PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 25453083-1 2014 Dihydrofolate reductase (DHFR) catalyzes the NADPH-dependent reduction of dihydrofolate (DHF) to tetrahydrofolate (THF). dihydrofolate 74-87 Dihydrofolate reductase Escherichia coli 0-23 25453083-1 2014 Dihydrofolate reductase (DHFR) catalyzes the NADPH-dependent reduction of dihydrofolate (DHF) to tetrahydrofolate (THF). dihydrofolate 74-87 Dihydrofolate reductase Escherichia coli 25-29 25453083-1 2014 Dihydrofolate reductase (DHFR) catalyzes the NADPH-dependent reduction of dihydrofolate (DHF) to tetrahydrofolate (THF). dihydrofolate 25-28 Dihydrofolate reductase Escherichia coli 0-23 24517487-1 2014 A weak association between osmolytes and dihydrofolate (DHF) decreases the affinity of the substrate for the Escherichia coli chromosomal and R67 plasmid dihydrofolate reductase (DHFR) enzymes. dihydrofolate 41-54 Dihydrofolate reductase Escherichia coli 154-177 24517487-1 2014 A weak association between osmolytes and dihydrofolate (DHF) decreases the affinity of the substrate for the Escherichia coli chromosomal and R67 plasmid dihydrofolate reductase (DHFR) enzymes. dihydrofolate 41-54 Dihydrofolate reductase Escherichia coli 179-183 24517487-1 2014 A weak association between osmolytes and dihydrofolate (DHF) decreases the affinity of the substrate for the Escherichia coli chromosomal and R67 plasmid dihydrofolate reductase (DHFR) enzymes. dihydrofolate 56-59 Dihydrofolate reductase Escherichia coli 154-177 24517487-1 2014 A weak association between osmolytes and dihydrofolate (DHF) decreases the affinity of the substrate for the Escherichia coli chromosomal and R67 plasmid dihydrofolate reductase (DHFR) enzymes. dihydrofolate 56-59 Dihydrofolate reductase Escherichia coli 179-183 12862454-1 2003 Dihydrofolate Reductase (DHFR) catalyzes the reduction of dihydrofolate (H2F) to tetrahydrofolate. dihydrofolate 58-71 Dihydrofolate reductase Escherichia coli 0-23 23420416-4 2013 The linkage between protein motions and catalysis is investigated in the context of a model enzyme, E. coli dihydrofolate reductase (DHFR), that catalyzes the hydride transfer reaction in the conversion of dihydrofolate to tetrahydrofolate. dihydrofolate 108-121 Dihydrofolate reductase Escherichia coli 133-137 18724364-5 2008 Instead, it arises from accumulation of DHFR"s substrate dihydrofolate, which we show is a potent FP-gamma-GS inhibitor. dihydrofolate 57-70 Dihydrofolate reductase Escherichia coli 40-44 12765545-1 2003 DHFR (dihydrofolate reductase) catalyses the metabolically important reduction of 7,8-dihydrofolate by NADPH. dihydrofolate 82-99 Dihydrofolate reductase Escherichia coli 0-4 12765545-1 2003 DHFR (dihydrofolate reductase) catalyses the metabolically important reduction of 7,8-dihydrofolate by NADPH. dihydrofolate 82-99 Dihydrofolate reductase Escherichia coli 6-29 12852950-3 2003 Secondary screening of these revealed twelve molecules that were competitive with dihydrofolate, nine of which have not been previously characterized as inhibitors of dihydrofolate reductase. dihydrofolate 82-95 Dihydrofolate reductase Escherichia coli 167-190 17916364-1 2007 Escherichia coli dihydrofolate reductase (DHFR) catalyzes the reduction of dihydrofolate to tetrahydrofolate. dihydrofolate 17-30 Dihydrofolate reductase Escherichia coli 42-46 16241906-1 2006 The enzyme DHFR (dihydrofolate reductase) catalyses hydride