Functional role of a mobile loop of Escherichia coli dihydrofolate reductase in transition-state stabilization

Biochemistry ◽  
1992 ◽  
Vol 31 (34) ◽  
pp. 7826-7833 ◽  
Author(s):  
Luyuan Li ◽  
Peter E. Wright ◽  
Stephen J. Benkovic ◽  
Christopher J. Falzone
Keyword(s):  
Escherichia Coli ◽  
Transition State ◽  
Dihydrofolate Reductase ◽  
Functional Role ◽  
Transition State Stabilization

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

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 Role of aspartate 27 in the binding of methotrexate to dihydrofolate reductase from Escherichia coli.

1988 ◽  
Vol 263 (19) ◽  
pp. 9187-9198 ◽  
Author(s):  
J R Appleman ◽  
E E Howell ◽  
J Kraut ◽  
M Kühl ◽  
R L Blakley
Keyword(s):  
Escherichia Coli ◽  
Dihydrofolate Reductase

Sequence Perturbation Analysis: Addressing Amino Acid Indices to Elucidate the C-Terminal Role of Escherichia Coli Dihydrofolate Reductase

2009 ◽  
Vol 145 (6) ◽  
pp. 751-762 ◽  
Author(s):  
Hisashi Takahashi ◽  
Akiko Yokota ◽  
Tatsuyuki Takenawa ◽  
Masahiro Iwakura
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Dihydrofolate Reductase ◽  
Perturbation Analysis ◽  
Amino Acid Indices

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

Functional tyrosine residue in the active center of human dipeptidyl peptidase III

2008 ◽  
Vol 389 (2) ◽  
pp. 163-167 ◽  
Author(s):  
Branka Salopek-Sondi ◽  
Bojana Vukelić ◽  
Jasminka Špoljarić ◽  
Šumski Šimaga ◽  
Dušica Vujaklija ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Transition State ◽  
Active Site ◽  
Functional Role ◽  
Dipeptidyl Peptidase ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis ◽  
Tyrosine Residue ◽  
Transition State Stabilization ◽  
Endogenous Defense

Abstract Human dipeptidyl peptidase III (DPP III) is a member of the metallopeptidase family M49 with an implied role in the pain-modulatory system and endogenous defense against oxidative stress. Here, we report the heterologous expression of human DPP III and the site-directed mutagenesis results which demonstrate a functional role for Tyr318 at the active site of this enzyme. The substitution of Tyr318 to Phe decreased k cat by two orders of magnitude without altering the binding affinity of substrate, or of a competitive hydroxamate inhibitor designed to interact with S1 and S2 subsites. The results indicate that the conserved tyrosine could be involved in transition state stabilization during the catalytic action of M49 peptidases.

Dihydrofolate reductase from Escherichia coli: probing the role of aspartate-27 and phenylalanine-137 in enzyme conformation and the binding of NADPH

Biochemistry ◽  
1990 ◽  
Vol 29 (37) ◽  
pp. 8569-8576 ◽  
Author(s):  
Susan M. J. Dunn ◽  
Thomas M. Lanigan ◽  
Elizabeth E. Howell
Keyword(s):  
Escherichia Coli ◽  
Dihydrofolate Reductase
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