Abstract
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.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 29-34 |
| Number of pages | 6 |
| Journal | Journal of Biological Chemistry |
| Volume | 287 |
| Issue number | 1 |
| DOIs | |
| State | Published - Jan 2 2012 |
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ASJC Scopus subject areas
- Biochemistry
- Cell Biology
- Molecular Biology
Cite this
Divergent evolution in enolase superfamily : Strategies for assigning functions. / Gerlt, John A.; Babbitt, Patricia C.; Jacobson, Matthew P.; Almo, Steven C.
In: Journal of Biological Chemistry, Vol. 287, No. 1, 02.01.2012, p. 29-34.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Divergent evolution in enolase superfamily
T2 - Strategies for assigning functions
AU - Gerlt, John A.
AU - Babbitt, Patricia C.
AU - Jacobson, Matthew P.
AU - Almo, Steven C.
PY - 2012/1/2
Y1 - 2012/1/2
N2 - 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.
AB - 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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UR - http://www.scopus.com/inward/citedby.url?scp=84855286291&partnerID=8YFLogxK
U2 - 10.1074/jbc.R111.240945
DO - 10.1074/jbc.R111.240945
M3 - Article
VL - 287
SP - 29
EP - 34
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
SN - 0021-9258
IS - 1
ER -