分枝杆菌素合成酶活性参数的标准化

Standardization of parameters for the mycobacillin synthetase activity.

作者信息

Mukhopadhyay N K, Majumder S, Ghosh S K, Bhattacharya D, Bose S K

出版信息

Folia Microbiol (Praha). 1984;29(4):295-300. doi: 10.1007/BF02875960.

Abstract

An effective method of preparation involving sonication was developed for cell-free mycobacillin synthetase from Bacillus subtilis. The enzyme showed optimum activity at a buffer concentration of 50 mM (Tris-HCl) and pH 7.5. ATP and Mg2+ which were essential for synthesis showed an optimum requirement at a ratio of 1:1. The synthetase was markedly inhibited by ADP whereas AMP was without any effect. ATP or ATP-generating system could not be replaced by GTP, UTP or CTP. Co2+ and Mn2+ could to some extent substitute Mg2+. Mercapto reagents inhibited the antibiotic synthesis. Exogenous addition of pantothenic acid had no effect.

摘要

开发了一种有效的制备方法，该方法涉及超声处理，用于从枯草芽孢杆菌中制备无细胞分枝杆菌素合成酶。该酶在50 mM（Tris-HCl）缓冲液浓度和pH 7.5时表现出最佳活性。合成所必需的ATP和Mg2+在1:1的比例下显示出最佳需求。ADP对合成酶有明显抑制作用，而AMP则没有任何影响。GTP、UTP或CTP不能替代ATP或ATP生成系统。Co2+和Mn2+在一定程度上可以替代Mg2+。巯基试剂抑制抗生素合成。外源添加泛酸没有效果。