2,5-dihydroxyacetanilide epoxidase from Streptomyces LL-C10037 (DHAE I)
catalyzes the epoxidation of hydroquinone 4, to form epoxyquinone 7. DHAE I has been
purified to homogeneity, with an overall purification factor greater than 23,000. N-terminal
and internal amino acid sequences have been obtained from the purified enzyme so
that the epoxidase gene...
The loss of all deuterium labels from previous feedings of [2-²H]-,
[3,3-²H₂]-, and [2,3,3-²H₃]arginines had indicated the possible intermediacy
of β-hydroxy- and β-ketoarginine (30 and 31, respectively) in the
biosynthesis of the streptolidine portion of streptothricin F (la).
In order to confirm or refute this evidence, D,L-[2,3,3,5,5-²H₅]-
arginine (32) was...
Early studies on the biosynthesis of the quinoline quinone portion of
streptonigrin, 1, had suggested the intermediacy of novel aromatic amino
acids. In order to test this hypothesis, a series of compounds was synthesized
and tested for potential incorporation. [4-¹⁵N] 4-Aminoanthranilic acid,
4 5 a , [4-² H] 7-aminoquinaldinic acid,...
Feeding of [3-¹³C, 2-¹⁵N]arginine, 38a, unequivocally established that the β-
arginine moiety of blasticidin S, 1, was formed from α-arginine by an intramolecular
migration of the α-amino group to the β- position. Further feedings using chirally
deuteriated arginines 38e and 38f revealed that the aminomutase process occurred with
inversion of...