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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U2 - 10.1074/jbc.R111.240945
DO - 10.1074/jbc.R111.240945
M3 - Short survey
C2 - 22069326
AN - SCOPUS:84855286291
SN - 0021-9258
VL - 287
SP - 29
EP - 34
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 1
ER -