transfer from NADPH to, and protonation of, dihydrofolate. dihydrofolate 17-30 Dihydrofolate reductase Escherichia coli 11-15 15726569-3 2005 Using the semiempirical PM3 method to model the QM region, the application of this PQA/MM method is illustrated by calculation of the relative protonation free energy of the conserved OD2 (Asp27) and the N5 (dihydrofolate) proton acceptor sites in the active site of Escherichia coli dihydrofolate reductase (DHFR) with the bound nicotinamide adenine dinucleotide phosphate (NADPH) cofactor. dihydrofolate 208-221 Dihydrofolate reductase Escherichia coli 284-307 15726569-3 2005 Using the semiempirical PM3 method to model the QM region, the application of this PQA/MM method is illustrated by calculation of the relative protonation free energy of the conserved OD2 (Asp27) and the N5 (dihydrofolate) proton acceptor sites in the active site of Escherichia coli dihydrofolate reductase (DHFR) with the bound nicotinamide adenine dinucleotide phosphate (NADPH) cofactor. dihydrofolate 208-221 Dihydrofolate reductase Escherichia coli 309-313 15609999-5 2004 Spectra were recorded for binary and ternary complexes of wild-type DHFR bound to the substrate dihydrofolate (DHF), the product tetrahydrofolate (THF), the pseudosubstrate folate, reduced and oxidized NADPH cofactor, and the inactive cofactor analogue 5,6-dihydroNADPH. dihydrofolate 96-109 Dihydrofolate reductase Escherichia coli 68-72 15213241-1 2004 To address the effects of ligand binding on the structural fluctuations of Escherichia coli dihydrofolate reductase (DHFR), the hydrogen/deuterium (H/D) exchange kinetics of its binary and ternary complexes formed with various ligands (folate, dihydrofolate, tetrahydrofolate, NADPH, NADP(+), and methotrexate) were examined using electrospray ionization mass spectrometry. dihydrofolate 92-105 Dihydrofolate reductase Escherichia coli 117-121 12862454-1 2003 Dihydrofolate Reductase (DHFR) catalyzes the reduction of dihydrofolate (H2F) to tetrahydrofolate. dihydrofolate 58-71 Dihydrofolate reductase Escherichia coli 25-29 12756296-1 2003 Dihydrofolate reductase (DHFR) catalyzes the reduction of dihydrofolate to tetrahydrofolate. dihydrofolate 58-71 Dihydrofolate reductase Escherichia coli 0-23 12756296-1 2003 Dihydrofolate reductase (DHFR) catalyzes the reduction of dihydrofolate to tetrahydrofolate. dihydrofolate 58-71 Dihydrofolate reductase Escherichia coli 25-29 7011378-1 1981 Reduced nicotinamide adenine dinucleotide phosphate (NADPH), folate, dihydrofolate, and the inhibitors trimethoprim and methotrexate bind rapidly and reversibly to both dihydrofolate reductase isoenzymes isolated from Escherichia coli RT500. dihydrofolate 69-82 Dihydrofolate reductase Escherichia coli 169-192 8461309-4 1993 D27S+F153S and D27S+I155N DHFRs display 2-3-fold increases in kcat over D27S DHFR values, but only the F153S mutation decreases the Km for dihydrofolate by a factor of 2. dihydrofolate 139-152 Dihydrofolate reductase Escherichia coli 26-30 3275776-2 1988 A strictly conserved residue at the dihydrofolate binding site of DHFR, phenylalanine-31, has been replaced with tyrosine or valine to ascertain the importance for binding of this hydrophobic amino acid, which interacts with both the pteridine ring and the p-aminobenzoyl moiety. dihydrofolate 36-49 Dihydrofolate reductase Escherichia coli 66-70 12021443-1 2002 Dihydrofolate reductase (DHFR) catalyzes