The structural and functional basis of antibody catalysis

Herschel Wade, Thomas (Tom) Scanlan

Research output: Contribution to journalArticle

32 Citations (Scopus)

Abstract

Ten years have passed since the initial reports that antibodies could be programmed to have enzymatic activity by immunization with a transition-site analog. Much of the research over the last decade has focused on defining the scope and generality of antibody catalysis; however, during the past two years the first few crystal structures of catalytic antibody transition- state analogs have been reported. This review analyzes four such structures of catalytic antibodies that catalyze markedly different reactions, including ester hydrolysis, sulfide oxidation, and a pericyclic rearrangement. Structure-function relations for these catalysts are discussed and compared to the structure and function of natural enzymes, as well as the chemistry that occurs in solution.

Original languageEnglish (US)
Pages (from-to)461-493
Number of pages33
JournalAnnual Review of Biophysics and Biomolecular Structure
Volume26
DOIs
StatePublished - 1997
Externally publishedYes

Fingerprint

Catalytic Antibodies
Catalysis
Antibodies
Immunization
Sulfides
Hydrolysis
Esters
Enzymes
Crystal structure
Oxidation
Catalysts
Research

Keywords

  • Abzymes
  • Antigen binding
  • Catalysis
  • Catalytic mechanism

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology

Cite this

The structural and functional basis of antibody catalysis. / Wade, Herschel; Scanlan, Thomas (Tom).

In: Annual Review of Biophysics and Biomolecular Structure, Vol. 26, 1997, p. 461-493.

Research output: Contribution to journalArticle

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