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Mimicking enzyme evolution by generating new (betaalpha)8-barrels from (betaalpha)4-half-barrels.

Höcker, Birte, Claren, Jörg and Sterner, Reinhard (2004) Mimicking enzyme evolution by generating new (betaalpha)8-barrels from (betaalpha)4-half-barrels. Proceedings of the National Academy of Sciences of the United States of America 101 (47), pp. 16448-53.

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Gene duplication and fusion events that multiply and link functional protein domains are crucial mechanisms of enzyme evolution. The analysis of amino acid sequences and three-dimensional structures suggested that the (betaalpha)8-barrel, which is the most frequent fold among enzymes, has evolved by the duplication, fusion, and mixing of (betaalpha)4-half-barrel domains. Here, we mimicked this ...


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Item type:Article
Institutions:Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie > Prof. Dr. Reinhard Sterner
Identification Number:
11801240PubMed ID
Aldose-Ketose Isomerases/metabolismMESH
Base SequenceMESH
Cloning, MolecularMESH
DNA, Bacterial/geneticsMESH
Evolution, MolecularMESH
Gene DuplicationMESH
Genes, BacterialMESH
Models, MolecularMESH
Protein Structure, SecondaryMESH
Recombinant Proteins/metabolismMESH
Thermotoga maritima/geneticsMESH
Dewey Decimal Classification:500 Science > 570 Life sciences
Refereed:Yes, this version has been refereed
Created at the University of Regensburg:Yes
Item ID:13679
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