Protein Engineering of Dihydrofolate Reductase. pH Dependency of Phe-31 Mutants
Author:
Publisher
The Chemical Society of Japan
Subject
General Chemistry
Link
https://www.jstage.jst.go.jp/article/bcsj1926/60/8/60_8_3025/_pdf
Reference9 articles.
1. Site-specific mutagenesis of dihydrofolate reductase fromEscherichia coli
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4. Crystal structures of Escherichia coli and Lactobacillus casei dihydrofolate reductase refined at 1.7 A resolution. I. General features and binding of methotrexate.
5. Crystal structures of Escherichia coli and Lactobacillus casei dihydrofolate reductase refined at 1.7 A resolution. II. Environment of bound NADPH and implications for catalysis.
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1. Eukaryotic Dihydrofolate Reductase;Advances in Enzymology - and Related Areas of Molecular Biology;2006-11-22
2. Engineering Specificity for Folate into Dihydrofolate Reductase from Escherichia coli;Biochemistry;1996-01-01
3. Role of the Active-Site Carboxylate in Dihydrofolate Reductase: Kinetic and Spectroscopic Studies of the Aspartate 26 .fwdarw. Asparagine Mutant of the Lactobacillus casei Enzyme;Biochemistry;1995-03-07
4. Nonadditivity of mutational effects at the folate binding site of Escherichia coli dihydrofolate reductase;Biochemistry;1994-09-27
5. 13C and 15N Nuclear Magnetic Resonance Evidence That the Active Site Carboxyl Group of Dihydrofolate Reductase Is Not Involved in the Relay of a Proton to Substrate;Archives of Biochemistry and Biophysics;1993-11
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