Biosynthesis of long-chain polyamines by crenarchaeal polyamine synthases from Hyperthermus butylicus and Pyrobaculum aerophilum
Biosynthesis of long-chain polyamines by crenarchaeal polyamine synthases from Hyperthermus butylicus and Pyrobaculum aerophilum
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DOI：
10.1016/j.febslet.2009.10.014
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发表时间：
2009-11-03
期刊：
影响因子：
3.5
通讯作者：
Knott, Juergen Manfred
中科院分区：
文献类型：
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作者：
Knott, Juergen Manfred
多胺普遍存在于所有生物体中。除了常见的多胺外，嗜热古菌还能合成长链多胺。本研究克隆了来自丁酸热菌和嗜气热菌的多胺合成酶，并分析了它们的底物特异性。来自H. butylicus的多胺合成酶HbSpeE II合成了高活性的长链多胺，其机制与广泛的生物体合成普通多胺的机制相同，其中氨基丙基残基来自脱羧的s -腺苷蛋氨酸。这是第一个合成比毒鼠胺长且活性高的多胺合成酶。(C) 2009年欧洲生化学会联合会。Elsevier b.v.版权所有。
Polyamines are ubiquitously present in all organisms. In addition to the common polyamines, thermophilic archaea synthesize long-chain polyamines. In the present study polyamine synthases from Hyperthermus butylicus and Pyrobaculum aerophilum were cloned and their substrate specificity was analyzed. The polyamine synthase HbSpeE II from H. butylicus synthesized long-chain polyamines with high activity using the same mechanism that is used by a wide range of organisms to synthesize common polyamines, in which the aminopropyl residue derives from decarboxylated S-adenosylmethionine. This is the first polyamine synthase described that synthesizes a polyamine longer than a tetramine with high activity. (C) 2009 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.