Specificity of molecular recognition in oligomerization of bacterial L-asparaginases

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• 作者：Yu. V. Mezentsev (1) yuri.mezentsev@ibmc.msk.ru
  A. A. Molnar (1)
  N. N. Sokolov (1)
  V. B. Lisitsina (2)
  M. A. Shatskaya (2)
  A. S. Ivanov (1)
  A. I. Archakov (1)
• 关键词：specificity &#8211 ; molecular recognition &#8211 ; oligomerization &#8211 ; L ; asparaginase &#8211 ; computer modeling &#8211 ; optical biosensor &#8211 ; surface plasmon resonance
• 刊名：Biochemistry (Moscow) Supplemental Series B ; Biomedical Chemistry
• 出版时间：June 2011
• 出版年：2011
• 期刊代码：pc316_1990-7508
• 类别：ch
• 卷：5
• 期：2
• 页码：124-134
• 数据来源：sp

摘要

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 these enzymes. High stability of aspaginase tetramers is determined by ion pair formation between subunits, and this suggests high specificity of molecular recognition during oligomerization of bacterial L-asparaginases. In this study we have investigated specificity of molecular recognition in oligomerization of some bacterial asparaginases by a biosensor based on surface plasmon resonance. It was shown, that a stable tetrameric complex could be formed only by the subunits of the same L-asparaginase. Using two mutants of Helicobacter pylori L-asparaginase it was shown that even a single point mutation at the interface of highly homologous and closely related subunits significantly reduced specificity of molecular recognition.