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J. Biochem, 1988, Vol. 103, No. 5 867-871
© 1988 Japanese Biochemical Society

research-article

Undecaprenyl Diphosphate Synthase from Micrococcus luteus B-P 26: Essential Factors for the Enzymatic Activity1

Tanetoshi Koyama, Ichirou Yoshida and Kyozo Ogura

Chemical Research Institute of Non-Aqueous Solutions, Tohoku University Sendai, Miyagi 980

An undecaprenyl diphosphate synthase fraction, which was free of other prenyltransferases and was active without the addition of detergent or phospholipid, was obtained by Sephadex G-100 chromatography of cell-free extracts of Micrococcus luteus B-P 26 cells. The addition of small amounts of Triton X-100 to this fraction caused a marked loss of the enzyme activity, but the activity was gradually restored as further detergent was added. When the enzyme fraction was chromatographed on DEAE-cellulose, the synthase was partially purified, but the activity was not detected unless assayed with addition of the detergent or a lipid fraction of this bacterium. Among the three phospholipids isolated from this bacterium, cardiolipin and phosphatidylglycerol had a marked effect in activating lipid-depleted undecaprenyl diphosphate synthase, but O-lysylphosphatidylglycerol, which occurs prominently in this bacterium, had little effect.

1This work was supported in part by Grants-in-Aid for Scientific Research (Nos. 60540346 and 60303006) from the Ministry of Education, Science and Culture of Japan, and by funds from the Asahi Glass Foundation for contributions to industrial technology.


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