Triosephosphate isomerase: the perfect enzyme, but how does it work?
Author:
Publisher
International Union of Crystallography (IUCr)
Subject
Condensed Matter Physics,General Materials Science,Biochemistry,General Chemistry
Link
http://journals.iucr.org/m/issues/2021/04/00/me6138/me6138.pdf
Reference10 articles.
1. Structural studies show that the A178L mutation in the C-terminal hinge of the catalytic loop-6 of triosephosphate isomerase (TIM) induces a closed-like conformation in dimeric and monomeric TIM
2. Atomic resolution crystallography of a complex of triosephosphate isomerase with a reaction-intermediate analog: New insight in the proton transfer reaction mechanism
3. On the three-dimensional structure and catalytic mechanism of triose phosphate isomerase
4. Structure of chicken muscle triose phosphate isomerase determined crystallographically at 2.5Å resolution: using amino acid sequence data
5. Neutron structures of Leishmania mexicana triosephosphate isomerase in complex with reaction-intermediate mimics shed light on the proton-shuttling steps
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