EC Number |
Natural Substrates |
---|
2.5.1.87 | (2E,6E)-farnesyl diphosphate + 13 isopentenyl diphosphate |
- |
2.5.1.87 | (2E,6E)-farnesyl diphosphate + 13 isopentenyl diphosphate |
Rer2p Z-prenyltransferase synthesizes a well-defined family of polyprenols of 1318 isoprene residues with dominating C80 (16 isoprene residues) extending to C120. Two polyisoprenoid families with dominating C80 and C110 indicating the activity of both yeast Z-prenyltransferases Rer2p and Srt1p, respectively. The family of longer chain dolichols appearing in the stationary growth phase contains dolichols with even more than 50 isoprene units exhibiting monotonically decreasing amounts with increasing chain lengths. The family of shorter chain dolichols is characteristic of the Rer2p products synthesized during the logarithmic growth phase of yeast. It forms a well-defined family of dolichols with 1318 isoprene residues with a certain level of longer dolichols composed of up to 24 isoprene units |
2.5.1.87 | (2E,6E)-farnesyl diphosphate + 14 isopentenyl diphosphate |
- |
2.5.1.87 | (2E,6E)-farnesyl diphosphate + 19 isopentenyl diphosphate |
- |
2.5.1.87 | (2E,6E)-farnesyl diphosphate + 21 isopentenyl diphosphate |
trans,trans-farnesyl diphosphate is a better substrate than geranylgeranyl diphosphate. The enzyme catalyzes the formation of polyprenyl diphosphates with predominant carbon number C120. In vitro rubber biosynthesis analysis indicates that the Arabidopsis cis-prenyltransferase itself could not catalyze the formation of high molecular weight polyprenyl diphosphate such as natural rubber |
2.5.1.87 | (2E,6E)-farnesyl diphosphate + 5 isopentenyl diphosphate |
the polyprenol product of Srt1p is longer in chain length than that of Rer2p and is not sufficiently converted to dolichol and dolichyl phosphate, unlike that of Rer2p |
2.5.1.87 | (2E,6E)-farnesyl diphosphate + 6 isopentenyl diphosphate |
the polyprenol product of Srt1p is longer in chain length than that of Rer2p and is not sufficiently converted to dolichol and dolichyl phosphate, unlike that of Rer2p |
2.5.1.87 | (2E,6E)-farnesyl diphosphate + n isopentenyl diphosphate |
the enzyme preferably utilizes both geranyl diphosphate and farnesyl diphosphate as the starting substrate |
2.5.1.87 | (2E,6E)-farnesyl diphosphate + n isopentenyl diphosphate |
- |
2.5.1.87 | (2E,6E)-farnesyl diphosphate + n isopentenyl diphosphate |
cis-prenyltransferase activity of the Candida albicans Rer2 homologue |