the nicotinamide adenine dinucleotide phosphate (NADPH)-dependent reduction of 7,8-dihydrofolate (H2F) to 5,6,7,8-tetrahydrofolate (H4F). dihydrofolate 120-137 Dihydrofolate reductase Escherichia coli 0-23 12021443-1 2002 Dihydrofolate reductase (DHFR) catalyzes the nicotinamide adenine dinucleotide phosphate (NADPH)-dependent reduction of 7,8-dihydrofolate (H2F) to 5,6,7,8-tetrahydrofolate (H4F). dihydrofolate 120-137 Dihydrofolate reductase Escherichia coli 25-29 11472112-1 2001 Despite much experimental and computational study, key aspects of the mechanism of reduction of dihydrofolate (DHF) by dihydrofolate reductase (DHFR) remain unresolved, while the secondary DHFR-catalyzed reduction of folate has been little studied. dihydrofolate 96-109 Dihydrofolate reductase Escherichia coli 119-142 11472112-1 2001 Despite much experimental and computational study, key aspects of the mechanism of reduction of dihydrofolate (DHF) by dihydrofolate reductase (DHFR) remain unresolved, while the secondary DHFR-catalyzed reduction of folate has been little studied. dihydrofolate 96-109 Dihydrofolate reductase Escherichia coli 144-148 11472112-1 2001 Despite much experimental and computational study, key aspects of the mechanism of reduction of dihydrofolate (DHF) by dihydrofolate reductase (DHFR) remain unresolved, while the secondary DHFR-catalyzed reduction of folate has been little studied. dihydrofolate 96-109 Dihydrofolate reductase Escherichia coli 189-193 11472112-1 2001 Despite much experimental and computational study, key aspects of the mechanism of reduction of dihydrofolate (DHF) by dihydrofolate reductase (DHFR) remain unresolved, while the secondary DHFR-catalyzed reduction of folate has been little studied. dihydrofolate 111-114 Dihydrofolate reductase Escherichia coli 119-142 11472112-1 2001 Despite much experimental and computational study, key aspects of the mechanism of reduction of dihydrofolate (DHF) by dihydrofolate reductase (DHFR) remain unresolved, while the secondary DHFR-catalyzed reduction of folate has been little studied. dihydrofolate 111-114 Dihydrofolate reductase Escherichia coli 144-148 11472112-1 2001 Despite much experimental and computational study, key aspects of the mechanism of reduction of dihydrofolate (DHF) by dihydrofolate reductase (DHFR) remain unresolved, while the secondary DHFR-catalyzed reduction of folate has been little studied. dihydrofolate 111-114 Dihydrofolate reductase Escherichia coli 189-193 8003467-0 1994 Determination by Raman spectroscopy of the pKa of N5 of dihydrofolate bound to dihydrofolate reductase: mechanistic implications. dihydrofolate 56-69 Dihydrofolate reductase Escherichia coli 79-102 8003467-1 1994 Dihydrofolate reductase (DHFR) catalyzes the reduction of dihydrofolate (H2folate) to tetrahydrofolate by NADPH, and this requires that the pteridine ring be protonated at N5. dihydrofolate 58-71 Dihydrofolate reductase Escherichia coli 0-23 8003467-1 1994 Dihydrofolate reductase (DHFR) catalyzes the reduction of dihydrofolate (H2folate) to tetrahydrofolate by NADPH, and this requires that the pteridine ring be protonated at N5. dihydrofolate 58-71 Dihydrofolate reductase Escherichia coli 25-29 8003467-3 1994 We have determined the pKa of N5 of dihydrofolate in the Escherichia coli DHFR/NADP+/H2folate ternary complex by Raman difference spectroscopy and found that the value is 6.5. dihydrofolate 