PMID:7045104
| Citation |
Heide, L, Arendt, S and Leistner, E (1982) Enzymatic synthesis, characterization, and metabolism of the coenzyme A ester of o-succinylbenzoic acid, an intermediate in menaquinone (vitamin K2) biosynthesis. J. Biol. Chem. 257:7396-400 |
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| Abstract |
The enzymatic synthesis of the "active" o-succinylbenzoic acid is described and the factors controlling its formation are investigated. Tritium-labeled coenzyme A is incorporated into "active" o-succinylbenzoic acid, but label from [2-3H]ATP or [gamma-32P is not, indicating that the active compound is a coenzyme A thio ester(2). The compound is shown by two different methods to contain 1 mol only of coenzyme A per mol of o-succinylbenzoic acid. The o-succinylbenzoic and coenzyme A ester (2) is unstable at alkaline and neutral pH, but is fairly stable under acid conditions. The coenzyme A ester (2) is converted to 1,4-dihydroxy-2-naphthoic acid (3) by enzyme preparations from Mycobacterium phlei and Escherichia coli without any cofactor requirement. |
| Links | |
| Keywords |
Acyl Coenzyme A/analogs & derivatives; Acyl Coenzyme A/metabolism; Cell-Free System; Escherichia coli/metabolism; Kinetics; Mycobacterium/metabolism; Mycobacterium phlei/metabolism; Phosphorus Radioisotopes; Radioisotope Dilution Technique; Tritium; Vitamin K/biosynthesis |
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