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A common evolutionary origin of two elementary enzyme folds.

Höcker, Birte and Schmidt, Steffen and Sterner, Reinhard (2002) A common evolutionary origin of two elementary enzyme folds. FEBS letters 510 (3), pp. 133-5.

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Abstract

The (beta alpha)(8)-barrel is the most frequent and most versatile fold among enzymes [Höcker et al., Curr. Opin. Biotechnol. 12 (2001) 376-381; Wierenga, FEBS Lett. 492 (2001) 193-198]. Structural and functional evidence suggests that (beta alpha)(8)-barrels evolved from an ancestral half-barrel, which consisted of four (beta alpha) units stabilized by dimerization [Lang et al., Science 289 ...

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Item Type:Article
Date:2002
Institutions:Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie > Prof. Dr. Reinhard Sterner
Identification Number:
ValueType
11801240PubMed ID
Classification:
NotationType
Computational BiologyMESH
Databases, ProteinMESH
Enzymes/physiologyMESH
Escherichia coliMESH
Evolution, MolecularMESH
Flavodoxin/chemistryMESH
Models, MolecularMESH
PropionibacteriumMESH
Protein FoldingMESH
Sequence Homology, Amino AcidMESH
Structure-Activity RelationshipMESH
Thermotoga maritimaMESH
Subjects:500 Science > 570 Life sciences
Status:Published
Refereed:Yes, this version has been refereed
Created at the University of Regensburg:Yes
Owner: Universitätsbibliothek Regensburg
Deposited On:22 Mar 2010 08:37
Last Modified:22 Mar 2010 08:37
Item ID:13693
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