Abstract

Tryptophan synthetase was initially selected as a subject for investigation of the relationship between gene structure and protein structure. Early studies with this enzyme first demonstrated the existence in mutants of immunologically cross‐reacting material (CRM) and the restoration of a wild‐type enzyme by genetic suppression. Fine structure analyses with E. coli tryptophan synthetase missense mutants proved the colinearity of gene structure and catalytic capabilities of this enzyme have been subjects for numerous studies.