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放线菌中pppApp合成活性的出现及嘌呤核苷酸焦磷酸转移酶的分离。

Occurrence of pppApp-synthesizing activity in actinomycetes and isolation of purine nucleotide pyrophosphotransferase.

作者信息

Oki T, Yoshimoto A, Ogasawara T, Sato S, Takamatsu A

出版信息

Arch Microbiol. 1976 Mar 19;107(2):183-7. doi: 10.1007/BF00446837.

DOI:10.1007/BF00446837
PMID:1259517
Abstract

The occurrence of adenosine 5'-triphosphate-3'diphosphate-synthesizing activity was detected in five strains of actinomycetes; Streptomyces morookaensis, Streptomyces aspergilloides, Streptomyces hachijoensis, tactinomyces violascens and Streptoverticillium septatum, out of 825 strains of actinomycetes, bacteria, fungi and fungi imperficti. Purine nucleotide pyrophosphotransferase were extracellularly excreted associating with the cell growth, and were purified partially or to apparent homogeneiety from the culture filtrate. The enzymes are a monomeric protein with molecular weight of 18,000-26,000 and synthesize adenosine, guanosine and inosine 5'-phosphate (mono, di or tri)-3'-diphosphate such as pApp, ppA pp, pppApp, pGpp, ppGpp, pppGpp, and pppIpp by transferring a pyrophosphoryl group from the 5'-position of ATP, dATP and ppApp to the 3'-position of purine nucleotides in the presence of a divalent cation and in alkaline state.

摘要

在825株放线菌、细菌、真菌和半知菌中,检测到五株放线菌(室伏链霉菌、曲霉状链霉菌、八丈岛链霉菌、紫色放线菌和横隔链霉菌)具有腺苷5'-三磷酸-3'-二磷酸合成活性。嘌呤核苷酸焦磷酸转移酶在细胞生长过程中分泌到细胞外,并从培养滤液中部分纯化或纯化至表观均一。这些酶是分子量为18,000 - 26,000的单体蛋白,在二价阳离子存在且呈碱性的状态下,通过将焦磷酸基团从ATP、dATP和ppApp的5'-位转移至嘌呤核苷酸的3'-位,合成腺苷、鸟苷和肌苷5'-磷酸(单、二或三)-3'-二磷酸,如pApp、ppA pp、pppApp、pGpp、ppGpp、pppGpp和pppIpp。

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Arch Microbiol. 1976 Mar 19;107(2):183-7. doi: 10.1007/BF00446837.
2
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J Biol Chem. 1983 Feb 10;258(3):1678-83.

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本文引用的文献

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High-Resolution Density Gradient Sedimentation Analysis.高分辨率密度梯度沉降分析。
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