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Literature summary extracted from

  • Zik, M.; Fridmann-Sirkis, Y.; Fromm, H.
    C-terminal residues of plant glutamate decarboxylase are required for oligomerization of a high-molecular weight complex and for activation by calcium/calmodulin (2006), Biochim. Biophys. Acta, 1764, 872-876.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
4.1.1.15 Ca2+ 24fold activation of wild-type in presence of both Ca2+ and calmodulin. For mutant lacking 19 amino acids at N-terminus, 12.9fold activation. Mutant lacking 9 amino acids at C-terminus, complete loss of activation Petunia sp.
4.1.1.15 Calmodulin 24fold activation of wild-type in presence of both Ca2+ and calmodulin. For mutant lacking 19 amino acids at N-terminus, 12.9fold activation. Mutant lacking 9 amino acids at C-terminus, complete loss of activation Petunia sp.

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.1.1.15 expression in Escherichia coli Petunia sp.

Protein Variants

EC Number Protein Variants Comment Organism
4.1.1.15 DELTAC9 9 amino acid C-terminal deletion mutant, no formation of complexes larger than 340 kDa, no activation by Ca2+/calmodulin. The ability to bind calmodulin in the presence of Ca2+ is retained, and mutant may be purified by calmodulin affinity chroamtography. 12% of wild-type activity at pH 5.8 Petunia sp.
4.1.1.15 DELTAN18 18 amino acid N-terminal deletion mutant, activation by Ca2+/calmodulin is reduced by about 50%. 40% of wild-type activity at pH 5.8 Petunia sp.

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
4.1.1.15 58000
-
 x * 58000, SDS-PAGE of full-length enzyme Petunia sp.
4.1.1.15 300000
-
 gel filtration, absence of Ca2+/calmodulin Petunia sp.
4.1.1.15 580000
-
 gel filtration, absence of Ca2+/calmodulin Petunia sp.
4.1.1.15 680000
-
 gel filtration, presence of Ca2+/calmodulin Petunia sp.

Organism

EC Number Organism UniProt Comment Textmining
4.1.1.15 Petunia sp.
-
-
-

Subunits

EC Number Subunits Comment Organism
4.1.1.15 oligomer x * 58000, SDS-PAGE of full-length enzyme Petunia sp.