36-49 Dihydrofolate reductase Escherichia coli 74-78 1961697-1 1991 Escherichia coli dihydrofolate reductase (DHFR) carries a net charge of -10 electrons yet it binds ligands with net charges of -4 (NADPH) and -2 (folate or dihydrofolate). dihydrofolate 17-30 Dihydrofolate reductase Escherichia coli 42-46 2502633-6 1989 Those compounds that had basic substituents in the 2-position of the quinoline ring were also highly specific for bacterial dihydrofolate DHFR, relative to a vertebrate counterpart. dihydrofolate 124-137 Dihydrofolate reductase Escherichia coli 138-142 3052577-8 1988 As NADPH and dihydrofolate function as activators and as NADPH behaves as a sticky substrate, the kinetic mechanism of the dihydrofolate reductase reaction with the natural substrates is steady-state random. dihydrofolate 13-26 Dihydrofolate reductase Escherichia coli 123-146 30724552-1 2019 Dihydrofolate reductase (DHFR) reduces dihydrofolate (DHF) to tetrahydrofolate using NADPH as a cofactor. dihydrofolate 39-52 Dihydrofolate reductase Escherichia coli 0-23 30979096-1 2019 A class of gold(I) phosphane complexes have been identified as inhibitors of dihydrofolate reductase (DHFR) from E. coli, an enzyme that catalyzes the reduction of dihydrofolate (DHF) to tetrahydrofolate (THF), using NADPH as a coenzyme. dihydrofolate 77-90 Dihydrofolate reductase Escherichia coli 102-106 30979096-1 2019 A class of gold(I) phosphane complexes have been identified as inhibitors of dihydrofolate reductase (DHFR) from E. coli, an enzyme that catalyzes the reduction of dihydrofolate (DHF) to tetrahydrofolate (THF), using NADPH as a coenzyme. dihydrofolate 102-105 Dihydrofolate reductase Escherichia coli 77-100 30724552-1 2019 Dihydrofolate reductase (DHFR) reduces dihydrofolate (DHF) to tetrahydrofolate using NADPH as a cofactor. dihydrofolate 39-52 Dihydrofolate reductase Escherichia coli 25-29 30724552-1 2019 Dihydrofolate reductase (DHFR) reduces dihydrofolate (DHF) to tetrahydrofolate using NADPH as a cofactor. dihydrofolate 25-28 Dihydrofolate reductase Escherichia coli 0-23 30564747-1 2018 Dihydrofolate reductase (DHFR) catalyzes the stereospecific reduction of 7,8-dihydrofolate (FH2) to (6s)-5,6,7,8-tetrahydrofolate (FH4) via hydride transfer from NADPH. dihydrofolate 73-90 Dihydrofolate reductase Escherichia coli 0-23 30564747-1 2018 Dihydrofolate reductase (DHFR) catalyzes the stereospecific reduction of 7,8-dihydrofolate (FH2) to (6s)-5,6,7,8-tetrahydrofolate (FH4) via hydride transfer from NADPH. dihydrofolate 73-90 Dihydrofolate reductase Escherichia coli 25-29 30040418-1 2018 Dihydrofolate reductase (DHFR) catalyzes the reduction of dihydrofolate (DHF) to tetrahydrofolate (THF) in the presence of NADPH. dihydrofolate 58-71 Dihydrofolate reductase Escherichia coli 0-23 30040418-1 2018 Dihydrofolate reductase (DHFR) catalyzes the reduction of dihydrofolate (DHF) to tetrahydrofolate (THF) in the presence of NADPH. dihydrofolate 58-71 Dihydrofolate reductase Escherichia coli 25-29 30040418-1 2018 Dihydrofolate reductase (DHFR) catalyzes the reduction of dihydrofolate (DHF) to tetrahydrofolate (THF) in the presence of NADPH. dihydrofolate 25-28 Dihydrofolate reductase Escherichia coli 0-23 28422217-2 2017 DHFR catalyzes the reduction of dihydrofolate to tetrahydrofolate, which is a precursor for purine and thymidylate synthesis. dihydrofolate 32-45 Dihydrofolate reductase Escherichia coli 0-4