EC Number |
Protein Variants |
Reference |
---|
2.7.1.24 | D32A |
the mutant shows a catalytic efficiency of only 5% of the native enzyme |
723528 |
2.7.1.24 | D32E |
the mutant shows increased catalytic efficiency compared to the wild type enzyme |
723528 |
2.7.1.24 | D32N |
the mutant shows an almost 2.54times increased Km value for 3'-dephospho-CoA compared to the wild type enzyme. The absence of magnesium completely ablates activity for the D32N mutant |
723528 |
2.7.1.24 | G8A |
this mutation does not change either the Km or the Kcat of the reaction considerably |
723528 |
2.7.1.24 | K14A |
the substitution affects the kinetic parameters of the reaction resulting in a mere 19% reduction in the Kcat of the enzyme, the mutant demonstrates a 50% increase in the Km for ATP |
723528 |
2.7.1.24 | L114A |
the mutation results in a decrease in the affinity of the enzyme for the acceptor substrate |
723528 |
2.7.1.24 | more |
disruption of the TK1697 resulting in CoA auxotrophy. The DELTATK1697 mutant is inoculated in ASW-YT-pyruvate-agmatine medium, but no growth is observed. When 1 mM CoA is added to the medium, the growth defect is partially complemented, with lower growth rate and less cell yield than the wild-type strain KPD1. In the strain transformed with pRPETK1697, the growth defect is almost fully complemented |
-, 759707 |
2.7.1.24 | more |
experiments to generate a single gene deletion of DPCK in Plasmodium yoelii 17X-NL parasites show that the inability to delete PyPPAT and PyDPCK is not due to a technical reason, nor the inability to access the gene loci, but due to a crucial role that both enzymes play in the growth and/or survival of blood stage parasites in mouse erythrocytes |
759223 |
2.7.1.24 | more |
generation of trophozoites of Ehdpck1 and Ehdpck2 gene-silenced strains. Ehdpck1 and Ehdpck2 gene-silenced strains show significant growth defect in normal growth medium. The level of growth inhibition by Ehdpck2 gene silencing is more severe compared to that by Ehdpck1 gene silencing |
759246 |
2.7.1.24 | R140A |
this mutation completely abolishes kinetic activity |
723528 |