Substrate specificity of cis-prenyltransferase in rat liver microsomes.

作者: J Ericsson , A Thelin , T Chojnacki , G Dallner

DOI: 10.1016/S0021-9258(18)41836-4

关键词:

摘要: Long chain cis-prenyltransferase in rat liver microsomes was studied using various allylic isoprenoid substrates. Microsomes could utilize trans-geranyl pyrophosphate, but not cis-geranyl pyrophosphate for polyprenyl synthesis. Both trans, trans-farnesyl and trans,cis-farnesyl were used as substrates with Km values of 24 5 microM, respectively. trans,trans,cis-Geranylgeranyl be substrate an apparent 36 microM. trans,trans,trans-Geranylgeranyl also utilized substrate, a very low affinity. After pulse labeling 4 min, [3H]isopentenyl trans,trans-farnesyl the only product formed trans,trans,cis-geranylgeranyl which, upon chasing, yielded pyrophosphate. Independent nature used, even case 12-pyrophosphate all-trans-nonaprenyl lengths products identical, i.e. pyrophosphates 15-18 isoprene residues. able to synthesize substrate. The results indicate that contain farnesyl synthase activity reaction catalyzed by may consist two individual steps, synthesis elongation this long pyrophosphates.

参考文章(37)
G. Popják, J.W. Cornforth, Rita H. Cornforth, R. Ryhage, DeWitt S. Goodman, Studies on the Biosynthesis of Cholesterol XVI. CHEMICAL SYNTHESIS OF 1-H23-2-C14- AND 1-D2-2-C14-TRANS-TRANS-FARNESYL PYROPHOSPHATE AND THEIR UTILIZATION IN SQUALENE BIOSYNTHESIS Journal of Biological Chemistry. ,vol. 237, pp. 56- 61 ,(1962) , 10.1016/S0021-9258(18)81360-6
Hiroshi Sagami, Kyozo Ogura, Shuichi Seto, Tadashi Kurokawa, A new prenyltransferase from Micrococcus lysodeikticus. Biochemical and Biophysical Research Communications. ,vol. 85, pp. 572- 578 ,(1978) , 10.1016/0006-291X(78)91201-9
T Chojnacki, G Dallner, The biological role of dolichol. Biochemical Journal. ,vol. 251, pp. 1- 9 ,(1988) , 10.1042/BJ2510001
Tomasz Vogtman, Tadeusz Chojnacki, The occurrence and seasonal distribution of C50-C60-polyprenols and of C100-and similar long-chain polyprenols in leaves of plants. Acta Biochimica Polonica. ,vol. 31, pp. 115- 126 ,(1984)
Hiroshi Sagami, Koichi Ishii, Kyozo Ogura, [21] Geranylgeranylpyrophosphate synthetase of pig liver Methods in Enzymology. ,vol. 110, pp. 184- 188 ,(1985) , 10.1016/S0076-6879(85)10074-1
M.J. James, A.A. Kandutsch, Inter-relationships between dolichol and sterol synthesis in mammalian cell cultures. Journal of Biological Chemistry. ,vol. 254, pp. 8442- 8446 ,(1979) , 10.1016/S0021-9258(19)86911-9
O Tollbom, C Valtersson, T Chojnacki, G Dallner, Esterification of dolichol in rat liver. Journal of Biological Chemistry. ,vol. 263, pp. 1347- 1352 ,(1988) , 10.1016/S0021-9258(19)57308-2
Allan G. Gornall, Charles J. Bardawill, Maxima M. David, Determination of serum proteins by means of the biuret reaction. Journal of Biological Chemistry. ,vol. 177, pp. 751- 766 ,(1949) , 10.1016/S0021-9258(18)57021-6
A. Joly, G. Popják, P.A. Edwards, In vitro identification of a soluble protein:geranylgeranyl transferase from rat tissues. Journal of Biological Chemistry. ,vol. 266, pp. 13495- 13498 ,(1991) , 10.1016/S0021-9258(18)92724-9
J.E. Potter, M.J. James, A.A. Kandutsch, Sequential cycles of cholesterol and dolichol synthesis in mouse spleens during phenylhydrazine-induced erythropoiesis. Journal of Biological Chemistry. ,vol. 256, pp. 2371- 2376 ,(1981) , 10.1016/S0021-9258(19)69789-9