Pea Seedling Histaminase as a Novel Therapeutic Approach to Anaphylactic and Inflammatory Disorders

Amine oxidases (AOs) are ubiquitous enzymes involved in the metabolism of biogenic amines. Copper AOs (Cu-AOs) catalyze the oxidative deamination of primary amine groups of several biogenic amines, such as putrescine, cadaverine, and histamine. In the present review, the effects of a plant amine oxidase (Cu-AO, histaminase, EC1.4.3.6) purified from pea seedlings in the modulation of IgE-mediated allergic reactions, and in the prevention of cardiac and splachnic postischemic reperfusion damage are reported.

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Unique protonation states of aspartate and topaquinone in the active site of copper amine oxidase

RSC Advances ◽

10.1039/d0ra06365g ◽

2020 ◽

Vol 10 (63) ◽

pp. 38631-38639

Author(s):

Mitsuo Shoji ◽

Takeshi Murakawa ◽

Mauro Boero ◽

Yasuteru Shigeta ◽

Hideyuki Hayashi ◽

...

Keyword(s):

Biogenic Amines ◽

Active Site ◽

Amine Oxidase ◽

First Principle ◽

Amine Oxidases ◽

Oxidative Deamination ◽

Copper Amine Oxidase ◽

First Principle Calculations ◽

Copper Amine Oxidases ◽

Copper Amine

Copper amine oxidases catalyze the oxidative deamination of biogenic amines. We investigated the unique protonation states in the active site using first-principle calculations.

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Mechanism of reaction of allylamine with the quinoprotein methylamine dehydrogenase

Biochemical Journal ◽

10.1042/bj3080487 ◽

1995 ◽

Vol 308 (2) ◽

pp. 487-492 ◽

Cited By ~ 10

Author(s):

V L Davidson ◽

M E Graichen ◽

L H Jones

Keyword(s):

Competitive Inhibition ◽

Amine Oxidase ◽

Kinetic Studies ◽

Kinetic Mechanism ◽

Competitive Inhibitor ◽

Amine Oxidases ◽

Methylamine Dehydrogenase ◽

Oxidative Deamination ◽

Tryptophan Tryptophylquinone ◽

Mechanism Of Reaction

Allylamine did not serve as an efficient substrate for methylamine dehydrogenase (EC 1.4.99.3) in a steady-state assay of activity and appeared to act as a competitive inhibitor of methylamine oxidation by methylamine dehydrogenase. Transient kinetic studies, however, revealed that allylamine rapidly reduced the tryptophan tryptophylquinone (TTQ) cofactor of methylamine dehydrogenase. The rate of TTQ reduction by allylamine was 322 s-1, slightly faster than the rate of reduction by methylamine. These data were explained by a kinetic mechanism in which allylamine and methylamine are alternative substrates for methylamine dehydrogenase. The apparent competitive inhibition by allylamine is due to a very slow rate of release of the aldehyde product, 0.28 s-1, relative to a rate of 18.6 s-1 for the release of the aldehyde product of methylamine oxidation. A reaction mechanism is proposed for the oxidative deamination of allylamine by methylamine dehydrogenase. This mechanism is discussed in relation to the reaction mechanisms of topa-bearing quinoprotein amine oxidases, the flavoprotein monoamine oxidase and the mammalian semicarbazide-sensitive amine oxidase.

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Review on biological degradation of biogenic amines in food

International Journal of Agricultural Science and Food Technology ◽

10.17352/2455-815x.000127 ◽

2021 ◽

pp. 331-334

Author(s):

Zeng Jihao ◽

Wu Jinhong ◽

Chen Huiyun ◽

Ni Sui

Keyword(s):

Hydrogen Peroxide ◽

Biogenic Amines ◽

Biogenic Amine ◽

Amine Oxidase ◽

Short Review ◽

Biological Degradation ◽

Amine Oxidases ◽

Amine Content ◽

Biological Methods

In this paper, the application of biological methods to reduce biogenic amine content in foods was introduced. Biogenic amine oxidase, a special protein that can degrade biogenic amine into acetaldehyde, hydrogen peroxide and ammonia, has been introduced in this paper, and two major amine oxidases and their degradation effects on different biogenic amines were briefly reviewed. In addition, various microorganisms that could produce amine oxidase were summarized in this paper, and their application in the fermentation was shown. This short review summarizes the important biological methods currently used to degrade biogenic amines and provides new theoretical guidance for removing or reducing the biogenic amines in foods.

