[Specificity of molecular recognition in oligomerization of bacterial L-asparaginases].
Bacterial L-asparaginases, which are widely used in the antitumor therapy, act only as homotetramers, because their active sites are located at the interface between the subunits of the enzyme. Since salt bridges substantially stabilize L-asparaginase tetramers, we have supposed that oligomerization of bacterial L-asparaginase is a high-avidity process. This assumption was proved by bioinformatic and biosensoric methods. It was shown, that a stable tetrameric complex can be formed only by the subunits of the same L-asparaginase. Using two mutants of L-asparaginase Helicobacter pylori it was shown that specificity of molecular recognition is significantly reduced even by single point mutation at the interface of high-homologous closely-related subunits.
Iu V
IuV
Mezentsev
A A
AA
Mol'nar
N N
NN
Sokolov
V B
VB
Lisitsyna
M A
MA
Shatskaia
A S
AS
Ivanov
A I
AI
Archakov
D000595:Amino Acid Sequence; D001215:Asparaginase / Q000737:chemistry*; D004926:Escherichia coli / Q000201:enzymology; D016480:Helicobacter pylori / Q000201:enzymology; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009154:Mutation; D055503:Protein Multimerization; D017434:Protein Structure, Tertiary; D017386:Sequence Homology, Amino Acid; D020349:Surface Plasmon Resonance / Q000379:methods; D013816:Thermodynamics
D001215:Asparaginase