[16] Eukaryotic prenyltransferases

作者: Hans C. Rilling

DOI: 10.1016/S0076-6879(85)10069-8

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摘要: Publisher Summary This chapter discusses the prenyltransferase of sterol biosynthesis in eukaryotes. enzyme condenses either a C 5 or 10 allylic pyrophosphate with homoallylic to give, as ultimate product, farnesyl which then serves substrate for squalene and synthesis. All eukaryotic synthetases are dimeric proteins molecular weight about 80,000. The specific activities homogeneous prenyltransferases vary from 900 pig liver 5200 yeast. There many different that produce every size product dimer (geranyl pyrophosphate) high polymers, gutta percha, rubber. Cis well trans isomers may be produced. these enzymes accept geranyl dimethylallylpyrophosphate substrates, Michaelis constants between 0.1 1 μM all substrates. It is also possible this produces dolichyl nonaprenyl (ubiquinone) However, it not clear if other participate those pathways. Prenyltransferase has been assayed onset by measuring conversion acid-stable (isopentenyl bearing radiolabel) acid-labile product. minor variations procedure, but general, after incubation mineral acid used hydrolysis nonpolar products thus formed extracted into an organic solvent determination radioactivity.

参考文章(11)
John W. Porter, Sandra L. Spurgeon, Biosynthesis of Isoprenoid Compounds ,(1981)
N L Eberhardt, H C Rilling, Prenyltransferase from Saccharomyces cerevisiae. Purification to homogeneity and molecular properties. Journal of Biological Chemistry. ,vol. 250, pp. 863- 866 ,(1975) , 10.1016/S0021-9258(19)41865-6
F.M. Laskovics, J.M. Krafcik, C.D. Poulter, Prenyltransferase. Kinetic studies of the 1'-4 coupling reaction with avian liver enzyme. Journal of Biological Chemistry. ,vol. 254, pp. 9458- 9463 ,(1979) , 10.1016/S0021-9258(19)83538-X
David N. Brems, Hans C. Rilling, Photoaffinity labeling of the catalytic site of prenyltransferase. Biochemistry. ,vol. 18, pp. 860- 864 ,(1979) , 10.1021/BI00572A019
Graham F. Barnard, Beatrice Langton, George Popják, Pseudo-isoenzyme forms of liver prenyl transferase☆ Biochemical and Biophysical Research Communications. ,vol. 85, pp. 1097- 1103 ,(1978) , 10.1016/0006-291X(78)90655-1
David N. Brems, Eveline Bruenger, Hans C. Rilling, Isolation and characterization of a photoaffinity-labeled peptide from the catalytic site of prenyltransferase Biochemistry. ,vol. 20, pp. 3711- 3718 ,(1981) , 10.1021/BI00516A007
Brent C. Reed, Hans C. Rilling, Substrate Binding of avian liver prenyltransferase. Biochemistry. ,vol. 15, pp. 3739- 3745 ,(1976) , 10.1021/BI00662A015
Brent C. Reed, Hans C. Rilling, Crystallization and partial characterization of prenyltransferase from avian liver Biochemistry. ,vol. 14, pp. 50- 54 ,(1975) , 10.1021/BI00672A009
Lai-Su Yeh, Hans C. Rilling, Purification and properties of pig liver prenyltransferase: Interconvertible forms of the enzyme☆ Archives of Biochemistry and Biophysics. ,vol. 183, pp. 718- 725 ,(1977) , 10.1016/0003-9861(77)90405-2
Tanetoshi KOYAMA, Yukiko SAITO, Kyozo OGURA, Shuichi SETO, Two forms of farnesyl pyrophosphate synthetase from hog liver. Journal of Biochemistry. ,vol. 82, pp. 1585- 1590 ,(1977) , 10.1093/OXFORDJOURNALS.JBCHEM.A131853