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能够合成精胺的醋杆菌中对鸟苷三磷酸不敏感的鸟氨酸脱羧酶。

GTP-insensitive ornithine decarboxylase in acetobacteria able to synthesize spermine.

作者信息

Paulin L, Vehmaanperä J, Nykänen I, Pösö H

出版信息

Biochem Biophys Res Commun. 1983 Jul 29;114(2):779-84. doi: 10.1016/0006-291x(83)90849-5.

Abstract

Several Acetobacteria contained large amounts of spermine in addition to the putrescine and spermidine, which are the polyamines normally found in prokaryotes. A spermine synthase present in cell extracts of these Acetobacteria is the first example of this enzyme in prokaryotes. Dicyclohexylammonium sulphate inhibited both spermidine synthase and spermine synthase activities in Acetobacteria. Their ornithine decarboxylase was not stimulated by GTP nor inhibited by ppGpp and pppGpp (magic spots I and II) in contrast to ornithine decarboxylase of nearly all bacteria studied so far. However, their S-adenosyl-L-methionine decarboxylase resembled other prokaryotic adenosylmethionine decarboxylases in requiring Mg2+ ions in vitro for full activity.

摘要

几种醋杆菌除了含有腐胺和亚精胺(这是原核生物中常见的多胺)外,还含有大量的精胺。这些醋杆菌细胞提取物中存在的精胺合酶是原核生物中该酶的首个实例。硫酸二环己基铵抑制醋杆菌中亚精胺合酶和精胺合酶的活性。与迄今为止研究的几乎所有细菌的鸟氨酸脱羧酶不同,它们的鸟氨酸脱羧酶不受GTP刺激,也不受ppGpp和pppGpp(魔斑I和II)抑制。然而,它们的S-腺苷-L-甲硫氨酸脱羧酶在体外需要Mg2+离子才能完全发挥活性,这一点与其他原核生物的腺苷甲硫氨酸脱羧酶相似。

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