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

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

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

scholarly journals Role of aspartate 27 of dihydrofolate reductase from Escherichia coli in interconversion of active and inactive enzyme conformers and binding of NADPH.

1990 ◽  
Vol 265 (10) ◽  
pp. 5579-5584
Author(s):  
J R Appleman ◽  
E E Howell ◽  
J Kraut ◽  
R L Blakley
Keyword(s):  
Escherichia Coli ◽  
Dihydrofolate Reductase

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

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

Role of MetR and PurR in the activation ofglyAby CsgD inEscherichia coliK-12

2004 ◽  
Vol 50 (9) ◽  
pp. 683-690 ◽  
Author(s):  
Neema T Chirwa ◽  
Muriel B Herrington
Keyword(s):  
Escherichia Coli ◽  
Dihydrofolate Reductase ◽  
Biofilm Formation ◽  
Serine Hydroxymethyltransferase ◽  
Regulatory Proteins ◽  
Multicopy Plasmid ◽  
Glya Gene

The csgD gene of Escherichia coli is required for the expression of curli fibres, surface fibres that are important for biofilm formation and infection. Previously, we demonstrated that expression of CsgD from a multicopy plasmid increased expression of the glyA gene, which codes for serine hydroxymethyltransferase. We show here that this activation requires the participation of both known regulatory proteins, MetR and PurR. The adjacent divergently transcribed gene hmp was weakly induced by CsgD, but its induction did not require MetR or PurR. The effect of CsgD on the expression of several pur and met genes was also tested.Key words: curli, regulation, serine hydroxymethyltransferase, Hmp, one-carbon, dihydrofolate reductase, MetR, PurR.

scholarly journals Dihydrofolate reductase as a model for studies of enzyme dynamics and catalysis

F1000Research ◽  
2015 ◽  
Vol 4 ◽  
pp. 1464 ◽  
Author(s):  
Amnon Kohen
Keyword(s):  
Escherichia Coli ◽  
Protein Dynamics ◽  
Dihydrofolate Reductase ◽  
Enzyme Catalysis ◽  
Kinetic Studies ◽  
Model System ◽  
Enzyme Kinetic ◽  
Enzyme Dynamics ◽  
Potential Use

Dihydrofolate reductase fromEscherichia coli(ecDHFR) serves as a model system for investigating the role of protein dynamics in enzyme catalysis. We discuss calculations predicting a network of dynamic motions that is coupled to the chemical step catalyzed by this enzyme. Kinetic studies testing these predictions are presented, and their potential use in better understanding the role of these dynamics in enzyme catalysis is considered. The cumulative results implicate motions across the entire protein in catalysis.

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