Outputs (2)

Recombinant expression and characterisation of the oxygen-sensitive 2-enoate reductase from Clostridium sporogenes (2017)
Journal Article
Mordaka, P. M., Hall, S. J., Minton, N. P., & Stephens, G. (in press). Recombinant expression and characterisation of the oxygen-sensitive 2-enoate reductase from Clostridium sporogenes. Microbiology, https://doi.org/10.1099/mic.0.000568

‘Ene’-reductases have attracted significant attention for the preparation of chemical intermediates and biologically active products. To date, research has been focussed primarily on Old Yellow Enzyme-like proteins, due to their ease of handling, whe... Read More about Recombinant expression and characterisation of the oxygen-sensitive 2-enoate reductase from Clostridium sporogenes.

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.