Kirromycin‐resistant elongation factor Tu from wild‐type of Lactobacillus brevis

FEBS Letters

Wolf, Heinz¹  Wörner, Walter¹ 

[1] Institut für Biologie II, Lehrstuhl für Mikrobiologie I der Universität, D-74000 Tübingen, FRG

关键词: Elongation factor Tu;    Lactobacillus brevis;    Kirromycin resistance;    Pulvomycin;    Nucleotide-binding site;    Heat stability;    EF;    elongation factor;    EF-Tuf;    nucleotide-free elongation factor Tu;    affices;    refer to the source of the protein;    Ec;    Escherichia coli;    Lb;    Lactobacillus brevis;   

DOI  :  10.1016/0014-5793(82)80944-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Properties of the elongation factor Tu from Lactobacillus brevis which is naturally insensitive to kirromycin are described. The protein is characterized by an unusual nucleotide-binding site with increased affinity for GTP and extreme heat stability. EF-Tu is sensitive to pulvomycin in the assay of polyphenylalanine synthesis. However, the failure of the protein to display pulvomycin-dependent GDP-binding and GTPase activity indicates that pulvomycin action in L. brevis differs from that in E. coli.

【 授权许可】

Unknown