Metal ion cofactors are necessary for prenyltransferase enzymes. Magnesium and manganese can be usedas metal ion cofactor by rubber transferase (a
cis-prenyltransferase) associated with purified rubber particles.The rubber initiation rate, biosynthetic rate, and molecular weight produced in vitro from
Hevea brasiliensisrubber transferase is regulated by metal ion concentration. In addition,
![](/isubscribe/journals/bomaf6/6/i01/eqn/bm049606we10001.gif)
varies significantly with[Mg
2+].
![](/isubscribe/journals/bomaf6/6/i01/eqn/bm049606we10002.gif)
decreases from 8000 ± 600
![](/images/entities/mgr.gif)
M at [Mg
2+] = 4 mM to 68 ± 10
![](/images/entities/mgr.gif)
M at [Mg
2+] = 8 mM andincreases back to 970 ± 70
![](/images/entities/mgr.gif)
M at [Mg
2+] = 30 mM. The highest affinity of rubber transferase for IPP·Mgoccurred when [Mg
2+] =
Amax (metal concentration that gives highest IPP incorporation rate). A metal ionis required for rubber biosynthesis, but an excess of metal ions interacts with the rubber transferase inhibitingits activity. The results suggest that
H. brasiliensis could use [Mg
2+] as a regulatory mechanism for rubberbiosynthesis and molecular weight in vivo.