Comparative Study
doi: 10.1073/pnas.75.1.113.
On the evolution of beta-galactosidase
- PMID: 415304
- PMCID: PMC411194
- DOI: 10.1073/pnas.75.1.113
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Comparative Study
On the evolution of beta-galactosidase
Proc Natl Acad Sci U S A.
1978 Jan.
Abstract
The amino acid sequence of beta-galactosidase (beta-D-galactoside galactohydrolase, EC 3.2.1.23) has been compared to itself and to other proteins. Two segments, each of about 380 amino acids, comprising the first three-fourths of the polypeptide chain, were found to be very similar to each other. It is concluded that they are homologous. The carboxyl-terminal fourth has a high percentage of amino acid identities with dihydrofolate reductase of Escherichia coli, suggesting these sequences also are homologous. A model for the origin of beta-galactosidase is presented. The overall similarity of beta-galactosidase to lac repressor does not appear to be significant.
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