Investigation of Indigoidine Synthetase Reveals Conserved Active Site Base Residue of Nonribosomal Peptide Synthetase Oxidases,Journal of the American Chemical Society

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Investigation of Indigoidine Synthetase Reveals Conserved Active Site Base Residue of Nonribosomal Peptide Synthetase Oxidases
Journal of the American Chemical Society ( IF 14.4 ) Pub Date : 2020-06-08 , DOI: 10.1021/jacs.0c04328
Bo Pang _{1,

2,

3} , Yan Chen _{2,

3} , Fei Gan _{1,

2,

3} , Chunsheng Yan ₂ , Liyuan Jin ₂ , Jennifer W Gin _{2,

3} , Christopher J Petzold _{2,

3} , Jay D Keasling _{1,

2,

3,

4,

5,

6}

Affiliation

Nonribosomal peptide synthetase (NRPS) oxidase (Ox) domains oxidize protein-bound intermediates to install crucial structural motifs in bioactive natural products. The mechanism of this domain remains elusive. Here, by studying indigoidine synthetase, a single-module NRPS involved in the biosynthesis of indigoidine and several other bacterial secondary metabolites, we demonstrate that its Ox domain utilizes an active site base residue, tyrosine 665, to deprotonate protein-bound L-glutaminyl residue. We further validate the generality of this active site residue among NRPS Ox domains. These findings not only resolve the biosynthetic pathway mediated by indigoidine synthetase but enable mechanistic insight into NRPS Ox domains.

中文翻译：

靛蓝合成酶的研究揭示了非核糖体肽合成酶氧化酶的保守活性位点碱基残基

非核糖体肽合成酶 (NRPS) 氧化酶 (Ox) 域氧化蛋白质结合的中间体，以在生物活性天然产物中安装关键的结构基序。该域的机制仍然难以捉摸。在这里，通过研究靛蓝合成酶，一种参与靛蓝和其他几种细菌次级代谢物生物合成的单模块 NRPS，我们证明其 Ox 结构域利用活性位点碱基残基酪氨酸 665 去质子化蛋白质结合的 L-谷氨酰胺残基. 我们进一步验证了这个活性位点残基在 NRPS Ox 域中的普遍性。这些发现不仅解决了由靛蓝合成酶介导的生物合成途径，而且使人们能够深入了解 NRPS Ox 结构域。

更新日期：2020-06-08

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