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Science 15 August 1986:
Vol. 233. no. 4765, pp. 788 - 790
DOI: 10.1126/science.3526552
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Articles

Science, Vol 233, Issue 4765, 788-790
Copyright © 1986 by American Association for the Advancement of Science

articles

Active human-yeast chimeric phosphoglycerate kinases engineered by domain interchange

MT Mas, CY Chen, RA Hitzeman, and AD Riggs

Phosphoglycerate kinase (PGK) is a monomeric protein composed of two domains of approximately equal size, connected by a hinge. Substrate-induced conformational change results in the closure of the active site cleft, which is situated between these two domains. In a study of the relations between structure and function of this enzyme, two interspecies hybrids were constructed, each composed of one domain from the human enzyme and one domain from the yeast enzyme. Despite a 35% difference in the amino acid composition between human and yeast PGK, catalytic properties of the hybrid enzymes are very similar to those of the parental proteins. This result demonstrates that the evolutionary substitutions within these two distantly related molecules do not significantly affect formation of the active site cleft, mechanism of domain closure, or enzyme activity itself.


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