120659-38-3Relevant articles and documents
Evolution of siderophore pathways in human pathogenic bacteria
Franke, Jakob,Ishida, Keishi,Hertweck, Christian
, p. 5599 - 5602 (2014)
Ornibactin and malleobactin are hydroxamate siderophores employed by human pathogenic bacteria belonging to the genus Burkholderia. Similarities in their structures and corresponding biosynthesis gene clusters strongly suggest an evolutionary relationship. Through gene coexpression and targeted gene manipulations, the malleobactin pathway was successfully morphed into an ornibactin assembly line. Such an evolutionary-guided approach has been unprecedented for nonribosomal peptide synthetases. Furthermore, the timing of amino acid acylation before peptide assembly, the absolute configuration of the ornibactin side chain, and the function of the acyl transferase were elucidated. Beyond providing a proof of principle for the rational design of siderophore pathways, a compelling model for the evolution of virulence traits is presented.
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Lemieux
, p. 415,422 (1951)
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Phototemtide A, a Cyclic Lipopeptide Heterologously Expressed from Photorhabdus temperata Meg1, Shows Selective Antiprotozoal Activity
Zhao, Lei,Vo, Tien Duy,Kaiser, Marcel,Bode, Helge B.
, p. 1288 - 1292 (2020)
A new cyclic lipopeptide, phototemtide A (1), was isolated from Escherichia coli expressing the biosynthetic gene cluster pttABC from Photorhabdus temperata Meg1. The structure of 1 was elucidated by HR-ESI-MS and NMR experiments. The absolute configurations of amino acids and 3-hydroxyoctanoic acid in 1 were determined by using the advanced Marfey's method and comparison after total synthesis of 1, respectively. Additionally, three new minor derivatives, phototemtides B–D (2–4), were identified by detailed HPLC–MS analysis. Phototemtide A (1) showed weak antiprotozoal activity against Plasmodium falciparum, with an IC50 value of 9.8 μm. The biosynthesis of phototemtides A–D (1–4) was also proposed.
The structure of viscosin, a peptide antibiotic. I. Syntheses of D- and L-3-hydroxyacyl-L-leucine hydrazides related to viscosin.
Hiramoto,Okada,Nagai,Kawamoto
, p. 1308 - 1314 (1971)
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Method for producing aliphatic carboxylic acid compound and pyridine compound adduct of aliphatic ketone compound
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Paragraph 0172; 0175-0176; 0182; 0185-0186; 0192; 0195-0196, (2020/05/02)
Provided are: a method for producing an aliphatic carboxylic acid compound safely and easily from a starting material that can be obtained or produced industrially without generating a harmful substance such as haloform; and a pyridine compound adduct of an aliphatic ketone compound. The method for producing an aliphatic carboxylic acid compound is a method for producing an aliphatic carboxylic acid compound represented by Formula (I), and comprises: a first step for obtaining a pyridine compound adduct by adding a pyridine compound to an aliphatic ketone compound having an alpha-methyl groupin the presence of an oxidizing agent; and a second step of hydrolyzing the pyridine compound adduct in the presence of a base. In the Formula, R1 represents a substituted or unsubstituted linear alkyl group having 4-8 carbon atoms or a substituted or unsubstituted branched alkyl group having 4-8 carbon atoms; M represents hydrogen, a metal belonging to Group 1 or Group 2 of the periodic table, amethyl group, an ethyl group, an n-propyl group or an isopropyl group.
Characterization of FabG and FabI of the Streptomyces coelicolor dissociated fatty acid synthase
Singh, Renu,Reynolds, Kevin A.
, p. 631 - 640 (2015/03/31)
Streptomyces coelicolor produces fatty acids for both primary metabolism and for biosynthesis of the secondary metabolite undecylprodiginine. The first and last reductive steps during the chain elongation cycle of fatty acid biosynthesis are catalyzed by FabG and FabI. The S. coelicolor genome sequence has one fabI gene (SCO1814) and three likely fabG genes (SCO1815, SCO1345, and SCO1846). We report the expression, purification, and characterization of the corresponding gene products. Kinetic analyses revealed that all three FabGs and FabI are capable of utilizing both straight and branched-chain β-ketoacyl-NAC and enoyl-NAC substrates, respectively. Furthermore, only SCO1345 differentiates between ACPs from both biosynthetic pathways. The data presented provide the first experimental evidence that SCO1815, SCO1346, and SCO1814 have the catalytic capability to process intermediates in both fatty acid and undecylprodiginine biosynthesis.
