Amine oxidase.  XII.  Association and dissociation, and number of subunits of beef plasma amine oxidase

Achee, Frances M.; Chervenka, Charles H.; Smith, Richard A.; Yasunobu, Kerry T.

doi:10.1021/bi00852a027

Cited by 36 publications

(10 citation statements)

References 20 publications

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“…Kumagai et al (1978) obtained a value for the subunit molecular weight of the A. niger enzyme of 125000 and suggested that the active enzyme is a dimer. Associationdissociation phenomena have been reported previously with pig plasma amine oxidase (Achee et al, 1968) and pig kidney diamine oxidase (Pionetti, 1974). The fact that the two amine oxidases of C. boidinii have similarly sized polypeptide subunits may indicate the possibility that they have evolved from duplicated genes (Clarke, 1978), and have undergone considerable changes in their quaternary structure as well as in their substrate specificity.…”

Section: Discussionmentioning

confidence: 77%

Microbial oxidation of amines. Distribution, purification and properties of two primary-amine oxidases from the yeast Candida boidinii grown on amines as sole nitrogen source

Haywood

Large

1981

Biochemical Journal

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1. The yeast Candida boidinii was grown on glucose as carbon source with a range of amines and amino acids as nitrogen sources. Cells grown on amines contained elevated activities of catalase. If the amines contained N-methyl groups, formaldehyde dehydrogenase, formate dehydrogenase and S-formylglutathione hydrolase were also elevated in activity compared with cells grown on (NH(4))(2)SO(4). 2. Cells grown on all the amines tested, but not those grown on urea or amino acids, contained an oxidase attacking primary amines, which is referred to as methylamine oxidase. In addition, cells grown on some amines contained a second amine oxidase, which is referred to as benzylamine oxidase. 3. Both amine oxidases were purified to near homogeneity. 4. Benzylamine oxidase was considerably more stable at 45 and 50 degrees C than was methylamine oxidase. 5. Both enzymes had a pH optimum in the region of 7.0, and had a considerable number of substrates in common. There were, however, significant differences in the substrate specificity of the two enzymes. The ratio V/K(app.) (m) increased with increasing n-alkyl carbon chain length for benzylamine oxidase, but decreased for methylamine oxidase. 6. Both enzymes showed similar sensitivity to carbonyl-group reagents, copper-chelating agents and other typical ;diamine oxidase inhibitors'. 7. The stoicheiometry for the reaction catalysed by each enzyme was established. 8. The kinetics of methylamine oxidase were examined by varying the methylamine and oxygen concentrations in turn. A non-Ping Pong kinetic pattern with intersecting double-reciprocal plots was obtained, giving K(m) values of 10mum for O(2) and 198mum for methylamine. The significance of this unusual kinetic behaviour is discussed. Similar experiments were not possible with the benzylamine oxidase, because it seemed to have an even lower K(m) for O(2). 9. Both enzymes had similar subunit M(r) values of about 80000, but the benzylamine oxidase behaved as if it were usually a dimer, M(r) 136000, which under certain conditions aggregated to a tetramer, M(r) 288000. Methylamine oxidase was mainly in the form of an octamer, M(r) 510000, which gave rise quite readily to dimers of M(r) 150000, and on gel filtration behaved as if the M(r) was 286000.

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Section: Discussionmentioning

confidence: 77%

Microbial oxidation of amines. Distribution, purification and properties of two primary-amine oxidases from the yeast Candida boidinii grown on amines as sole nitrogen source

Haywood

Large

1981

Biochemical Journal

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“…The specific activity of the purified polyamine oxidase from A. suum was about 2300 nmol of H202/min per mg, which is 2-fold higher than that reported for the enzyme from rat liver (Holtta, 1977) (Holtta, 1977). In contrast, the serum amine oxidase exists as a polymer with subunits of 90 kDa (Achee et al, 1968;Morgan, 1985 (H6ltta, 1977;Morgan, 1985). The carbonyl reagents isoniazid and iproniazid do not affect the tissue-type polyamine oxidase (Holtta, 1977), but both compounds were found to inhibit the nematode enzyme as well as the serum amine oxidases (Tabor et al, 1954;Buffoni, 1966;Holtta et al, 1975).…”

Section: Discussionmentioning

confidence: 99%

Purification and characterization of polyamine oxidase from Ascaris suum

Müller

Walter

1992

Biochemical Journal

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The interconversion of polyamines in the parasite nematode Ascaris suum by a novel type of polyamine oxidase was demonstrated. The nematode enzyme was clearly distinguishable from monoamine and diamine oxidases as well as from the mammalian polyamine oxidase, as shown by the use of the specific inhibitors pargyline, aminoguanidine and MDL 72527 respectively. All three inhibitors had no effect on the parasite polyamine oxidase, and the enzyme did not accept diamines such as putrescine, cadaverine or histamine as substrates. The parasite polyamine oxidase selectively oxidizes spermine and spermidine but not N-acetylated polyamines, whereas the mammalian tissue-type polyamine oxidase shows preference for the N-acetylated polyamines. These results suggest a regulatory function of the nematode polyamine oxidase in the degradation and interconversion of polyamines in parasite nematodes. The enzyme was purified to homogeneity by gel filtration, preparative isoelectric focusing and subsequent affinity chromatography on spermine-and berenil-Sepharose 4B. With respect to reaction type, the prosthetic group FAD, the molecular mass (66 kDa) and the contents of thiol and carbonyl groups, the polyamine oxidase from A. suum is similar to the isofunctional enzyme of mammalian tissue.

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“…The enzyme is a disulfide-linked homodimer; the monomeric molecular mass is 85,000 (17). The specific activity predicts a topaquinone content of 0.6 per monomeric subunit (18,19).…”

Section: Methodsmentioning

confidence: 99%

Amine binding and oxidation at the catalytic site for photosynthetic water oxidation

Ouellette

Anderson²,

Barry³

1998

Proc. Natl. Acad. Sci. U.S.A.

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Photosynthetic water oxidation occurs at the Mn-containing catalytic site of photosystem II (PSII). By the use of 14 C-labeled amines and SDS-denaturing PAGE, covalent adducts derived from primary amines and the PSII subunits, CP47, D2͞D1, and the Mn-stabilizing protein, can be observed. When PSII contains the 18-and 24-kDa extrinsic proteins, which restrict access to the active site, no 14 C labeling is obtained. NaCl, but not Na 2 SO 4 , competes with 14 C labeling in Mn-containing PSII preparations, and the concentration dependence of this competition parallels the activation of oxygen evolution. Formation of 14 C-labeled adducts is observed in the presence or in the absence of a functional manganese cluster. However, no significant Cl

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Amine oxidase. XII. Association and dissociation, and number of subunits of beef plasma amine oxidase

Cited by 36 publications

References 20 publications

Microbial oxidation of amines. Distribution, purification and properties of two primary-amine oxidases from the yeast Candida boidinii grown on amines as sole nitrogen source

Microbial oxidation of amines. Distribution, purification and properties of two primary-amine oxidases from the yeast Candida boidinii grown on amines as sole nitrogen source

Purification and characterization of polyamine oxidase from Ascaris suum

Amine binding and oxidation at the catalytic site for photosynthetic water oxidation

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