Polyamine N-acetyltransferase from Fasciola hepatica

Aisien, S.O.; Walter, Rolf D.

doi:10.1016/0166-6851(92)90201-t

Cited by 9 publications

(15 citation statements)

References 14 publications

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“…The occurrence of Nacetylated polyamines has also been reported in helminths; N 1-and NS-acetylspermidine have been identified in the trematodes Fasciola hepatica and Paragonimus uterobilateralis as well as in the spent media of maintained flukes (Aisien and Walter 1992;unpublished data). NAcetylputrescine and its excretion have also been described in the parasitic nematodes Onchocerca volvulus and Ascaris suum Walter 1989, 1990).…”

Section: Discussionmentioning

confidence: 99%

“…Various N-acetyltransferases have also been found in helminths Walter 1989, 1990;Aisien and Walter 1992;Davids et al 1994), whereas in protozoa only the presence of polyamine NS-acetyltransferase in Acanthamoeba culbertsoni has been reported (Shukla et al 1996). In this manuscript we describe the activity of N-acetyltransferase that shows a preference for the acetylation of spermidine at the N l-pOsitiOn and is proposed to be responsible for the occurrence of N ~-acetylspermidine in L. amazonensis (Rojas-Chaves et al 1996).…”

Section: Introductionmentioning

confidence: 99%

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Polyamine N-acetyltransferase in Leishmania amazonensis

1996

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N-Acetyltransferase, which is suggested to be responsible for the production of N1-acetylspermidine in Leishmania amazonensis and to be involved in the process of inactivation and degradation of excessive polyamines, was partially purified and characterized. Among the substrates tested, sym-norspermidine, sym-norspermine, and 1,3-diaminopropane had the highest reaction rates, but the naturally occurring polyamines spermine and spermidine were also acetylated at considerable rates, whereas putrescine was a poor substrate. The Michaelis constants (Km values) for spermine and spermidine were 0.66 and 3.3 mM, respectively. The Km value for acetylcoenzyme A (acetyl-CoA) was determined to be 34 microM. CoA inhibited the reaction in a competitive manner; the inhibition constant was 5 microM. The enzyme showed an apparent relative molecular mass of 35,000.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Polyamine N-acetyltransferase in Leishmania amazonensis

1996

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“…The cytosolic enzyme, in contrast, is totally inactive toward putrescine (Della Ragione and Pegg 1983). The ability to acetylate putrescine has also been found to be a feature of the polyamine N-acetyltransferase from the liver fluke Fasciola hepatica, which acetylates spermidine at the N 1 -and N 8 -positions at similar rates (Aisien and Walter 1992;unpublished data). Although the Acanthamoeba polyamine N-acetyltransferase shares certain properties of the liver nuclear N-acetyltransferases, differences exist in the molecular sizes of their proteins.…”

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confidence: 96%

“…The overall purification factor was only 16 orders of magnitude and the yield was about 5%. The assay for the polyamine N-acetyltransferase, the isolation of acetylated polyamines, and the counting of radioactivity were done as previously described (Aisien and Walter 1992). The standard incubation mixture of 100 µl contained 1 mM spermidine if not stated otherwise, 50 mM TRIS-HCl buffer (pH 9), 4.2 µM (25 nCi, 60 mCi mmol −1 ), [1-14 C]-acetylcoenzyme A (acetyl-CoA), 0.1 mM DTT, 0.1 mM EDTA, and an appropriate amount of the partially purified enzyme.…”

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confidence: 99%

“…The reaction was terminated by the addition of perchloric acid. Precipitated proteins were removed and the supernatants were dansylated, partially purified on silica gel (Seiler et al 1978), and analyzed as previously reported (Aisien and Walter 1992). Separation 271 of the dansyl chloride derivatives was performed on a microbore Spherisorb 5 µm ODS II (2×250 mm, Knauer, Berlin) at a flow rate of 0.45 ml min −1 .…”

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Identification of the polyamine N 8 -acetyltransferase involved in the pathway of 1,3-diaminopropane production in Acanthamoeba culbertsoni

Shukla

Aisien

Bergmann

et al. 1996

Parasitology Research

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A cytosolic polyamine N-acetyltransferase that preferentially catalyzes the acetylation of spermidine in the N8-position was identified in the free-living pathogenic amoeba Acanthamoeba culbertsoni. In addition to spermidine, the enzyme also catalyzed the acetylation of spermine and putrescine with Michaelis constants (Km values) of 97, 12, and 10 microM, respectively. The Km value for acetylcoenzyme A (acetyl-CoA) was estimated to be 11 microM, whereas CoA had an inhibitory constant of 6 microM. The N-acetylase has a molecular mass of approximately 45 kDa. That the enzyme preferentially catalyzed the acetylation of spermidine at the N8-position, resulting in N8-acetylspermidine, the preferred substrate of the polyamine oxidase found in A. culbertsoni, indicates a role for the enzyme in the production of 1,3-diaminopropane, the major polyamine found in the Acanthamoeba.

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Characterization of the arylalkylamine N -acetyltransferase in Onchocerca volvulus

Aisien

Hellmund

Walter

1996

Parasitology Research

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The characteristics and kinetic properties of an arylalkylamine N-acetyltransferase were studied in partially purified preparations of the human filarial parasite Onchocerca volvulus. The enzyme, which had a relative molecular mass (M(r)) of 37-38 kDa, catalyzed the acetylation of arylalkylamines but did not accept arylamines or polyamines as substrates. The optimal pH for enzyme activity was found to be 8.5 in TRIS-HCI. The apparent Michaelis constant (K(m)) and maximum velocity (Vmax) determined from Lineweaver-Burk plots for tryptamine were 1.8 microM and 29 nmol min-1 mg protein-1, respectively. Except for the catecholamines, the other arylalkylamines such as 5-hydroxytryptamine (5-HT), tyramine, and octopamine similarly exhibited high affinities and reaction rates. Whereas the enzyme is inhibited by metals and p-chloro-mercuribenzoate, it is inactivated neither by amethopterin nor by cystamine and is thereby distinguished from the mammalian arylamine N-acetyltransferase. Like other N-acetyltransferases whose function is the regulation of intracellular amine levels, the enzyme may have a role in the inactivation of excess biogenic amine in this parasite.

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Polyamine N-acetyltransferase from Fasciola hepatica

Cited by 9 publications

References 14 publications

Polyamine N-acetyltransferase in Leishmania amazonensis

Polyamine N-acetyltransferase in Leishmania amazonensis

Identification of the polyamine N 8 -acetyltransferase involved in the pathway of 1,3-diaminopropane production in Acanthamoeba culbertsoni

Characterization of the arylalkylamine N -acetyltransferase in Onchocerca volvulus

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