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Title: The inner workings of an enzyme
Predictive understanding for how a particular amino acid sequence encodes enzymatic function is a grand challenge in molecular biology, with profound impacts in fields ranging from industrial biotechnology, computational protein design, and agriculture to predictive identification of disease mutations ( 1 ) and medicinal chemistry. Innovative methods for high-throughput and quantitative measurements of different aspects of enzymatic function are needed to achieve this goal. On page 411 of this issue, Markin et al. ( 2 ) describe a laboratory-on-a-chip platform called High-Throughput Microfluidic Enzyme Kinetics (HT-MEK) as a step in this direction. The technique allows high-fidelity in vitro biochemical and biophysical characterization of more than 1000 mutants of the model enzyme PafA (phosphate-irrepressible alkaline phosphatase of Flavobacterium). HT-MEK identifies partially overlapping yet distinct networks of amino acids that undergird individual reaction steps of PafA, illuminating the mechanistic basis of catalysis for this enzyme.  more » « less
Award ID(s):
2030221
PAR ID:
10345161
Author(s) / Creator(s):
;
Date Published:
Journal Name:
Science
Volume:
373
Issue:
6553
ISSN:
0036-8075
Page Range / eLocation ID:
391 to 392
Format(s):
Medium: X
Sponsoring Org:
National Science Foundation
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