Federal Research Center «Pushchino Scientific Center for Biological Research of the Russian Academy of Sciences», G.K. Skryabin Institute of Biochemistry and Physiology of Microorganisms of the Russian Academy of Sciences, Pushchino, Russian Federation.
FEMS Microbiol Lett. 2020 Jan 15;367(24). doi: 10.1093/femsle/fnaa207.
The biochemical routes for assimilation of one-carbon compounds in bacteria require many clarifications. In this study, the role of malyl-CoA lyase in the metabolism of the aerobic type I methanotroph Methylotuvimicrobium alcaliphilum 20Z has been investigated by gene inactivation and biochemical studies. The functionality of the enzyme has been confirmed by heterologous expression in Escherichia coli. The mutant strain lacking Mcl activity demonstrated the phenotype of glycine auxotrophy. The genes encoding malyl-CoA lyase are present in the genomes of all methanotrophs, except for representatives of the phylum Verrucomicrobium. We suppose that malyl-CoA lyase is the enzyme that provides glyoxylate and glycine synthesis in the type I methanotrophs supporting carbon assimilation via the serine cycle in addition to the major ribulose monophosphate cycle.
细菌中一碳化合物同化的生化途径需要许多澄清。在这项研究中，通过基因失活和生化研究，研究了丙二酰辅酶 A 裂解酶在需氧 I 型甲烷营养菌 Methylotuvimicrobium alcaliphilum 20Z 代谢中的作用。该酶的功能已通过在大肠杆菌中的异源表达得到证实。缺乏 Mcl 活性的突变株表现出甘氨酸营养缺陷型表型。除 Verrucomicrobium 门的代表外，编码丙二酰辅酶 A 裂解酶的基因存在于所有甲烷营养菌的基因组中。我们假设丙二酰辅酶 A 裂解酶是通过丝氨酸循环为 I 型甲烷营养菌提供乙醛酸和甘氨酸合成的酶，除了主要的核酮糖单磷酸循环外，还支持碳同化。
