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Enzymatic synthesis of the coenzyme a ester of o ‐succinylbenzoic acid, an intermediate in menaquinone (vitamin K 2 ) biosynthesis
Author(s) -
Heide L.,
Leistner E.
Publication year - 1981
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(81)80080-4
Subject(s) - biosynthesis , enzyme , chemistry , biochemistry
The quinonoid moiety of menaquinones (i.e., vitamin K,) (V) is known to be biosynthetically derived from shikimic acid [l] and 4-(2’.carboxyphenyl)4oxobutanoic acid (i.e., o-succinylbenzoic acid, OSB) (I) [2] (fig-l). While the cell-free synthesis of (I) has not yet been demonstrated its enzymic conversion to 1,4-dihydroxy-2-naphthoic acid (DHNA) (III) was shown to require ATP and CoASH [3]. This conversion is catalyzed by 2 different enzymes, viz., o-succinylbezoyl-coenzyme A synthetase and dihydroxynaphthoate synthase [4]. It has been assumed [3] that in the course of this conversion the aromatic carboxyl group of (I) is activated with coenzyme A. The postulated CoA ester (II; R 1 = SCoA; R2 = OH), however, has never been isolated. We now report on the detection of a CoA derivative of (I) in cell-free preparations ofMycobacterium phlei. The unstable CoA derivative, presumably a CoA ester, was isolated and shown to be converted to 1,4-dihydroxy-2.naphthoic acid (DHNA) (III) by an enzyme preparation from the same organism.