PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 2730668-1 1989 The significance of the enol form of the pterin ring in enzymatic reduction of dihydrofolate by DHFR is discussed on the basis of the results of ab initio calculations carried out on the keto/enol tautomers of 6-methyl-7, 8-dihydropterin as the model compound for the natural substrate, dihydrofolate. dihydrofolate 287-300 dihydrofolate reductase Homo sapiens 96-100 2730668-1 1989 The significance of the enol form of the pterin ring in enzymatic reduction of dihydrofolate by DHFR is discussed on the basis of the results of ab initio calculations carried out on the keto/enol tautomers of 6-methyl-7, 8-dihydropterin as the model compound for the natural substrate, dihydrofolate. dihydrofolate 79-92 dihydrofolate reductase Homo sapiens 96-100 33724022-13 2021 For the two proteins that were experimentally tested, DHFR, a well-studied protein that catalyzes the conversion of dihydrofolate to tetrahydrofolate, and the kinase ACVR1, FRAGSITE identified new small-molecule nanomolar binders. dihydrofolate 116-129 dihydrofolate reductase Homo sapiens 54-58 912881-2 1977 In the presence of dihydrofolate reductase (EC 1.5.1.3), dihydrofolic acid is converted to tetrahydrofolate. dihydrofolate 57-74 dihydrofolate reductase Homo sapiens 19-42 3587364-1 1987 In previous work, several methotrexate (MTX)-resistant variants were isolated frm the human cell line HeLa BU25, which exhibited a high degree of dihydrofolate (DHFR) gene amplification (estimated to be 250- to 300-fold). dihydrofolate 146-159 dihydrofolate reductase Homo sapiens 161-165 2448654-6 1987 Important elements in leucovorin rescue are reactivation of DHFR with depression of cellular dihydrofolate (FH2) and provision of folate substrate to circumvent the block in FH4 synthesis. dihydrofolate 93-106 dihydrofolate reductase Homo sapiens 60-64 24306990-5 1985 The carrot DHFR is characterized by a pH optimum of 5.9, Km values for dihydrofolate and NADPH of 3.7 muM and 2.2 muM, respectively and a turnover number of 4 750 or 1 500 when referring to the 183 K form or the 58 K monomer, respectively. dihydrofolate 71-84 dihydrofolate reductase Homo sapiens 11-15 6882460-7 1983 The observation that NADH supports the reduction of folate and dihydrofolate but not MTX binding suggests that natural resistance to MTX could exist if NADH replaces NADPH as the main cofactor for DHFR. dihydrofolate 63-76 dihydrofolate reductase Homo sapiens 197-201 32752079-2 2020 A known folate antagonist, methotrexate (MTX) inhibits human dihydrofolate reductase (hDHFR), the enzyme responsible for the catalysis of 7,8-dihydrofolate reduction to 5,6,7,8-tetrahydrofolate, in biosynthesis and cell proliferation. dihydrofolate 138-155 dihydrofolate reductase Homo sapiens 61-84 33315225-3 2021 DHFR is an essential enzyme that catalyzes the reduction of dihydrofolate to tetrahydrofolate. dihydrofolate 60-73 dihydrofolate reductase Homo sapiens 0-4 32752079-2 2020 A known folate antagonist, methotrexate (MTX) inhibits human dihydrofolate reductase (hDHFR), the enzyme responsible for the catalysis of 7,8-dihydrofolate reduction to 5,6,7,8-tetrahydrofolate, in biosynthesis and cell proliferation. dihydrofolate 138-155 dihydrofolate reductase Homo sapiens 86-91 30508692-3 2019 The binding affinities of all these species (DHF, DHFP and THF) contribute to the mechanism of DHFR catalytic action. dihydrofolate 45-48 dihydrofolate reductase Homo sapiens 95-99 32051770-3 2019 Here, we examined dihydrofolate reductase (DHFR), an enzyme that catalyzes hydride from C4" of NADPH to C6 of 7,8-dihydrofolate (H2F). dihydrofolate 110-127 dihydrofolate reductase Homo sapiens 18-41 32051770-3 2019 Here, we examined dihydrofolate reductase (DHFR), an enzyme that catalyzes hydride from C4" of NADPH to C6 of 7,8-dihydrofolate (H2F). dihydrofolate 110-127 dihydrofolate reductase Homo sapiens 43-47 31401334-2 2019 Dihydrofolate reductase (DHFR), an enzyme involved in folate metabolism converts dihydrofolate into tetrahydrofolate, which is required for the de novo synthesis of purines, and certain amino acids. dihydrofolate 81-94 dihydrofolate reductase Homo sapiens 0-23 31401334-2 2019 Dihydrofolate reductase (DHFR), an enzyme involved in folate metabolism converts dihydrofolate into tetrahydrofolate, which is required for the de novo synthesis of purines, and certain amino acids. dihydrofolate 81-94 dihydrofolate reductase Homo sapiens 25-29 27013776-3 2016 To be used, folic acid must be converted to 7,8-dihydrofolate by dihydrofolate reductase to generate one-carbon derivatives serving as important cellular cofactors in the synthesis of nucleotides and amino acids required for cell growth. dihydrofolate 44-61 dihydrofolate reductase Homo sapiens 65-88 30754680-1 2019 Dihydrofolate reductase (DHFR) is an essential cellular enzyme and thereby catalyzes thereduction of dihydrofolate to tetrahydrofolate (THF). dihydrofolate 101-114 dihydrofolate reductase Homo sapiens 0-23 30754680-1 2019 Dihydrofolate reductase (DHFR) is an essential cellular enzyme and thereby catalyzes thereduction of dihydrofolate to tetrahydrofolate (THF). dihydrofolate 101-114 dihydrofolate reductase Homo sapiens 25-29 30398861-1 2018 In the present study, we address the effect of active site structure and dynamics of different dihydrofolate reductase (DHFR) isoforms on the p Ka of the bound substrate 7,8-dihydrofolate, in an attempt to understand possible evolutionary trends. dihydrofolate 170-187 dihydrofolate reductase Homo sapiens 95-118 30398861-1 2018 In the present study, we address the effect of active site structure and dynamics of different dihydrofolate reductase (DHFR) isoforms on the p Ka of the bound substrate 7,8-dihydrofolate, in an attempt to understand possible evolutionary trends. dihydrofolate 170-187 dihydrofolate reductase Homo sapiens 120-124 30019321-1 2018 The enzyme dihydrofolate reductase (DHFR) catalyzes NADPH dependent reduction of dihydrofolate to tetrahydrofolate. dihydrofolate 11-24 dihydrofolate reductase Homo sapiens 36-40 28605138-7 2017 The molecular docking and Prime-MMGBSA calculations of the natural substrate (dihydrofolate, DHF) and classical DHFR inhibitor (methotrexate, MTX) were performed in protozoan DHFR enzymes. dihydrofolate 78-91 dihydrofolate reductase Homo sapiens 112-116 28605138-7 2017 The molecular docking and Prime-MMGBSA calculations of the natural substrate (dihydrofolate, DHF) and classical DHFR inhibitor (methotrexate, MTX) were performed in protozoan DHFR enzymes. dihydrofolate 78-91 dihydrofolate reductase Homo sapiens 175-179 24122410-2 2013 Although DHFRL1 have high sequence homology with human DHFR, dihydrofolate (DHF) exhibits a lowered binding affinity to DHFRL1 and the corresponding molecular mechanism is still unknown. dihydrofolate 61-74 dihydrofolate reductase Homo sapiens 9-13 26125523-1 2015 The stepwise reduction of dihydrofolate to tetrahydrofolate entails significant conformational changes of dihydrofolate reductase (DHFR). dihydrofolate 26-39 dihydrofolate reductase Homo sapiens 106-129 26125523-1 2015 The stepwise reduction of dihydrofolate to tetrahydrofolate entails significant conformational changes of dihydrofolate reductase (DHFR). dihydrofolate 