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Literature summary for 4.1.1.33 extracted from

  • Abbassi, S.; Patel, K.; Khan, B.; Bhosale, S.; Gaikwad, S.
    Functional and conformational transitions of mevalonate diphosphate decarboxylase from Bacopa monniera (2016), Int. J. Biol. Macromol., 83, 160-170 .
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Bacopa monnieri

General Stability

General Stability Organism
enzyme is a multi-tryptophan protein, the tryptophan environment gets perturbed even at low concentrations of denaturant, and the unfolding is gradual and partially reversible. The secondary structure of MDD is quite stable in acidic as well as alkaline pH range Bacopa monnieri

Organism

Organism UniProt Comment Textmining
Bacopa monnieri A0A0F6WBJ2
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Bacopa monnieri

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
40
-
thermal denaturation causes rapid structural transitions at and above 40°C and transient exposure of hydrophobic residues at 50°C, leading to aggregation of the protein Bacopa monnieri

pH Stability

pH Stability pH Stability Maximum Comment Organism
4
-
an acid-induced molten globule-like structure is observed at pH 4 Bacopa monnieri