Divergent evolution in enolase superfamily : strategies for assigning functions
Nature's strategies for evolving catalytic functions can be deciphered from the information contained in the rapidly expanding protein sequence databases. However, the functions of many proteins in the protein sequence and structure databases are either uncertain (too divergent to assign function based on homology) or unknown (no homologs), thereby limiting the utility of the databases. The mechanistically diverse enolase superfamily is a paradigm for understanding the structural bases for evolution of enzymatic function. We describe strategies for assigning functions to members of the enolase superfamily that should be applicable to other superfamilies.
Medienart: |
E-Artikel |
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Erscheinungsjahr: |
2012 |
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Erschienen: |
2012 |
Enthalten in: |
Zur Gesamtaufnahme - volume:287 |
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Enthalten in: |
The Journal of biological chemistry - 287(2012), 1 vom: 02. Jan., Seite 29-34 |
Sprache: |
Englisch |
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Beteiligte Personen: |
Gerlt, John A [VerfasserIn] |
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Links: |
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Themen: |
EC 4.2.1.11 |
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Anmerkungen: |
Date Completed 08.05.2012 Date Revised 21.10.2021 published: Print-Electronic Citation Status MEDLINE |
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doi: |
10.1074/jbc.R111.240945 |
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funding: |
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Förderinstitution / Projekttitel: |
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PPN (Katalog-ID): |
NLM212903071 |
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520 | |a Nature's strategies for evolving catalytic functions can be deciphered from the information contained in the rapidly expanding protein sequence databases. However, the functions of many proteins in the protein sequence and structure databases are either uncertain (too divergent to assign function based on homology) or unknown (no homologs), thereby limiting the utility of the databases. The mechanistically diverse enolase superfamily is a paradigm for understanding the structural bases for evolution of enzymatic function. We describe strategies for assigning functions to members of the enolase superfamily that should be applicable to other superfamilies | ||
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