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• W2891940234 endingPage "21" @default.
• W2891940234 startingPage "1" @default.
• W2891940234 abstract "X-ray and neutron crystallography are powerful techniques utilized to study the structures of biomolecules. Visualization of enzymes in complex with substrate/product and the capture of intermediate states can be related to activity to facilitate understanding of the catalytic mechanism. Subsequent analysis of small molecule binding within the enzyme active site provides insight into mechanisms of inhibition, supporting the design of novel inhibitors using a structure-guided approach. The first X-ray crystal structures were determined for small, ubiquitous enzymes such as carbonic anhydrase (CA). CAs are a family of zinc metalloenzymes that catalyze the hydration of CO 2 , producing<mml:math xmlns:mml=http://www.w3.org/1998/Math/MathML id=M1><mml:mi mathvariant=normal>H</mml:mi><mml:mi mathvariant=normal>C</mml:mi><mml:msup><mml:mrow><mml:msub><mml:mrow><mml:mi mathvariant=normal>O</mml:mi></mml:mrow><mml:mrow><mml:mn mathvariant=normal>3</mml:mn></mml:mrow></mml:msub></mml:mrow><mml:mrow><mml:mo>-</mml:mo></mml:mrow></mml:msup></mml:math>and a proton. The CA structure and ping-pong mechanism have been extensively studied and are well understood. Though the function of CA plays an important role in a variety of physiological functions, CA has also been associated with diseases such as glaucoma, edema, epilepsy, obesity, and cancer and is therefore recognized as a drug target. In this review, a brief history of crystallography and its impact on CA research is discussed." @default.
• W2891940234 created "2018-09-27" @default.
• W2891940234 creator A5003958981 @default.
• W2891940234 creator A5054738613 @default.
• W2891940234 creator A5079118082 @default.
• W2891940234 date "2018-09-13" @default.
• W2891940234 modified "2023-10-07" @default.
• W2891940234 title "Crystallography and Its Impact on Carbonic Anhydrase Research" @default.
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