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PMID: 415304 Published · ppublish English Comparative Study Journal Article Research Support, U.S. Gov't, P.H.S.

On the evolution of beta-galactosidase.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 75 ·No. 1 ·1978-01-00 ·Pages 113-6

Hood JM, Fowler AV, Zabin I

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.

MeSH Terms
Amino Acid Sequence Bacterial Proteins/genetics Biological Evolution Enzyme Repression Escherichia coli/enzymology,genetics Galactosidases/genetics Genes, Regulator Lactose/metabolism Operon Tetrahydrofolate Dehydrogenase/genetics beta-Galactosidase/genetics
Chemicals
Bacterial Proteins Tetrahydrofolate Dehydrogenase Galactosidases beta-Galactosidase Lactose
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Hood J M
Fowler A V
Zabin I
References (17)
17 references, click to expand
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.75.1.113
Published
1978-01-00
Pages
113-6
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC411194
Subset
IM
External Links
PubMed source DOI: 10.1073/pnas.75.1.113 PMC Full Text View journal details
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