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PMID: 7737457 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S. Review

The structure and evolution of alpha/beta barrel proteins.

Reardon D, Farber GK

Abstract

Roughly 10% of all known enzyme structures have an alpha/beta barrel domain. The members of this large family of proteins catalyze very different types of reactions. Such diversity of function has made this family a target for protein engineering. The evolutionary history of this family has been the subject of vigorous debate. In this paper, arguments are made to support the divergence of all members of this family from a common ancestor. Because of the lack of strong sequence homology, the ancestral molecule must be very old. A hypothesis concerning the relationship between chemical mechanism and evolutionary history is discussed. Evidence is presented to suggest that convergent molecular evolution occurs when there is only one energetically reasonable pathway for a chemical reaction.

MeSH Terms
Amino Acid Sequence Animals Biological Evolution Enzymes/chemistry Humans Molecular Sequence Data Protein Structure, Tertiary Sequence Homology, Amino Acid
Chemicals
Enzymes
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Reardon D
Department of Biochemistry and Molecular Biology, Pennsylvania State University, University Park 16802, USA.
Farber G K
Article Info
Journal
FASEB journal : official publication of the Federation of American Societies for Experimental Biology
Abbr.
FASEB J
ISSN
0892-6638
Published
1995-04-00
Pages
497-503
Language
English
Region
United States
NLM ID
8804484
Subset
IM
Databases
GENBANK
UNKNOWN
PIR
UNKNOWN
SWISSPROT
UNKNOWN
Corrections
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