Bacopa monniera recombinant mevalonate diphosphate decarboxylase: biochemical characterization

TitleBacopa monniera recombinant mevalonate diphosphate decarboxylase: biochemical characterization
Publication TypeJournal Article
Year of Publication2015
AuthorsAbbassi, S, Vishwakarma, RK, Patel, P, Kumari, U, Khan, BMohammad
JournalInternational Journal of Biological Macromolecules
Date PublishedAUG
KeywordsMevalonate diphosphate decarboxylase, pH activity profile, Phylogenetic analysis, stability

Mevalonate diphosphate decarboxylase (MDD; EC is an important enzyme in the mevalonic acid pathway catalyzing the Mg2+-ATP dependant decarboxylation of mevalonate 5-diphosphate (MVAPP) to isopentenyl diphosphate (IPP). Bacopa monniera recombinant MDD (BmMDD) protein was overexpressed in Escherichia coli BL21 (DE3) strain and purified to apparent homogeneity. K-m and V-max for MVAPP were 144 mu M and 52 U mg(-1) respectively. The values of turnover (k(cat)) and k(cat)/K-m, for mevalonate 5-diphosphate were determined to be 40 s(-1) and 2.77 x 10(5) M-1 s(-1) and k(cat) and k(cat)/K-m values for ATP were found to be 30 s(-1) and 2.20 x 10(4) M-1 s(-1), respectively. pH activity profile indicated the involvement of carboxylate ion, lysine and arginine for the activity of enzyme. The apparent activation energy for the BmMDD catalyzed reaction was 12.7 kJ mol(-1). Optimum pH and temperature for the forward reaction was found to be 8.0 and 45 degrees C. The enzyme was most stable at pH 7 at 20 degrees C with the deactivation rate constant (K-d(*)) of 1.69 x 10(-4) and half life (t(1/2)) of 68 h. The cation studies suggested that BmMDD is a cation dependant enzyme and optimum activity was achieved in the presence of Mg2+. (C) 2015 Elsevier B.V. All rights reserved.

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Biochemical Sciences