Three-dimensional structure of apotransketolase flexible loops at the active site enable cofactor binding
Author:
Publisher
Wiley
Subject
Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1016/0014-5793(92)81197-T/fullpdf
Reference10 articles.
1. Enzymes of pentose biosynthesis. The quaternary structure and reacting form of transketolase from baker's yeast
2. Three-dimensional structure of transketolase, a thiamine diphosphate dependent enzyme, at 2.5 A resolution.
3. The catalytic mechanism of transketolase. Thiamin pyrophosphate-derived transition states for transketolase and pyruvate dehydrogenase are not identical.
4. CRYSTALLINE TRANSKETOLASE FROM BAKERS' YEAST: ISOLATION AND PROPERTIES
5. Preliminary Crystallographic Data for Transketolase from Yeast
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5. Biophysical characterization of the inactivation of E. coli transketolase by aqueous co-solvents;2020-06-10
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