|
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 |
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