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Preparation of a Soluble Bifunctional Enzyme by Gene Fusion

Bio/Technology volume 3, pages 821–823 (1985)Cite this article

Abstract

Within the cellular framework are a number of sequentially operating enzyme systems, in many cases in the form of bi- or even multifunctional proteins each consisting of a single type of polypeptide chain but having two or more catalytic or binding functions. In order to study the properties of an artificial bifunctional enzyme, an in-frame fusion of the structural genes for β-galactosidase (lacZ) and galactokinase (galK) of Escherichia coli was made in vitro. This DNA chimaera was constructed by connecting the 3′-terminus of the lacZ gene to the 5′-terminus of the galK gene. The translated gene product was able to catalyze the sequential reaction normally carried out by the separate native enzymes.

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Author notes

  1. Klaus Mosbach

    Present address: Institute of Biotechnology, Swiss Federal Institute of Technology, ETH-Hönggerberg, CH-8093, Zürich, Switzerland

Authors and Affiliations

  1. Pure and Applied Biochemistry, Chemical Center, University of Lund, P.O. Box 124, S-221 00, Lund, Sweden

    Leif Bülow & Peter Ljungcrantz

Authors
  1. Leif Bülow
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Bülow, L., Ljungcrantz, P. & Mosbach, K. Preparation of a Soluble Bifunctional Enzyme by Gene Fusion. Nat Biotechnol 3, 821–823 (1985). https://doi.org/10.1038/nbt0985-821

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