Phosphopyridoxal complexes with histamine and histidine (3) the influence of presumed complex on activity of rat intestinal histaminase

Sasiak, K.; Kierska, D.; Bogusławski, M.; Maśliński, Cz.

doi:10.1007/bf02027154

Cited by 8 publications

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References 15 publications

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“…The inhibition of pig kidney DAO by high have been reported [5]. These experiments suggest that the inhibition of enzyme activity by u high concentrations of Hi was caused by a deficit t~.…”

Section: The Influence Of Excess Hi On Pig Kidney Dao and Rat Intementioning

confidence: 69%

“…The PLP content was determined according to WADA and SNELL [121. The rate of cyclic compound formation measured with isotopes was carried out in 0.1 M phosphate buffer, pH 7.5, in the presence of enzyme preparations described elsewhere [5]. The rate of cyclic compound formation measured with isotopes was carried out in 0.1 M phosphate buffer, pH 7.5, in the presence of enzyme preparations described elsewhere [5].…”

Section: Methodsmentioning

confidence: 99%

“…A Lineweaver-Burk plot of rat intestinal Hi-ase [5], as well as pig kidney DAO, presents a mixed type of inhibition (Fig. A Lineweaver-Burk plot of rat intestinal Hi-ase [5], as well as pig kidney DAO, presents a mixed type of inhibition (Fig.…”

Section: The Influence Of Excess Hi On Pig Kidney Dao and Rat Intementioning

confidence: 99%

“…It was of interest to examine the dynamics of cyclic compound formation in the presence of both enzymes and at an excess of Hi and PLP. The dynamics of cyclic compound formation was calculated as a percentage of the total radioactivity of ~4C-Hi bound into a spot of cyclic product [5] and as a percentage of PLP which disappeared from the incubation mixture. During incubation at 37~ the azomethine peak gradually decreased and a new maximum appeared at 330 nm; this indicates that during incubation the azomethine was transformed into a new cyclic product [1,2].…”

Section: Ill Dynamics Of Cyclic Compound Formation In the Presence Ofmentioning

confidence: 99%

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Phosphopyridoxal complexes with histamine and histidine (5) the kinetics of cyclic compound formation between histamine and pyridoxal-5′-phosphate in the presence of pig kidney diamine oxidase and rat intestinal histaminase

1977

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Pig kidney diamine oxidase (DAO) and rat intestinal histaminase (Hi-ase) activities are inhibited in vitro by high concentrations of both a substrate (histamine) and a coenzyme (pyridoxal-5'-phosphate). This inhibition may be at least partially associated with the formation of a cyclic compound between histamine (Hi) and pyridoxal-5'-phosphate (PLP). The dynamics of this cyclic compound formation in the presence of both enzymes has been examined. In an incubation mixture containing partially purified pig kidney DAO, the rate of cyclization decreased slightly as compared with a buffer. On the contrary, in the presence of crude rat intestinal histaminase, the rate of cyclization was inhibited significantly; this inhibition was proportional to the amount of enzyme preparation present in the incubation mixture. The possible mechanism of the influence of enzyme protein on the rate of cyclic compound formation, and its possible biological significance, are discussed.

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Section: The Influence Of Excess Hi On Pig Kidney Dao and Rat Intementioning

confidence: 69%

Section: Methodsmentioning

confidence: 99%

Section: The Influence Of Excess Hi On Pig Kidney Dao and Rat Intementioning

confidence: 99%

Section: Ill Dynamics Of Cyclic Compound Formation In the Presence Ofmentioning

confidence: 99%

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Phosphopyridoxal complexes with histamine and histidine (5) the kinetics of cyclic compound formation between histamine and pyridoxal-5′-phosphate in the presence of pig kidney diamine oxidase and rat intestinal histaminase

1977

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The amino compounds are able to react irreversibly with pyridoxal, pyridoxal-5-phosphate (PLP) or PLP-dependent enzymes. Previously, the possibility of the cyclic product formation was examined in the presence of crude histidine decarboxylase and histaminase preparations [3,4]. Previously, the possibility of the cyclic product formation was examined in the presence of crude histidine decarboxylase and histaminase preparations [3,4].

