Functional role for Tyr 31 in the catalytic cycle of chicken dihydrofolate reductase

2003 ◽  
Vol 51 (2) ◽  
pp. 216-223 ◽  
Author(s):  
Paul Shrimpton ◽  
Alex Mullaney ◽  
Rudolf K. Allemann
Keyword(s):  
Dihydrofolate Reductase ◽  
Functional Role ◽  
Catalytic Cycle

Kinetic investigation of the functional role of phenylalanine-31 of recombinant human dihydrofolate reductase

Biochemistry ◽  
1990 ◽  
Vol 29 (27) ◽  
pp. 6428-6436 ◽  
Author(s):  
Jiu Tsair Tsay ◽  
James R. Appleman ◽  
William A. Beard ◽  
Neal J. Prendergast ◽  
Tavner J. Delcamp ◽  
...  
Keyword(s):  
Dihydrofolate Reductase ◽  
Functional Role ◽  
Kinetic Investigation ◽  
Human Dihydrofolate Reductase

scholarly journals Protein motions and dynamic effects in enzyme catalysis

2015 ◽  
Vol 17 (46) ◽  
pp. 30817-30827 ◽  
Author(s):  
Louis Y. P. Luk ◽  
E. Joel Loveridge ◽  
Rudolf K. Allemann
Keyword(s):  
Dihydrofolate Reductase ◽  
Enzyme Catalysis ◽  
Catalytic Cycle ◽  
Dynamic Effects ◽  
Dynamic Coupling ◽  
Protein Motions ◽  
Catalytic Power

While the full catalytic power of dihydrofolate reductase depends on finely tuning protein motions in each step of the catalytic cycle, dynamic coupling to the actual chemical step is detrimental to catalysis.

Investigation of the functional role of tryptophan-22 in Escherichia coli dihydrofolate reductase by site-directed mutagenesis

Biochemistry ◽  
1991 ◽  
Vol 30 (46) ◽  
pp. 11092-11103 ◽  
Author(s):  
Mark S. Warren ◽  
Katherine A. Brown ◽  
Martin F. Farnum ◽  
Elizabeth E. Howell ◽  
Joseph Kraut
Keyword(s):  
Escherichia Coli ◽  
Dihydrofolate Reductase ◽  
Functional Role ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis

Conformational Changes in the Active Site Loops of Dihydrofolate Reductase during the Catalytic Cycle†

Biochemistry ◽  
2004 ◽  
Vol 43 (51) ◽  
pp. 16046-16055 ◽  
Author(s):  
Rani P. Venkitakrishnan ◽  
Eduardo Zaborowski ◽  
Dan McElheny ◽  
Stephen J. Benkovic ◽  
H. Jane Dyson ◽  
...  
Keyword(s):  
Dihydrofolate Reductase ◽  
Conformational Changes ◽  
Active Site ◽  
Catalytic Cycle

Probing the functional role of phenylalanine-31 of Escherichia coli dihydrofolate reductase by site-directed mutagenesis

Biochemistry ◽  
1987 ◽  
Vol 26 (13) ◽  
pp. 4093-4100 ◽  
Author(s):  
Jin Tann Chen ◽  
Kazunari Taira ◽  
Chen Pei D. Tu ◽  
Stephen J. Benkovic
Keyword(s):  
Escherichia Coli ◽  
Dihydrofolate Reductase ◽  
Functional Role ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis

scholarly journals Conformational Changes in the Active Site Loops of Dihydrofolate Reductase during the Catalytic Cycle

Biochemistry ◽  
2005 ◽  
Vol 44 (15) ◽  
pp. 5948-5948 ◽  
Author(s):  
Rani P. Venkitakrishnan ◽  
Eduardo Zaborowski ◽  
Dan McElheny ◽  
Stephen J. Benkovic ◽  
H. Jane Dyson ◽  
...  
Keyword(s):  
Dihydrofolate Reductase ◽  
Conformational Changes ◽  
Active Site ◽  
Catalytic Cycle

Conformational changes in the catalytic cycle of protochlorophyllide oxidoreductase: what lessons can be learnt from dihydrofolate reductase?

2009 ◽  
Vol 37 (2) ◽  
pp. 354-357 ◽  
Author(s):  
Derren J. Heyes ◽  
Nigel S. Scrutton
Keyword(s):  
Dihydrofolate Reductase ◽  
Conformational Changes ◽  
Catalytic Mechanism ◽  
Structural Information ◽  
Chlorophyll Biosynthesis ◽  
Catalytic Cycle ◽  
Protochlorophyllide Oxidoreductase ◽  
Protein Motions ◽  
Kinetic Information ◽  
Related Enzyme

In chlorophyll biosynthesis, the light-activated enzyme, POR (protochlorophyllide oxidoreductase), has been shown to be an excellent model system for studying the role of protein motions during catalysis. The catalytic cycle of POR is understood in detail and comprises an initial photochemical reaction, which is followed by a number of ‘dark’ steps. The latter steps in the reaction cycle have been shown to involve a series of ordered product release and substrate rebinding events and are known to require conformational changes in the protein in order to proceed. However, owing to the current lack of any structural information on the enzyme, the nature of these conformational rearrangements remains poorly understood. By contrast, there is a wealth of structural and kinetic information available on the closely related enzyme dihydrofolate reductase, which is known to have a similar catalytic mechanism to POR. Dihydrofolate reductase is able to adopt an ‘occluded’ and a ‘closed’ structure, depending on which ligand is bound in the active site, and as a result, the catalytic cycle is controlled by a ‘switching’ between these two conformations. By analogy, we suggest that a similar cycling between different conformations may be operating in POR.

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