在Fusobacterium nucleatum中进行梅索-兰西因的生物合成
Amanda Darbyshire1, Robert Mothersole1, Kirsten R Wolthers2
1Department of Chemistry, University of British Columbia, Okanagan Campus, Kelowna, B.C, V1V 1V7, Canada.
Archives of biochemistry and biophysics
|June 17, 2023
概括
这项研究调查了Fusobacterium nucleatum如何合成美索-兰西,这是其甘油层的关键组成部分. 研究人员确定了两种潜在的酶途径,涉及d-cysteine或类似表皮酶的酶,用于 meso-lanthionine 生物合成.
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:
- 口腔病原体fusobacterium nucleatum在它的peptidoglycan交叉链接中使用美索-兰西.
- 氨酸合成酶通常通过氨酸的自我凝结产生l,l-氨酸.
- 在F. nucleatum中,美索-兰因的生物合成在很大程度上仍未被阐明.
研究的目的:
- 探索在F. nucleatum.中形成美索-兰西因的潜在酶机制.
- 研究氨酸合成酶在中氨酸生产中的作用.
- 描述假定表皮酶FN1732.2.的酶活性.
主要方法:
- 使用meso-和l,l-diaminopimelate进行抑制研究,以探测氨酸合成酶活性.
- 对d-氨酸和l-氨酸反应的稳定状态和前稳定状态动态分析.
- 使用二氨基胺酸脱酶进行酶定量测试,以量化FN1732活性.
主要成果:
- 比l,l-diaminopimelate,meso-diaminopimelate 是一种比l,l-diaminopimelate 更强大的兰因合成酶抑制剂,这表明可能涉及d-cysteine.
- 动力学数据表明,d-氨酸与氨酸合成酶中间体的反应比l-氨酸更快.
- 基因产物FN1732有效地将l,l-兰因转化为美索-兰因 (kcat = 0.07 s-1,KM = 1.9 mM).
结论:
- 在F. nucleatum中提出了两种不同的酶机制,用于Meso-lanthionine生物合成.
- 兰氨酸合成酶可以通过涉及d-cysteine的β-替代产生meso-lanthionine.
- 酶FN1732作为一个表皮酶,将l,l-氨酸转化为中氨酸.
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