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B6db references: absnot

type Journal Article
authors Prabhakaran P. C., Woo N-T., Yorgey P.S., Gould S.J.
title Biosynthesis of blasticidin S from L-alpha-arginine. Stereochemistry in the arginine-2,3-aminomutase reaction
journal J. Am. Chem. Soc.
Activity arg.aminomutase
Family arg.aminomutase
sel selected
ui absnot
year (1988)
volume 110
number 17
pages 5785-91
abstract A series of labeled a-arginines have been fed to fermentations of Streptomyces griseochromogenes in order to examine the mechanism of L-beta-arginine formation in the biosynthesis of the antibiotic blasticidin S. [3-'3C,2-'SN]Arginine was synthesized and fed; analysis of the derived antibiotic by I3C NMR spectroscopy revealed the retention of the original a-nitrogen and its intramolecular migration to the @position, revealing the presence of an arginine-2,3-aminomutase. Feedings of [2,3,3-2H3]-, [3,3-*H2]-, and [2-2H]arginines revealed the complete retention of the original beta-hydrogens with migration of one to the a-position, as well as partial loss of the original a-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 a-arginine migrates to the a-position (C-2). 6-N-['3CH3]Methylarginine was synthesized, mixed with [guanidino-14~C]arginine, and fed to S . griseochromogenes. A 42% incorporation of radioactivity from arginine was obtained, but no I3C enrichment was observed in the blasticidin S sample, indicating that arginine, itself, is the aminomutase substrate.
last changed 2017/11/13 14:08

B6db references