Stretching exercises — flexibility in dihydrofolate reductase catalysis
نویسندگان
چکیده
منابع مشابه
Unraveling the role of protein dynamics in dihydrofolate reductase catalysis.
Protein dynamics have controversially been proposed to be at the heart of enzyme catalysis, but identification and analysis of dynamical effects in enzyme-catalyzed reactions have proved very challenging. Here, we tackle this question by comparing an enzyme with its heavy ((15)N, (13)C, (2)H substituted) counterpart, providing a subtle probe of dynamics. The crucial hydride transfer step of the...
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DHFR (dihydrofolate reductase) catalyses the metabolically important reduction of 7,8-dihydrofolate by NADPH. DHFR from the hyperthermophilic bacterium Thermotoga maritima (TmDHFR), which shares similarity with DHFR from Escherichia coli, has previously been characterized structurally. Its tertiary structure is similar to that of DHFR from E. coli but it is the only DHFR characterized so far th...
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Dihydrofolate reductase (DHFR) is often used as a model system to study the relation between protein dynamics and catalysis. We have studied a number of variants of the cold-adapted DHFR from Moritella profunda (MpDHFR), in which the catalytically important M20 and FG loops have been altered, and present a comparison with the corresponding variants of the well-studied DHFR from Escherichia coli...
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This corrects the article DOI: 10.1038/srep42494.
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1 The binding of a series of amide derivatives of methotrexate to Lactobacillus casei dihydrofolate reductase has been studied by inhibition constant measurements and by 'H n.m.r. spectroscopy. 2 Amide modification of the a-carboxylate of methotrexate was found to prevent interaction of the y-carboxylate with the imidazole of His 28. 3 Estimates of the contributions to the binding energy from t...
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ژورنال
عنوان ژورنال: Chemistry & Biology
سال: 1998
ISSN: 1074-5521
DOI: 10.1016/s1074-5521(98)90616-0