Energetically most likely substrate and active-site protonation sites and pathways in the catalytic mechanism of dihydrofolate reductase

scientific article published in April 2001

Energetically most likely substrate and active-site protonation sites and pathways in the catalytic mechanism of dihydrofolate reductase is …
instance of (P31):
scholarly articleQ13442814

External links are
P356DOI10.1021/JA0038474
P8608Fatcat IDrelease_ijpyn3pmsfhznewe25sqdpvbyu
P698PubMed publication ID11472112

P2093author name stringGready JE
Cummins PL
P433issue15
P407language of work or nameEnglishQ1860
P304page(s)3418-3428
P577publication date2001-04-01
P1433published inJournal of the American Chemical SocietyQ898902
P1476titleEnergetically most likely substrate and active-site protonation sites and pathways in the catalytic mechanism of dihydrofolate reductase
P478volume123

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cites work (P2860)
Q42041846Conformational change of the methionine 20 loop of Escherichia coli dihydrofolate reductase modulates pKa of the bound dihydrofolate
Q43228792Coupling of protein motions and hydrogen transfer during catalysis by Escherichia coli dihydrofolate reductase
Q27649179Crystal Structure of a Type II Dihydrofolate Reductase Catalytic Ternary Complex †
Q44356449Importance of substrate and cofactor polarization in the active site of dihydrofolate reductase
Q24531161Network of coupled promoting motions in enzyme catalysis
Q30389387Preliminary joint X-ray and neutron protein crystallographic studies of ecDHFR complexed with folate and NADP+.
Q34587682Preorganization and protein dynamics in enzyme catalysis
Q51527441Reduction potentials and acidity constants of Mn superoxide dismutase calculated by QM/MM free-energy methods.
Q34129428Role of water in the catalytic cycle of E. coli dihydrofolate reductase
Q36090362Searching sequence space: two different approaches to dihydrofolate reductase catalysis
Q27640788Structural and Kinetic Evidence for an Extended Hydrogen-bonding Network in Catalysis of Methyl Group Transfer: ROLE OF AN ACTIVE SITE ASPARAGINE RESIDUE IN ACTIVATION OF METHYL TRANSFER BY METHYLTRANSFERASES
Q57964414The search for new DHFR inhibitors: a review of patents, January 2001 – February 2005
Q30301213Toward resolving the catalytic mechanism of dihydrofolate reductase using neutron and ultrahigh-resolution X-ray crystallography

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