Mechanisms of enzyme action and inhibition: Transition state analogues for acid-base catalysis

1986 ◽  
Vol 5 (2) ◽  
pp. 147-155 ◽  
Author(s):  
Richard Wolfenden ◽  
Lloyd Frick
Keyword(s):  
Transition State ◽  
Base Catalysis ◽  
Acid Base ◽  
Enzyme Action ◽  
Transition State Analogues

scholarly journals Transition State Charge Stabilization and Acid–Base Catalysis of mRNA Cleavage by the Endoribonuclease RelE

Biochemistry ◽  
2015 ◽  
Vol 54 (47) ◽  
pp. 7048-7057 ◽  
Author(s):  
Brian F. Dunican ◽  
David A. Hiller ◽  
Scott A. Strobel
Keyword(s):  
Transition State ◽  
Base Catalysis ◽  
Acid Base ◽  
Mrna Cleavage ◽  
State Charge ◽  
Charge Stabilization

scholarly journals Crystal Structures of Streptomyces Coelicolor Methylmalonyl-CoA Epimerase with Substrate or Transition State Analog Contradicts a Simple General Acid-Base Catalytic Mechanism

2021 ◽  
Author(s):  
Lee M Stunkard ◽  
Aaron B Benjamin ◽  
James Bower ◽  
Tyler Huth ◽  
Jeremy Lohman
Keyword(s):  
Transition State ◽  
Crystal Structures ◽  
Conformational Changes ◽  
Catalytic Mechanism ◽  
Streptomyces Coelicolor ◽  
Base Catalysis ◽  
Acid Base ◽  
Transition State Analog ◽  
Catalytic Residues ◽  
General Acid

Crystal structures of Streptomyces coelicolor methylmalonyl-CoA epimerase in the holo-form, with substrate or the putative transition state analog, 2-nitroproionyl-CoA. The proposed catalytic mechanism is general acid-base catalysis. The proposed catalytic residues are too far from the substrate or analog, unless conformational changes take place or some other mechanism is used. <br>

Do Enzymes Change the Nature of Transition States? Mapping the Transition State for General Acid−Base Catalysis of a Serine Protease‡

Biochemistry ◽  
2003 ◽  
Vol 42 (36) ◽  
pp. 10545-10553 ◽  
Author(s):  
Richard R. Bott ◽  
Gina Chan ◽  
Blanca Domingo ◽  
Grant Ganshaw ◽  
Constance Y. Hsia ◽  
...  
Keyword(s):  
Transition State ◽  
Serine Protease ◽  
Transition States ◽  
Base Catalysis ◽  
Acid Base ◽  
General Acid

scholarly journals Crystal Structures of Streptomyces Coelicolor Methylmalonyl-CoA Epimerase with Substrate or Transition State Analog Contradicts a Simple General Acid-Base Catalytic Mechanism

2021 ◽  
Author(s):  
Lee M Stunkard ◽  
Aaron B Benjamin ◽  
James Bower ◽  
Tyler Huth ◽  
Jeremy Lohman
Keyword(s):  
Transition State ◽  
Crystal Structures ◽  
Conformational Changes ◽  
Catalytic Mechanism ◽  
Streptomyces Coelicolor ◽  
Base Catalysis ◽  
Acid Base ◽  
Transition State Analog ◽  
Catalytic Residues ◽  
General Acid

Crystal structures of Streptomyces coelicolor methylmalonyl-CoA epimerase in the holo-form, with substrate or the putative transition state analog, 2-nitroproionyl-CoA. The proposed catalytic mechanism is general acid-base catalysis. The proposed catalytic residues are too far from the substrate or analog, unless conformational changes take place or some other mechanism is used. <br>

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