remarkable diversity in the enzymes catalyzing the last step in synthesis of the pimelate moiety of biotin显著的多样性的酶催化合成的最后一步庚二酸生物素的一部分.pdfVIP

Remarkable Diversity in the Enzymes Catalyzing the Last Step in Synthesis of the Pimelate Moiety of Biotin 1 1 1,2 Madelyn M. Shapiro , Vandana Chakravartty , John E. Cronan * 1 Department of Microbiology, University of Illinois, Urbana, Illinois, United States of America, 2 Department of Biochemistry, University of Illinois, Urbana, Illinois, United States of America Abstract Biotin synthesis in Escherichia coli requires the functions of the bioH and bioC genes to synthesize the precursor pimelate moiety by use of a modified fatty acid biosynthesis pathway. However, it was previously noted that bioH has been replaced with bioG or bioK within the biotin synthetic gene clusters of other bacteria. We report that each of four BioG proteins from diverse bacteria and two cyanobacterial BioK proteins functionally replace E. coli BioH in vivo. Moreover, purified BioG proteins have esterase activity against pimeloyl-ACP methyl ester, the physiological substrate of BioH. Two of the BioG proteins block biotin synthesis when highly expressed and these toxic proteins were shown to have more promiscuous substrate specificities than the non-toxic BioG proteins. A postulated BioG-BioC fusion protein was shown to functionally replace both the BioH and BioC functions of E. coli. Although the BioH, BioG and BioK esterases catalyze a common reaction, the proteins are evolutionarily distinct. Citation: Shapiro MM, Chakravartty V, Cronan JE (2012) Remarkable Diversity in the Enzymes Catalyzing the Last Step in Synthesis of the Pimelate Moiety of Biotin. PLoS ONE 7(11): e49440. doi:10.1371/journal.pone.0049440 Editor: Christophe Herman, Baylor College of Medicine, United States of America Received July 23, 2012; Accepted October 9,