Monoamine oxidase VI. Physicochemical properties of plasma monoamine oxidase

Yamada, Hideaki; Gee, Pinkie S.; Ebata, Mitsuo; Yasunobu, Kerry T.

doi:10.1016/0926-6569(64)90347-5

Cited by 13 publications

(14 citation statements)

References 15 publications

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“…AOs can also be classified according to their cofactor: the copper-containing amine oxidases (Cu-AOs, EC 1.4.3.6) [20] and the flavincontaining amine oxidases (FAD-AOs, EC 1.4.3.4; FAD-PAOs, EC 1.5.3.11) [21]. Cu-AOs are found in more than 25 plant species, such as in Avena sativa, Helianthus tuberosus, Nicotiana tabacum, and Pisum sativum [22].…”

Section: Introductionmentioning

confidence: 99%

Evidence of parietal amine oxidase activity in Solanum torvum Sw. stem calli after Ralstonia solanacearum inoculation

Aribaud¹,

Noirot²,

Gauvin³

et al. 2009

Plant Physiology and Biochemistry

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Section: Introductionmentioning

confidence: 99%

Evidence of parietal amine oxidase activity in Solanum torvum Sw. stem calli after Ralstonia solanacearum inoculation

Aribaud¹,

Noirot²,

Gauvin³

et al. 2009

Plant Physiology and Biochemistry

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“…Monoamine oxidases from mitochondria of animal organs (9,13,31,42,59) and plasma (4,21,49,54), pea seedlings (22), various microorganisms (51)(52)(53), and the cell membranes of bacteria (27) have been characterized. The enzyme has a broad substrate specificity and plays a major role in the metabolism of biogenic amines, such as the neurotransmitters of the central nervous system.…”

mentioning

confidence: 99%

maoB, a gene that encodes a positive regulator of the monoamine oxidase gene (maoA) in Escherichia coli

et al. 1996

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The structural gene for copper-and topa quinone-containing monoamine oxidase (maoA) and an unknown amine oxidase gene have been located at 30.9 min on the Escherichia coli chromosome. Deletion analysis showed that the unknown gene was located within a 1.1-kb cloned fragment adjacent to the maoA gene. The nucleotide sequence of this fragment was determined, and a single open reading frame (maoB) consisting of 903 bp was found. The gene encoded a polypeptide with a predicted molecular mass of 34,619 Da which was correlated with the migration on a sodium dodecyl sulfate-polyacrylamide gel. The predicted amino acid sequence of the MaoB protein was identical to the NH 2 -terminal amino acid sequence derived by Edman degradation of the protein synthesized under the self-promoter. No homology of the nucleotide sequence of maoB to the sequences of any reported genes was found. However, the amino acid sequence of MaoB showed a high level of homology with respect to the helix-turn-helix motif of the AraC family in its C terminus. The homology search and disruption of maoA on the chromosome led to the conclusion that MaoB is a transcriptional activator of maoA but not an amine oxidase. The consensus sequence of the cyclic AMP-cyclic AMP receptor protein complex binding domain was adjacent to the putative promoter for the maoB gene. By use of lac gene fusions with the maoA and maoB genes, we showed that the maoA gene is regulated by tyramine and MaoB and that the expression of the maoB gene is subject to catabolite repression. Thus, it seems likely that tyramine and the MaoB protein activate the transcription of maoA by binding to the regulatory region of the maoA gene.

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“…Amine oxidase from bovine plasma has been studied extensively by Yasunobu and co-workers (21)(22)(23) Ethanol Fractionation. The clarified preparation was placed in a beaker immersed in a mixture of ice and salt at -7 C. Absolute ethanol, prechilled to -7 C, was added slowly with vigorous stirring until the solution was 10% (v/v) in ethanol.…”

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confidence: 99%

Purification and Properties of Amine Oxidase from Epicotyls of Pisum sativum

McGowan¹,

Muir²

1971

Plant Physiol.

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A procedure has been developed for the purification of amine oxidase (E.C. 1.4.3.4) from etiolated pea epicotyls (Pisum sativum cv. Little Marvel). The enzyme is sensitive to copper chelating reagents and carbonyl reagents, but is not inhibited by sulfhydryl reagents. The purified enzyme has a molecular weight of 1.85 X 105, as determined by sedimentation equilibrium centrifugation, and has been shown to be specifically stimulated by phosphate.enzyme. In addition, the enzymes from bovine and porcine plasma have been found to contain pyridoxal phosphate (4, 23). The amine oxidase from porcine plasma has a molecular weight of 1.95 X 105 (5), and the amine oxidase from bovine plasma has a molecular weight of 1.7 x 10' (1). The enzyme from bovine plasma has a subunit molecular weight of 8.05 X 104(1).The study reported here describes a purification procedure for the amine oxidase from etiolated pea epicotyls, confirmation of copper and R-COR as functional groups in catalysis, the molecular weight as determined by ultracentrifugation, and the requirement of phosphate for maximal catalysis.Recent studies in this laboratory have indicated the possibility that IAA synthesis in Pisum could proceed through tryptamine and that the enzyme responsible for catalyzing this reaction could be purified (10, 14). As part of an investigation of IAA biosynthesis in Pisum, an enzyme which forms IAA from tryptamine was purified and found to be an amine oxidase. In view of the wide interest in amine oxidases from mammals and the one amine oxidase purified from a higher plant, it was decided to characterize this enzyme for a further understanding of the plant enzyme and for a comparison with the mammalian enzymes.Amine oxidase from plants was first purified and studied by Mann, who found that the enzyme was a pink, copper-containing protein which was sensitive to carbonyl reagents (12). The visible absorption spectrum of this enzyme had an absorbance maximum at 500 nm (13). This absorbance maximum could be shifted to lower wavelengths by incubation of the enzyme with substrate under anaerobic conditions or by incubation of the enzyme with copper-chelating reagents. These spectral shifts could be reversed by incubation under aerobic conditions in the first case and cupric ions in the second (9). The enzyme was found to be active in catalyzing the oxidative deamination of a wide variety of substrates (9). The purified enzyme had an s5,,0 of 7.7S, measured from sedimentation velocity centrifugation, and a molecular weight of 9.6 X 104, calculated from electron micrographs (9). Recently, Yamasaki et al. (24) have shown that the binding of oxygen to amine oxidase from peas is dependent upon amine concentration.Amine oxidase from bovine plasma has been studied extensively by Yasunobu and co-workers (21-23) who have found that the visible absorbance spectrum, copper content, and sensitivity to carbonyl reagents are similar to the plant

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Monoamine oxidase VI. Physicochemical properties of plasma monoamine oxidase

Cited by 13 publications

References 15 publications

Evidence of parietal amine oxidase activity in Solanum torvum Sw. stem calli after Ralstonia solanacearum inoculation

Evidence of parietal amine oxidase activity in Solanum torvum Sw. stem calli after Ralstonia solanacearum inoculation

maoB, a gene that encodes a positive regulator of the monoamine oxidase gene (maoA) in Escherichia coli

Purification and Properties of Amine Oxidase from Epicotyls of Pisum sativum

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