Mechanism of Coenzyme A Biosynthesis by Sarcina lutea
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概要
- 論文の詳細を見る
The enzyme activities relating to Coenzyme A (CoA) biosynthesis in Sarcina lutea were investigated, and the CoA biosynthesis mechanism was discussed.This bacterium contained all the enzymes for operation of Brown's pathway, that is, pantothenic acid (PaA) kinase, 4'-phosphopantothenoylcysteine synthetase, 4'-phosphopantothenoylcysteine decarboxylase, 3'-dephospho-CoA pyrophosphorylase and 3'-dephospho-CoA kinase. Panthetheine was phosphorylated, but panthothenoylcysteine decarboxylase on Novelli's pathway was not detected. The activities of all these enzymes reached the maximal levels in the early stationary phase. PaA kinase, the enzyme catalyzing the first step of CoA biosynthesis, was inhibited more than 65% in the presence of 1 mM CoA, whereas this feedback inhibition was hardly observed for other enzymes.Degradation of CoA, PaA, AMP and adenine was hardly seen. Cysteine, adenosine and ATP were especially degraded in the early stationary phase. Most intermediates were converted to CoA effectively in this phase.These results indicated that CoA was synthesized from PaA through Brown's pathway in Sarcina lutea.
- 公益社団法人日本生物工学会の論文
- 1983-02-25
著者
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Nishimura Noriyuki
Research Laboratory Of Applied Biochemistry Tanabe Seiyaku Co. Ltd.
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Chibata Ichiro
Research Laboratories Tanabe Seiyaku Co. Ltd.
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KAKIMOTO TOSHIO
Research Laboratory of Applied Biochemistry, Tanabe Seiyaku Co., Ltd.,
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Kakimoto Toshio
Research Laboratory Of Applied Biochemistry Tanabe Seiyaku Co. Ltd.
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