio rerio) monoamine oxidase (MAO) in Pichia pastoris: purification and comparison with human MAO A and MAO B.

Arslan, Betül Kacar / Edmondson, Dale E

Protein expression and purification

2010 Volume 70, Issue 2, Page(s) 290–297

Abstract: The expression, purification and characterization of zebrafish monoamine oxidase (zMAO) using the methylotropic yeast Pichia pastoris expression system is described. A 1L fermentation culture of Pichia pastoris containing the gene encoding zMAO under ... ...

Abstract	The expression, purification and characterization of zebrafish monoamine oxidase (zMAO) using the methylotropic yeast Pichia pastoris expression system is described. A 1L fermentation culture of Pichia pastoris containing the gene encoding zMAO under control of the methanol oxidase promotor expresses approximately 200mg of zMAO exhibiting 300 U of total activity. The enzyme is found in the mitochondrial fraction of the expression host and is purified in a 30% yield as a homogenous species with a M(r) of approximately 60,000 on SDS-PAGE and a mass of 58,525+/-40 Da from MALDI-TOF measurements. The zMAO preparation contains one mole of covalent flavin cofactor per mole of enzyme and exhibits >80% functionality. The covalent flavin exhibits fluorescence and EPR spectral properties consistent with known properties of 8 alpha-S-cysteinyl FAD. Chemical degradation of the flavin peptide results in the liberation of FAD. zMAO exhibits no immuno-chemical cross-reactivity with polyclonal anti-sera raised against human MAO A. The enzyme preparation exhibits reasonable thermostability up to a temperature of 30 degrees C. Benzylamine is oxidized with a k(cat) value of 4.7+/-0.1 min(-1) (K(m)=82+/-9 microM) and the enzyme oxidizes phenylethylamine with a k(cat) value of 204 min(-1) (K(m)=86+/-13 microM). 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.
MeSH term(s)	Amino Acid Sequence ; Animals ; Benzylamines/metabolism ; Cloning, Molecular ; Electrophoresis, Polyacrylamide Gel ; Enzyme Stability ; Hot Temperature ; Humans ; Kinetics ; Molecular Sequence Data ; Monoamine Oxidase/biosynthesis ; Monoamine Oxidase/isolation & purification ; Monoamine Oxidase/metabolism ; Monoamine Oxidase Inhibitors/pharmacology ; Phenethylamines/metabolism ; Pichia/metabolism ; Recombinant Proteins/antagonists & inhibitors ; Recombinant Proteins/metabolism ; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization ; Zebrafish
Chemical Substances	Benzylamines ; Monoamine Oxidase Inhibitors ; Phenethylamines ; Recombinant Proteins ; benzylamine (A1O31ROR09) ; Monoamine Oxidase (EC 1.4.3.4)
Language	English
Publishing date	2010-01-14
Publishing country	United States
Document type	Comparative Study ; Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	1055455-5
ISSN	1096-0279 ; 1046-5928
ISSN (online)	1096-0279
ISSN	1046-5928
DOI	10.1016/j.pep.2010.01.005
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Zs.A 3084: Show issues

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Article ; Online: Development of spin-labeled pargyline analogues as specific inhibitors of human monoamine oxidases A and B.

Upadhyay, Anup K / Edmondson, Dale E

Biochemistry

2009 Volume 48, Issue 18, Page(s) 3928–3935

Abstract: Three TEMPO-conjugated pargyline analogues (ParSL-1, ParSL-2, and ParSL-3) have been synthesized and their inhibitory properties tested for the two human monoamine oxidase isoforms (hMAOA and hMAOB). The three analogues differ in flexibility and ... ...

Abstract	Three TEMPO-conjugated pargyline analogues (ParSL-1, ParSL-2, and ParSL-3) have been synthesized and their inhibitory properties tested for the two human monoamine oxidase isoforms (hMAOA and hMAOB). The three analogues differ in flexibility and substituent positions (para or meta) of the linkers connecting the TEMPO group to the pargyline phenyl ring. ParSL-1 contains a flexible acetamido (-CH(2)-CO-NH-) linker connecting the two moieties at the para position. In contrast, the TEMPO moieties in ParSL-2 and ParSL-3 are attached with rigid amido (-CO-NH-) linkers to the para or meta positions of the pargyline phenyl ring, respectively. These variations in conformational flexibility and substituent position are shown to have profound effects in tuning the specificities of these analogues toward the two MAO isoforms. ParSL-1 irreversibly inhibits either MAOA and MAOB, ParSL-2 inhibits only MAOB (K(i) = 15 +/- 5 microM), and ParSL-3 is found to be specific for MAOA (K(i) = 268 +/- 72 microM). These results thus provide additional insights into the role of conformational flexibility and structural properties of MAO inhibitors in tuning their isoform specificities. These active site probes have been used to determine the topological orientation of these enzymes in the mitochondrial membrane. Studies with intact mitochondria show MAOA is topologically on the cytosolic face of the outer membrane in human placenta but recombinant MAOA is situated on the opposite inner face in Pichia mitochondria. Recombinant MAOB is found to be situated on the cytosolic face of the outer membrane in Pichia mitochondria.
MeSH term(s)	Electron Spin Resonance Spectroscopy ; Humans ; Kinetics ; Monoamine Oxidase/drug effects ; Monoamine Oxidase Inhibitors/pharmacology ; Pargyline/analogs & derivatives ; Pargyline/chemistry ; Recombinant Proteins/drug effects ; Spectrometry, Mass, Electrospray Ionization ; Spectrophotometry, Ultraviolet ; Spin Labels
Chemical Substances	Monoamine Oxidase Inhibitors ; Recombinant Proteins ; Spin Labels ; Pargyline (9MV14S8G3E) ; Monoamine Oxidase (EC 1.4.3.4)
Language	English
Publishing date	2009-03-19
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	1108-3
ISSN	1520-4995 ; 0006-2960
ISSN (online)	1520-4995
ISSN	0006-2960
DOI	10.1021/bi9002106
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