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The enzymatic nature of antibody catalysis - development of multistep kinetic processing

Academic Article
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Overview

authors

  • Benkovic, S. J.
  • Adams, J. A.
  • Borders, C. L.
  • Janda, Kim
  • Lerner, Richard

publication date

  • November 1990

journal

  • Science  Journal

abstract

  • Detailed kinetic investigations of a catalytic antibody that promotes the hydrolyses of an anilide and phenyl ester show that this catalyst uses a multistep kinetic sequence resembling that found in serine proteases to hydrolyze its substrates, although antibody was elicited to a single transition-state analog. Like the serine proteases the antibody catalyzes the hydrolysis reactions through a putative covalent intermediate, but unlike the enzymes it may use hydroxide ion to cleave the intermediates. Nevertheless, the antibody is a potent catalyst with turnover at higher pH values rivaling that of chymotrypsin. This analysis also reveals that turnover by the antibody is ultimately limited by product desorption, suggesting that improvements in catalytic efficiency may be achieved by judicious changes in the structure of the substrate, so that it is not superimposable on that of the eliciting hapten.

subject areas

  • Acylation
  • Aniline Compounds
  • Antibodies
  • Catalysis
  • Enzymes
  • Hydrogen-Ion Concentration
  • Hydrolysis
  • Kinetics
  • Nitrophenols
  • Spectrometry, Fluorescence
  • Thermodynamics
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Identity

International Standard Serial Number (ISSN)

  • 0036-8075

Digital Object Identifier (DOI)

  • 10.1126/science.2251500

PubMed ID

  • 2251500
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Additional Document Info

start page

  • 1135

end page

  • 1139

volume

  • 250

issue

  • 4984

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