Converting Transaldolase into Aldolase through Swapping of the Multifunctional Acid–Base Catalyst: Common and Divergent Catalytic Principles in F6P Aldolase and Transaldolase-Reference-Cited by-同舟云学术

Converting Transaldolase into Aldolase through Swapping of the Multifunctional Acid–Base Catalyst: Common and Divergent Catalytic Principles in F6P Aldolase and Transaldolase

Published:2015-07-20 Issue:29 Volume:54 Page:4475-4486
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Sautner Viktor¹,Friedrich Mascha Miriam¹,Lehwess-Litzmann Anja¹,Tittmann Kai¹

Affiliation:

1. Göttingen Center for Molecular Biosciences, Department of Molecular Enzymology, Georg-August University Göttingen, Ernst-Caspari-Haus, Justus-von-Liebig-Weg 11, D-37077 Göttingen, Germany

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.biochem.5b00283

Reference33 articles.

1. ON THE NATURE OF THE TRANSLDOLASE-DIHYDROXYACETONE COMPLEX

2. Fructose-6-phosphate Aldolase Is a Novel Class I Aldolase from Escherichia coli and Is Related to a Novel Group of Bacterial Transaldolases

3. Sweet siblings with different faces: The mechanisms of FBP and F6P aldolase, transaldolase, transketolase and phosphoketolase revisited in light of recent structural data

4. Crystal Structure of Decameric Fructose-6-Phosphate Aldolase from Escherichia coli Reveals Inter-subunit Helix Swapping as a Structural Basis for Assembly Differences in the Transaldolase Family

5. Twisted Schiff base intermediates and substrate locale revise transaldolase mechanism

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