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Biosynthesis of chloramphenicol
Author(s) -
Westlake D. W. S.,
Vining L. C.
Publication year - 1969
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/bit.260110609
Subject(s) - chloramphenicol , biosynthesis , phenylalanine , biochemistry , tyrosine , enzyme , streptomyces , biology , antibiotics , chemistry , stereochemistry , amino acid , bacteria , genetics
The current knowledge concerning the biosynthesis of chloramphenicol is discussed. Cultures of Streptomyces sp. 3022a fed 14 C‐shikimie acid incorporated the label to the same extent into phenylalanine, tyrosine, and chloramphenicol. Of possible precursors of the phenylpropanoid nucleus of this antibiotic only p ‐aminophenylalanine and DL ‐ threo ‐ p ‐amino phenylserine specifically labeled chloramphenicol. On the basis of these results a pathway for the biosynthesis of chloramphenicol is presented. The lack of specific incorporation of 15 N‐nitrogen from a competitive feeding experiment in which both l5 N‐nitrate and 14 N‐ DL ‐serine were fed to growing cultures suggests that both the amido‐ and the nitro‐nitrogen atom present in this antibiotic are derived from a common pool. Studies on the enzyme, DAHP synthetase, show that in streptomyces sp. 3022a it is not subject to feed back inhibition by either phenylalanine, tyrosine, or chloramphenicol.