Mevalonate-5-diphosphate decarboxylase function

Mevalonate diphosphate decarboxylase (MVP EC4.1.1.33) catalyzes the conversion of mevalonate diphosphate to isopentenyl diphosphate, a key building block for a large family of functionally important terpenoids. Fig. (6). This reaction is the third step in the biosynthesis of steroids and terpenoids from the mevalonate pathway, and the last well characterized step in the mevalonate pathway for the biosynthesis of isopentenyl pyrophophaste, the isoprenoids precursor [296-298]. Some reports showed that MVP is located predominantly in the cytosolic fraction and its expression is independent of peroxisome proliferation [299-300]. 

Alvear, M., Jabalquinto, A.M., and Cardemil, E. (1989) Inactivation of chicken liver mevalonate 5-diphosphate decarboxylase by sulfhydryl-directed reagents Evidence of a functional dithiol. Biochim. Biophys. Acta 994, 7-11. 

Once mevalonate has been formed it is sequentially phosphorylated by two separate kinases yielding mevalonate 5-diphosphate. A third ATP-consuming reaction involving a decarboxylase then generates the universal isoprene unit, isopentenyl pyrophosphate (Figure 7.18). The function of the ATP in this reaction appears to be to act as an acceptor for the leaving OH group in the dehydration part of the reaction. 

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See also in sourсe #XX -- [ ]

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