BIOSYNTHESIS OF THE SIDE-CHAIN OF UBIQUINONE-TRANS-PRENYLTRANSFERASE IN RAT-LIVER MICROSOMES

被引:0
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作者
TECLEBRHAN, H
OLSSON, J
SWIEZEWSKA, E
DALLNER, G
机构
[1] KAROLINSKA INST,HUDDINGE HOSP,CLIN RES CTR,S-14186 HUDDINGE,SWEDEN
[2] POLISH ACAD SCI,INST BIOCHEM & BIOPHYS,PL-02532 WARSAW,POLAND
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中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The trans-prenyltransferase activity present in rat liver microsomes was investigated using an in vitro system. Geranyl-PP, but not farnesyl-PP is utilized as substrate. The pH optimum is at 8.0, and Mn2+ and Mg2 activate, while Zn2+ completely inhibits the enzyme. Digitonin, taurodeoxycholate, and Tween 80 increase this activity, whereas deoxycholate and SDS are inhibitory. In contrast to the cis-prenyltransferase, the trans-prenyltransferase is not dependent on cytosolic protein factors. The trans-prenyltransferase is present at the cytoplasmic surface of rough and smooth microsomes. Solanesyl-PP and all-trans-geranylgeranyl-PP inhibit the transferase activity but poly-cis-polyprenyl-12-PP, an intermediate in the cis-prenyltransferase reaction, does not. The enzyme reaction gives rise to two products, solanesyl-PP and an unidentified polyprenyl metabolite. Mevinolin treatment distinguishes this enzyme from the cytoplasmic geranylgeranyl-PP synthase. The results demonstrate that rat liver microsomes synthesize solanesyl-PP via a trans-prenyltransferase, which is distinct from cis-prenyltransferase and geranylgeranyl-PP synthase.
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页码:23081 / 23086
页数:6
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