在Bacillus subtilis中以前未被识别的kanosamine生物合成途径
Natasha D Vetter1, David M Langill, Shazia Anjum
1Department of Chemistry, University of Saskatchewan, 110 Science Place, Saskatoon, SK, Canada, S7N 5C9.
Journal of the American Chemical Society
|April 17, 2013
概括
细菌细菌酶NtdA,NtdB和NtdC从葡萄糖-6-酸盐中合成诺胺. 这一发现揭示了一种新的抗生素生物合成途径,与以前已知的途径不同.
科学领域:
- 微生物学 微生物学
- 生物化学 生物化学
- 酶学 是一种酶学.
背景情况:
- 细菌细菌中的ntd操作子对于合成3,3'-neotrehalosadiamine (NTD),一种具有抗生素特性的分糖胺至关重要.
- 在这种操作子中,NtdA,NtdB和NtdC酶的特定功能在体外以前没有被描述.
研究的目的:
- 阐明从细菌细菌中获得的NtdA,NtdB和NtdC的体外酶功能.
- 描述Bacillus subtilis中可诺山胺生物合成的新途径.
主要方法:
- 进行了酶定量测试,以确定纯化的NtdA,NtdB和NtdC的催化活性.
- 分析了基质特异性和反应产物,以确定生物化学途径.
主要成果:
- NtdC被确定为一种葡萄糖-6-酸盐3-脱酶.
- NtdA作为一种依赖于皮里多克萨尔酸盐的3-oxo-glucose-6-phosphate:glutamate氨基转移酶而起作用.
- NtdB 作为一种可诺山胺-6-酸盐酸酶,从葡萄糖-6-酸盐完成可诺山胺生物合成途径.
结论:
- 这项研究表明,Bacillus subtilis中可诺山胺生物合成的新型酶途径,由NtdA,NtdB和NtdC催化.
- 这一途径代表了与UDP-葡萄糖依赖途径相比,可诺山胺生产的替代途径,这种途径在Amycolatopsis mediterranei中发现.
- 这些发现为不寻常的糖的生物合成提供了新的见解,这些糖具有潜在的抗生素应用.
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