Neutron crystallographic studies of carbonic anhydrase

Neutron crystallographic studies of carbonic anhydrase

The carbonic anhydrases (CAs; EC 4.2.1.1) are a family of metalloenzymes that catalyze the reversible hydration of carbon dioxide (CO ) and bicarbonate (HCO ). Since their discovery in 1933, CAs have been at the forefront of scientific discovery: the understanding of enzymatic reactions, structural...

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Veröffentlicht in:Methods in enzymology 2020, Vol.634, p.281-309
Hauptverfasser: Combs, Jacob E, Andring, Jacob T, McKenna, Robert
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description The carbonic anhydrases (CAs; EC 4.2.1.1) are a family of metalloenzymes that catalyze the reversible hydration of carbon dioxide (CO ) and bicarbonate (HCO ). Since their discovery in 1933, CAs have been at the forefront of scientific discovery: the understanding of enzymatic reactions, structural biology, molecular dynamics, drug discovery, and clinical medicine. These ubiquitous enzymes equilibrate the reaction between CO , HCO , and protons. Hence, CAs have important roles in ion transport, acid-base regulation, gas exchange, photosynthesis, and CO fixation. In this chapter, we describe the protocols leading to, and the analysis of CA neutron crystal structures. This accumulation of structural knowledge adds to our understanding of the enzymatic mechanism and development of CA inhibitors.
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