88597-07-3Relevant academic research and scientific papers
Biosynthesis of blasticidin S from L-α-arginine. Stereochemistry in the arginine-2,3-aminomutase reaction
Prabhakaran,Woo,Yorgey,Gould
, p. 5785 - 5791 (1988)
A series of labeled α-arginines have been fed to fermentations of Streptomyces griseochromogenes in order to examine the mechanism of L-β-arginine formation in the biosynthesis of the antibiotic blasticidin S. [3-13C,2-15N]Arginine was synthesized and fed; analysis of the derived antibiotic by 13C NMR spectroscopy revealed the retention of the original α-nitrogen and its intramolecular migration to the β-position, revealing the presence of an arginine-2,3-aminomutase. Feedings of [2,3,3-2H3]-, [3,3-2H2]-, and [2-2H]arginines revealed the complete retention of the original β-hydrogens with migration of one to the α-position, as well as partial loss of the original α-hydrogen presumably due to arginine racemase activity. (3R)-[3-2H]- and (3S)-[3-2H]arginines were synthesized unambiguously and used to determine that the pro-3R hydrogen of α-arginine migrates to the α-position (C-2). δ-N-[13CH3]Methylarginine was synthesized, mixed with [guanidino-14C]arginine, and fed to S. griseochromogenes. A 42% incorporation of radioactivity from arginine was obtained, but no 13C enrichment was observed in the blasticidin S sample, indicating that arginine, itself, is the aminomutase substrate.
The biosynthesis of the streptolidine moiety in streptothricin F
Martinkus,Tann,Gould
, p. 3493 - 3505 (2007/10/02)
A series of arginines specifically labeled either with 13C and 15N or with 2H were synthesized and fed to Streptomyces L-1689-23. The streptothricin F isolated in each case was analyzed by either 13C or 2H NMR, respectively, in order to determine the labeling pattern obtained. From these results, it appears that arginine is metabolized to a β-ketoarginine, possibly via a pyridoxal phosphate adduct, and then via cyclization, reduction, rearrangement, and hydroxylation to the streptolidine moiety. The pathway described can also account for the formation of other known antibiotics, and for β-hydroxy-γ-amino acids, generally.
