Journal
BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY
Volume 79, Issue 11, Pages 1833-1837Publisher
TAYLOR & FRANCIS LTD
DOI: 10.1080/09168451.2015.1050992
Keywords
resorcinomycin; biosynthesis; ATP-grasp-ligase; Streptoverticillium roseoverticillatum
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Funding
- Japan Society for the Promotion of Science (JSPS) [23108101, 25560397]
- Grants-in-Aid for Scientific Research [25560397, 15H03110] Funding Source: KAKEN
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Resorcinomycin (1) is composed of a nonproteinogenic amino acid, (S)-2-(3,5-dihydroxy-4-isopropylphenyl)-2-guanidinoacetic acid (2), and glycine. A biosynthetic gene cluster was identified in a genome database of Streptoverticillium roseoverticillatum by searching for orthologs of the genes responsible for biosynthesis of pheganomycin (3), which possesses a (2)-derivative at its N-terminus. The cluster contained a gene encoding an ATP-grasp-ligase (res5), which was suggested to catalyze the peptide bond formation between 2 and glycine. A res5-deletion mutant lost 1 productivity but accumulated 2 in the culture broth. However, recombinant RES5 did not show catalytic activity to form 1 with 2 and glycine as substrates. Moreover, heterologous expression of the cluster resulted in accumulation of only 2 and no production of 1 was observed. These results suggested that a peptide with glycine at its N-terminus may be used as a nucleophile and then maturated by a peptidase encoded by a gene outside of the cluster.
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