@article { ISI:000359166300084,
	title = {Bacopa monniera recombinant mevalonate diphosphate decarboxylase: biochemical characterization},
	journal = {International Journal of Biological Macromolecules},
	volume = {79},
	year = {2015},
	month = {AUG},
	pages = {661-668},
	publisher = {ELSEVIER SCIENCE BV},
	address = {PO BOX 211, 1000 AE AMSTERDAM, NETHERLANDS},
	abstract = {<p>Mevalonate diphosphate decarboxylase (MDD; EC 4.1.1.33) 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.</p>},
	keywords = {Mevalonate diphosphate decarboxylase, pH activity profile, Phylogenetic analysis, stability},
	issn = {0141-8130},
	doi = {10.1016/j.ijbiomac.2015.05.041},
	author = {Shakeel Abbassi and Vishwakarma, Rishi K. and Patel, Parth and Kumari, Uma and Khan, Bashir Mohammad}
}
@article { ISI:000369200500019,
	title = {Functional and conformational transitions of mevalonate diphosphate decarboxylase from Bacopa monniera},
	journal = {International Journal of Biological Macromolecules},
	volume = {83},
	year = {2016},
	month = {FEB},
	pages = {160-170},
	publisher = {ELSEVIER SCIENCE BV},
	address = {PO BOX 211, 1000 AE AMSTERDAM, NETHERLANDS},
	abstract = {<p>Functional and conformational transitions of mevalonate diphosphate decarboxylase (MDD), a key enzyme of mevalonate pathway in isoprenoid biosynthesis, from Bacopa monniera (BmMDD), cloned and overexpressed in Escherichia coli were studied under thermal, chemical and pH-mediated denaturation conditions using fluorescence and Circular dichroism spectroscopy. Native BmMDD is a helix dominant structure with 45\% helix and 11\% sheets and possesses seven tryptophan residues with two residues exposed on surface, three residues partially exposed and two situated in the interior of the protein. Thermal denaturation of BmMDD causes rapid structural transitions at and above 40 degrees C and transient exposure of hydrophobic residues at 50 degrees C, leading to aggregation of the protein. An acid induced molten globule like structure was observed at pH 4, exhibiting altered but compact secondary structure, distorted tertiary structure and exposed hydrophobic residues. The molten globule displayed different response at higher temperature and similar response to chemical denaturation as compared to the native protein. The surface tryptophans have predominantly positively charged amino acids around them, as indicated by higher K-SV for IC as compared to that for CsCl. The native enzyme displayed two different lifetimes, vi (1.203 +/- 0.036 ns) and tau 2 (3.473 +/- 0.12 ns) indicating two populations of tryptophan. (C) 2015 Elsevier B.V. All rights reserved.</p>},
	keywords = {Aggregation, CD spectroscopy, Fluorescence quenching, Mevalonate diphosphate decarboxylase, Unfolding},
	issn = {0141-8130},
	doi = {10.1016/j.ijbiomac.2015.11.067},
	author = {Shakeel, Abbassi and Patel, Krunal and Khan, Bashir Mohammad and Bhosale, Siddharth H. and Gaikwad, Sushama M.}
}
