代谢途径
固碳
同化(音韵学)
酶
背景(考古学)
生物化学
碳纤维
计算生物学
化学
生物
计算机科学
光合作用
古生物学
哲学
复合数
语言学
算法
作者
Justin B. Siegel,Amanda Lee Smith,Sean Poust,Adam J. Wargacki,Arren Bar‐Even,Catherine Louw,Betty Shen,Christopher B. Eiben,Huu M. Tran,Elad Noor,Jasmine L. Gallaher,Jacob B. Bale,Yasuo Yoshikuni,Michael H. Gelb,Jay D. Keasling,Barry Stoddard,Mary E. Lidstrom,David Baker
标识
DOI:10.1073/pnas.1500545112
摘要
Significance This paper describes the development of a computationally designed enzyme that is the cornerstone of a novel metabolic pathway. This enzyme, formolase, performs a carboligation reaction, directly fixing one-carbon units into three-carbon units that feed into central metabolism. By combining formolase with several naturally occurring enzymes, we created a new carbon fixation pathway, the formolase pathway, which assimilates one-carbon units via formate. Unlike native carbon fixation pathways, this pathway is linear, not oxygen sensitive, and consists of a small number of thermodynamically favorable steps. We demonstrate in vitro pathway function as a proof of principle of how protein design in a pathway context can lead to new efficient metabolic pathways.
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