...
首页> 外文期刊>Journal of bacteriology >Heterologous expression of the bchM gene product from Rhodobacter capsulatus and demonstration that it encodes S-adenosyl-L-methionine:Mg-protoporphyrin IX methyltransferase.
【24h】

Heterologous expression of the bchM gene product from Rhodobacter capsulatus and demonstration that it encodes S-adenosyl-L-methionine:Mg-protoporphyrin IX methyltransferase.

机译:荚膜红细菌bchM基因产物的异源表达,并证明其编码S-腺苷-L-蛋氨酸:Mg-原卟啉IX甲基转移酶。

获取原文
   

获取外文期刊封面封底 >>

       

摘要

The bacteriochlorophyll biosynthesis gene, bchM, from Rhodobacter capsulatus was previously believed to code for a polypeptide involved in formation of the cyclopentone ring of protochlorophyllide from Mg-protoporphyrin IX monomethyl ester. In this study, R. capsulatus bchM was expressed in Escherichia coli and the gene product was subsequently demonstrated by enzymatic analysis to catalyze methylation of Mg-protoporphyrin IX to form Mg-protoporphyrin IX monomethyl ester. Activity required the substrates Mg-protoporphyrin IX and S-adenosyl-L-methionine. 14C-labeled product was formed in incubations containing 14C-methyl-labeled S-adenosyl-L-methionine. On the basis of these and previous results, we also conclude that the bchH gene, which was previously reported to code for Mg-protoporphyrin IX methyltransferase, is most likely involved in the Mg chelation step.
机译:以前认为来自荚膜红细菌的细菌叶绿素生物合成基因bchM编码一种多肽,该多肽参与了由Mg-原卟啉IX单甲酯形成原叶绿素环戊酮环的过程。在这项研究中,荚膜红衣菌bchM在大肠杆菌中表达,随后通过酶促分析证明基因产物催化Mg-原卟啉IX甲基化形成Mg-原卟啉IX单甲基酯。活性需要底物Mg-原卟啉IX和S-腺苷-L-蛋氨酸。在含有14C-甲基标记的S-腺苷-L-蛋氨酸的培养液中形成14C标记的产物。根据这些结果和先前的结果,我们还得出结论,以前据报道编码Mg-原卟啉IX甲基转移酶的bchH基因很可能参与了Mg螯合步骤。

著录项

相似文献

  • 外文文献
  • 中文文献
  • 专利
获取原文

客服邮箱:kefu@zhangqiaokeyan.com

京公网安备:11010802029741号 ICP备案号:京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有
  • 客服微信

  • 服务号