TY - JOUR
T1 - Mechanistically diverse enzyme superfamilies
T2 - The importance of chemistry in the evolution of catalysis
AU - Gerlt, John A.
AU - Babbitt, Patricia C.
N1 - Funding Information:
The authors would like to thank the National Institutes of Health (grant numbers GM-40570 and GM-52594) for financial support of their work in the study of enzyme superf:amilies.
PY - 1998
Y1 - 1998
N2 - The strategy that nature has used to evolve new catalytic activities from pre-existing enzymes (i.e. retention of substrate binding or of catalytic mechanism) has been controversial. Recent work supports a strategy in which a partial reaction, catalyzed by a progenitor, is retained, and the active-site architecture is modified to allow the intermediate generated to be directed to different products.
AB - The strategy that nature has used to evolve new catalytic activities from pre-existing enzymes (i.e. retention of substrate binding or of catalytic mechanism) has been controversial. Recent work supports a strategy in which a partial reaction, catalyzed by a progenitor, is retained, and the active-site architecture is modified to allow the intermediate generated to be directed to different products.
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U2 - 10.1016/S1367-5931(98)80091-4
DO - 10.1016/S1367-5931(98)80091-4
M3 - Article
C2 - 9818186
AN - SCOPUS:0032176603
SN - 1367-5931
VL - 2
SP - 607
EP - 612
JO - Current Opinion in Chemical Biology
JF - Current Opinion in Chemical Biology
IS - 5
ER -