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Identification of a Lactic Acid Bacteria to Degrade Biogenic Amines in Chinese Rice Wine and Its Enzymatic Mechanism

Foods ◽

10.3390/foods8080312 ◽

2019 ◽

Vol 8 (8) ◽

pp. 312 ◽

Cited By ~ 4

Author(s):

Tianjiao Niu ◽

Xing Li ◽

Yongjie Guo ◽

Ying Ma

Keyword(s):

Biogenic Amines ◽

Amine Oxidase ◽

Fermentation Broth ◽

Optimal Choice ◽

Rice Wine ◽

Amine Oxidases ◽

Chinese Rice Wine ◽

Sephadex Column ◽

Enzymatic Mechanism

A L. plantarum, CAU 3823, which can degrade 40% of biogenic amines (BAs) content in Chinese rice wine (CRW) at the end of post-fermentation, was selected and characterized in this work. It would be an optimal choice to add 106 cfu/mL of selected strain into the fermentation broth to decrease the BAs while keeping the character and quality of CRW. Nine amine oxidases were identified from the strain and separated using Sephadex column followed by LC-MS/MS analysis. The purified amine oxidase mixture showed a high monoamine oxidase activity of 19.8 U/mg, and more than 40% of BAs could be degraded. The biochemical characters of the amine oxidases were also studied. This work seeks to provide a better solution to degrade BAs in CRW prior to keeping the character and quality of CRW and a better understanding of the degradability of the strain to the BAs.

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Oxidative Deamination of Biogenic Amines by Intestinal Amine Oxidases: Histamine is Specifically Inactivated by Diamine Oxidase

Hoppe-Seyler´s Zeitschrift für physiologische Chemie ◽

10.1515/bchm2.1975.356.2.1485 ◽

1975 ◽

Vol 356 (2) ◽

pp. 1485-1496 ◽

Cited By ~ 17

Author(s):

Jürgen Kusche ◽

Wilfried Lorenz ◽

Johanna Schmidt

Keyword(s):

Biogenic Amines ◽

Diamine Oxidase ◽

Amine Oxidases ◽

Oxidative Deamination

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SPERMINE OXIDASE: AN AMINE OXIDASE WITH SPECIFICITY FOR SPERMINE AND SPERMIDINE

Journal of Experimental Medicine ◽

10.1084/jem.97.3.345 ◽

1953 ◽

Vol 97 (3) ◽

pp. 345-355 ◽

Cited By ~ 73

Author(s):

James G. Hirsch

Keyword(s):

Competitive Inhibition ◽

Amine Oxidase ◽

Spermine Oxidase ◽

Amine Oxidases ◽

Oxidative Deamination ◽

Cyanide Ion ◽

Mercuric Ion ◽

Low Concentrations ◽

Rate Of Oxygen Consumption ◽

Buffer Composition

Sheep serum and bovine serum contain an enzyme which brings about a rapid oxidative deamination of certain biological amines. This enzyme differs from previously described amine oxidases in several regards and especially in its substrate specificity. Studies thus far indicate that only spermine and the closely related compound spermidine serve as substrates for the enzyme in sheep serum. For this reason, the enzyme has been named spermine oxidase. Spermine oxidase is active in a variety of fluids of various ionic strength and buffer composition. The reaction takes place between pH 6.0 and pH 8.0 with an optimal rate in the vicinity of neutrality. Under certain conditions, the rate of oxygen consumption during the initial phase of the reaction is independent of the concentration of substrate. The diminution in rate observed during the latter phase of the enzymatic attack appears to be due to an alteration in the kinetics at low concentrations of substrate, or to competitive inhibition by a product of the reaction. Carbonyl reagents almost completely block the action of spermine oxidase, while certain amines and the cyanide ion bring about partial inhibition. Thiol reagents and sequestering compounds do not alter the course of the oxidative process. In the presence of low concentrations of mercuric chloride, the sheep serum-spermine system consumes approximately twice as much oxygen as controls containing no mercuric ion. The mechanism by which the mercuric ion stimulates additional oxygen uptake is obscure.

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