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mentioning

confidence: 99%

The kinetics of complex formation between histidine and pyridoxal-5-phosphate in the presence of bacterial histidine decarboxylase

Kierska

Maśliński

1975

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The dynamics of the complex formation between pyridoxal 5'-phosphate (PLP) and histidine in the presence of bacterial histidine deearboxylase was examined. Since PLP is able to form a cyclic product with histidine and histamine, the possibility of complex formation between PLP and histamine formed during a deearboxylation reaction was examined too. It was found that the cyclization reaction between PLP and histidine is equimolecular and the rate of cyclic product formation is not significantly influenced by the presence of enzyme. In the presence of bacterial histidine deearboxylase both the cyelization reaction and cyclic product formation were observed. Predominance of histamine or cyclic product formation was dependent on pH and substrate concentration. In the presence of histidine and enzymatic protein, histamine formed during the deearboxylation reaction was unable to form a cyclic product with PLP.Metabolism and catabolism of amines and/ or amino acids largely depends on PLP-enzymes. In these reactions Schiff's bases are formed between amino compound and pyridoxal, pyridoxal Y-phosphate (PLP) or PLP-enzymes. On the other hand it is known that under certain conditions Schiff's bases may be transformed into stable cyclic condensation products [1][2][3][4]. During studies on activity of different enzymes such as pyridoxal kinase [5], amino acid decarboxylase [6], aminotransferase [7] and histaminase [8], the possibility of complex compounds formation between substrates and PLP has been shown. On the basis of these investigations it was suggested that the formation of PLPcomplexes during an enzymatic reaction may lead to the inhibition of metabolic processes. It also has been found that an excess of substrate [9][10][11][12] or coenzyme [13, 14] may lead to a decrease in enzyme activity. Binding of PLP with a part of substrate and/or product into cyclic compound could apparently decrease enzyme activity. Therefore it should be expected that the formation of complex compound results in substrate or PLP deficiency and consequently can lead to a decrease of the PLP-dependent enzyme activity.The purpose of our investigations was to establish the dynamics of cyclic product formation between histidine (substrate) and PLP in the presence of bacterial histidine deearboxylase as well as to examine a possibility of formation of a cyclic compound between PLP and liistamine produced during decarboxylation reaction. MethodsThe reaction between histidine (His) and PLP was carried out at: pH 5.0 (close to the optimum pH for the bacterial histidine decarboxylase activity) [15], pH 6.2 and pH 7.4 (optimal for complex formation) [16].Substrate concentrations from 10 -5 M to 10-~ M were used. Two kinds of experiments were performed: (1) Reaction of His with PLP in equimolecular ratio (1 : 1) in phosphate buffer; (2) reaction of His with PLP in ratio 1 : 1 in the presence of bacterial histidine decarboxylase from Clostridium Welchii. The mixture of His and PLP in phosphate buffer, and in the presence of enzyme, was incubat...

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Conditions for the formation of cyclic compounds between pyridoxal phosphate and 5-hydroxytryptamine or 5-hydroxytryptophan

1978

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5-Hydroxytryptamine (5HT) and 5-hydroxytryptophan (5HTP) form cyclic compounds (probably of the tetrahydro-beta-carboline type) with pyridoxal phosphate (PLP). In the first step of reaction a Schiff's base is formed; during incubation it is transformed into a cyclic compound with a maximum absorption spectrum at 330 nm. The degree of cyclization depends on pH and substrate concentrations. One mole of 5HT or 5HTP reacts with one mole of coenzyme. The velocity of cyclization increased with an excess of either 5HT (5HTP) or PLP, without any change in the mole to mole ratio. The formation of cyclic compounds was confirmed by the use of isotopes, separation from substrates being achieved by high-voltage electrophoresis.

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Phosphopyridoxal complexes with histamine and histidine (3) the influence of presumed complex on activity of rat intestinal histaminase

Cited by 8 publications

References 15 publications

Phosphopyridoxal complexes with histamine and histidine (5) the kinetics of cyclic compound formation between histamine and pyridoxal-5′-phosphate in the presence of pig kidney diamine oxidase and rat intestinal histaminase

Phosphopyridoxal complexes with histamine and histidine (5) the kinetics of cyclic compound formation between histamine and pyridoxal-5′-phosphate in the presence of pig kidney diamine oxidase and rat intestinal histaminase

The kinetics of complex formation between histidine and pyridoxal-5-phosphate in the presence of bacterial histidine decarboxylase

Conditions for the formation of cyclic compounds between pyridoxal phosphate and 5-hydroxytryptamine or 5-hydroxytryptophan

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