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

Shukla, O. P.; Aisien, S.O.; Bergmann, Bärbel; Hellmund, Claudia; Walter, Rolf D.

doi:10.1007/s004360050110

Cited by 4 publications

(1 citation statement)

References 13 publications

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“…However, spermidine oxidation by a plant-like polyamine oxidase [37] could produce aminobutyraldehyde and 1,3-diaminopropane as catabolic products. The Acanthamoeba culbertsoni polyamine oxidase acts on N 8 -acetylspermidine to produce large quantities of 1,3-diaminopropane in this organism [38] and if equivalent activity is present in diatoms, the 1,3-diaminopropane could serve as the initial substrate for the AdoMetDC/thermospermine synthase-like fusion proteins. A co-product of aminopropyltransferases is methylthioadenosine (MTA), a potent inhibitor of methyltransferases and aminopropyltransferases.…”

Section: Precursors and Co-productsmentioning

confidence: 99%

Molecular machines encoded by bacterially-derived multi-domain gene fusions that potentially synthesize,N-methylate and transfer long chain polyamines in diatoms

Michael¹

2011

FEBS Letters

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a b s t r a c tSilica glass formation in diatoms requires the biosynthesis of unusual, very long chain polyamines (LCPA) composed of iterated aminopropyl units. Diatoms processively synthesize LCPA, N-methylate the amine groups and transfer concatenated, N-dimethylated aminopropyl groups to silaffin proteins. Here I show that diatom genomes possess signal peptide-containing gene fusions of bacterially-derived polyamine biosynthetic enzymes S-adenosylmethionine decarboxylase (AdoMetDC) and an aminopropyltransferase, sometimes fused to a eukaryotic histone N-methyltransferase domain, that potentially synthesize and N-methylate LCPA. Fusions of similar, alternatively configured domains but with a catalytically dead AdoMetDC and in one case a Tudor domain, may N-dimethylate and transfer multiple aminopropyl unit polyamines onto silaffin proteins.

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Section: Precursors and Co-productsmentioning

confidence: 99%

Molecular machines encoded by bacterially-derived multi-domain gene fusions that potentially synthesize,N-methylate and transfer long chain polyamines in diatoms

Michael¹

2011

FEBS Letters

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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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Polyamines biosynthesis and oxidation in free-living amoebae

et al. 2004

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In this paper we describe the polyamine biosynthesis and oxidation processes, giving an overview about recent results in free-living Amoebae. The protozoa polyamine levels are different in comparison with mammalian cells. Also, the polyamine levels in protozoa cells change if these species are pathological or not for the human beings. All the amoeba strains show high concentrations of 1,3-diaminopropane (DAP), spermidine and acetylspermidine while spermine is absent. In these amoeba a considerable polyamine oxidase activity has been found, which acts on N8-acetylspermidine, but not on free polyamines. This enzyme is responsible, together with polyamine acetylase, of DAP synthesis whose function is not well known.

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

Cited by 4 publications

References 13 publications

Molecular machines encoded by bacterially-derived multi-domain gene fusions that potentially synthesize,N-methylate and transfer long chain polyamines in diatoms

Molecular machines encoded by bacterially-derived multi-domain gene fusions that potentially synthesize,N-methylate and transfer long chain polyamines in diatoms

Polyamine N-acetyltransferase in Leishmania amazonensis

Polyamines biosynthesis and oxidation in free-living amoebae

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