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通过理性设计同型柠檬酸合酶在酿酒酵母中高水平生产赖氨酸。

High-Level Production of Lysine in the Yeast Saccharomyces cerevisiae by Rational Design of Homocitrate Synthase.

机构信息

Division of Biological Science, Graduate School of Science and Technology, Nara Institute of Science and Technology, Ikoma, Nara, Japan.

Department of Biochemistry, Molecular Biology and Biophysics, University of Minnesota, Saint Paul, Minnesota, USA.

出版信息

Appl Environ Microbiol. 2021 Jul 13;87(15):e0060021. doi: 10.1128/AEM.00600-21.

Abstract

Homocitrate synthase (HCS) catalyzes the aldol condensation of 2-oxoglutarate (2-OG) and acetyl coenzyme A (AcCoA) to form homocitrate, which is the first enzyme of the lysine biosynthetic pathway in the yeast Saccharomyces cerevisiae. The HCS activity is tightly regulated via feedback inhibition by the end product lysine. Here, we designed a feedback inhibition-insensitive HCS of S. cerevisiae (ScLys20) for high-level production of lysine in yeast cells. docking of the substrate 2-OG and the inhibitor lysine to ScLys20 predicted that the substitution of serine with glutamate at position 385 would be more suitable for desensitization of the lysine feedback inhibition than the substitution from serine to phenylalanine in the already known Ser385Phe variant. Enzymatic analysis revealed that the Ser385Glu variant is far more insensitive to feedback inhibition than the Ser385Phe variant. We also found that the lysine contents in yeast cells expressing the Ser385Glu variant were 4.62- and 1.47-fold higher than those of cells expressing the wild-type HCS and Ser385Phe variant, respectively, due to the extreme desensitization to feedback inhibition. In this study, we obtained highly feedback inhibition-insensitive HCS using docking and enzymatic analysis. Our results indicate that the rational engineering of HCS for feedback inhibition desensitization by lysine could be useful for constructing new yeast strains with higher lysine productivity. A traditional method for screening toxic analogue-resistant mutants has been established for the breeding of microbes that produce high levels of amino acids, including lysine. However, another efficient strategy is required to further improve their productivity. Homocitrate synthase (HCS) catalyzes the first step of lysine biosynthesis in the yeast Saccharomyces cerevisiae, and its activity is subject to feedback inhibition by lysine. Here, design of a key enzyme that regulates the biosynthesis of lysine was utilized to increase the productivity of lysine. We designed HCS for the high-level production of lysine in yeast cells by docking simulation. The engineered HCS exhibited much less sensitivity to lysine and conferred higher production of lysine than the already known variant obtained by traditional breeding. The combination of design and experimental analysis of a key enzyme will contribute to advances in metabolic engineering for the construction of industrial microorganisms.

摘要

同型柠檬酸合酶(HCS)催化 2-氧代戊二酸(2-OG)和乙酰辅酶 A(AcCoA)的醛缩合反应,形成同型柠檬酸,这是酿酒酵母赖氨酸生物合成途径中的第一个酶。HCS 的活性通过终产物赖氨酸的反馈抑制来严格调节。在这里,我们设计了酿酒酵母的一种对赖氨酸反馈抑制不敏感的 HCS(ScLys20),用于在酵母细胞中高水平生产赖氨酸。通过对接 2-OG 和抑制剂赖氨酸到 ScLys20,预测在位置 385 用谷氨酸替代丝氨酸比在已经知道的 Ser385Phe 变体中用苯丙氨酸替代丝氨酸更适合于赖氨酸反馈抑制的脱敏。酶分析表明,Ser385Glu 变体比 Ser385Phe 变体对反馈抑制的敏感性低得多。我们还发现,表达 Ser385Glu 变体的酵母细胞中的赖氨酸含量分别比表达野生型 HCS 和 Ser385Phe 变体的细胞中的赖氨酸含量高 4.62 倍和 1.47 倍,这是由于对反馈抑制的极端脱敏。在这项研究中,我们通过对接和酶分析获得了对反馈抑制不敏感的高度 HCS。我们的结果表明,通过赖氨酸对 HCS 的合理工程化进行反馈抑制脱敏可能有助于构建具有更高赖氨酸生产能力的新型酵母菌株。传统的筛选有毒类似物抗性突变体的方法已经被用于筛选产生高水平氨基酸的微生物,包括赖氨酸。然而,还需要另一种有效的策略来进一步提高它们的生产力。同型柠檬酸合酶(HCS)催化酿酒酵母中赖氨酸生物合成的第一步,其活性受到赖氨酸的反馈抑制。在这里,我们利用调节赖氨酸生物合成的关键酶的设计来提高赖氨酸的生产力。我们通过对接模拟设计了在酵母细胞中高效生产赖氨酸的 HCS。与传统育种获得的已知变体相比,工程化的 HCS 对赖氨酸的敏感性更低,赖氨酸产量更高。关键酶的设计与实验分析的结合将有助于代谢工程的进展,以构建工业微生物。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ac18/8276798/25e8dceb8284/aem.00600-21-f0001.jpg

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