Affiliation:
1. Department of Biochemistry, College of Physicians and Surgeons, Columbia University, New York, New York 10032
Abstract
The enzymatic synthesis of 7-oxo-8-aminopelargonic acid (7-KAP) from pimelyl-coenzyme A and
l
-alanine was demonstrated in cell-free extracts of a biotin mutant of
Escherichia coli
K-12 which excretes only 7-KAP into the growth medium. This biotin vitamer was identified by its chromatographic and electrophoretic properties. The enzyme (7-KAP synthetase) was repressed when the organism was grown in biotin concentrations greater than 0.2 ng/ml. The parent strain and members of other mutant groups that excrete 7-KAP, in addition to other vitamers, also exhibited synthetase activity. A mutant group that failed to excrete 7-KAP was further sub-divided into three groups, one of which lacked synthetase activity. These results are discussed in relation to a previously proposed scheme for biotin biosynthesis in which the formation of 7-KAP is considered the point of entry for pimelic acid into the biotin pathway.
Publisher
American Society for Microbiology
Subject
Molecular Biology,Microbiology
Cited by
81 articles.
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