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丙酮酸甲酸裂解酶使大肠杆菌能够在乙酸盐和甲酸盐上高效生长。

Pyruvate Formate-Lyase Enables Efficient Growth of Escherichia coli on Acetate and Formate.

作者信息

Zelcbuch Lior, Lindner Steffen N, Zegman Yonatan, Vainberg Slutskin Ilya, Antonovsky Niv, Gleizer Shmuel, Milo Ron, Bar-Even Arren

机构信息

Department of Plant and Environmental Sciences, Weizmann Institute of Science , Rehovot 76100, Israel.

Max Planck Institute of Molecular Plant Physiology , Am Mühlenberg 1, 14476 Potsdam-Golm, Germany.

出版信息

Biochemistry. 2016 May 3;55(17):2423-6. doi: 10.1021/acs.biochem.6b00184. Epub 2016 Apr 21.

Abstract

Pyruvate formate-lyase (PFL) is a ubiquitous enzyme that supports increased ATP yield during sugar fermentation. While the PFL reaction is known to be reversible in vitro, the ability of PFL to support microbial growth by condensing acetyl-CoA and formate in vivo has never been directly tested. Here, we employ Escherichia coli mutant strains that cannot assimilate acetate via the glyoxylate shunt and use carbon labeling experiments to unequivocally demonstrate PFL-dependent co-assimilation of acetate and formate. Moreover, PFL-dependent growth is faster than growth on acetate using the glyoxylate shunt. Hence, growth via the reverse activity of PFL could have substantial ecological and biotechnological significance.

摘要

丙酮酸甲酸裂解酶(PFL)是一种普遍存在的酶,可在糖发酵过程中提高ATP产量。虽然已知PFL反应在体外是可逆的,但PFL在体内通过缩合乙酰辅酶A和甲酸来支持微生物生长的能力从未得到直接验证。在此,我们使用无法通过乙醛酸循环途径同化乙酸盐的大肠杆菌突变菌株,并通过碳标记实验明确证明了PFL依赖的乙酸盐和甲酸盐的共同化作用。此外,依赖PFL的生长比使用乙醛酸循环途径利用乙酸盐的生长更快。因此,通过PFL的逆向活性进行生长可能具有重大的生态和生物技术意义。

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