The putative mevalonate diphosphate decarboxylase from Picrophilus torridus is in reality a mevalonate-3-kinase with high potential for bioproduction of isobutene

Rossoni, Luca; Hall, Stephen J.; Eastham, Graham; Licence, Peter; Stephens, Gill

doi:10.1128/AEM.04033-14

All Outputs (2)

An automated fabrication strategy to create patterned tubular architectures at cell and tissue scales (2015)
Journal Article
Othman, R., Morris, G. E., Shah, D. A., Hall, S., Hall, G., Wells, K., …Dixon, J. E. (2015). An automated fabrication strategy to create patterned tubular architectures at cell and tissue scales. Biofabrication, 7(2), Article 025003. https://doi.org/10.1088/1758-5090/7/2/025003

The putative mevalonate diphosphate decarboxylase from Picrophilus torridus is in reality a mevalonate-3-kinase with high potential for bioproduction of isobutene (2015)
Journal Article
Rossoni, L., Hall, S. J., Eastham, G., Licence, P., & Stephens, G. (2015). The putative mevalonate diphosphate decarboxylase from Picrophilus torridus is in reality a mevalonate-3-kinase with high potential for bioproduction of isobutene. Applied and Environmental Microbiology, 81(7), https://doi.org/10.1128/AEM.04033-14

Mevalonate diphosphate decarboxylase (MVD) is an ATP-dependent enzyme that catalyzes the phosphorylation/decarboxylation of (R)-mevalonate-5-diphosphate to isopentenyl pyrophosphate in the mevalonate (MVA) pathway.MVD is a key enzyme in engineered me... Read More about The putative mevalonate diphosphate decarboxylase from Picrophilus torridus is in reality a mevalonate-3-kinase with high potential for bioproduction of isobutene.