Two intermediates in the biosynthetic pathway to bacterial menaquinones are o-succinylbenzoic acid and 1,4-dihydroxy-2-naphthoic acid. Cell-free extracts have been prepared from Escherichia coli which catalyze the conversion of labeled o-succinylbenzoic acid to the naphthoic acid and also to menaquinones. The naphthoate synthetase has been partially purified and found to require coenzyme A and ATP. The synthetase has an approximate molecular weight of 45 000. The conversion of o-succinylbenzoic acid to menaquinones is stimulated by the presence of farnesyl pyrophosphate. The major menaquinone produced is then MK-3 with the farnesyl side chain.
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Bryant et al. (1976) studied this question.
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