26-39 dihydrofolate reductase Homo sapiens 131-135 24122410-5 2013 The van der Waals interaction are more crucial for the total DHF binding energies, while the difference between the DHF binding energies of human DHFR and DHFRL1 can be attributed to the electrostatic interaction and the polar desolvation free energy.More specifically, lower DHF affinity to DHFRL1 can be mainly attributed to the reduction of net electrostatic interactions of residues Arg32 and Gln35 of DHFRL1 with DHF as being affected by Arg24. dihydrofolate 116-119 dihydrofolate reductase Homo sapiens 146-150 24122410-6 2013 The side chain of Arg24 in DHFRL1 can extend deeply into the binding sites of DHF and NADPH, and disturb the DHF binding by steric effect, which rarely happens in human DHFR and R24W DHFRL1 mutant. dihydrofolate 78-81 dihydrofolate reductase Homo sapiens 27-31 24122410-3 2013 To address this question, we studied the binding of DHF to DHFRL1 and DHFR by using molecular dynamics simulation. dihydrofolate 52-55 dihydrofolate reductase Homo sapiens 59-63 24122410-5 2013 The van der Waals interaction are more crucial for the total DHF binding energies, while the difference between the DHF binding energies of human DHFR and DHFRL1 can be attributed to the electrostatic interaction and the polar desolvation free energy.More specifically, lower DHF affinity to DHFRL1 can be mainly attributed to the reduction of net electrostatic interactions of residues Arg32 and Gln35 of DHFRL1 with DHF as being affected by Arg24. dihydrofolate 116-119 dihydrofolate reductase Homo sapiens 146-150 24122410-5 2013 The van der Waals interaction are more crucial for the total DHF binding energies, while the difference between the DHF binding energies of human DHFR and DHFRL1 can be attributed to the electrostatic interaction and the polar desolvation free energy.More specifically, lower DHF affinity to DHFRL1 can be mainly attributed to the reduction of net electrostatic interactions of residues Arg32 and Gln35 of DHFRL1 with DHF as being affected by Arg24. dihydrofolate 116-119 dihydrofolate reductase Homo sapiens 146-150 23726796-3 2013 This function maintains the thymidine-5-prime monophosphate pool critical for DNA replication and repair and, THF is generated from dihydrofolate (DHF) through the activity of DHFR. dihydrofolate 132-145 dihydrofolate reductase Homo sapiens 176-180 24053355-8 2013 Additional kinetic studies revealed that substrate channeling occurs in which dihydrofolate is directly transferred from the TS to DHFR active site without entering bulk solution. dihydrofolate 78-91 dihydrofolate reductase Homo sapiens 131-135 24053355-9 2013 The crystal structure suggests that the positively charged DHFR domain governs this electrostatically mediated movement of dihydrofolate, preventing release from the enzyme. dihydrofolate 123-136 dihydrofolate reductase Homo sapiens 59-63 23726796-3 2013 This function maintains the thymidine-5-prime monophosphate pool critical for DNA replication and repair and, THF is generated from dihydrofolate (DHF) through the activity of DHFR. dihydrofolate 147-150 dihydrofolate reductase Homo sapiens 176-180 18247058-3 2008 Dihydrofolate reductase catalyzes the reduction of folic acid to dihydrofolate and thereafter to tetrahydrofolate. dihydrofolate 65-78 dihydrofolate reductase Homo sapiens 0-23 23267138-5 2013 Furthermore, DHFR assays in vitro indicated that in the presence of GA, DHFR activity was slightly inhibited and the affinity of the enzyme for dihydrofolate was markedly decreased. dihydrofolate 144-157 dihydrofolate reductase Homo sapiens 13-17 21876184-1 2011 Human dihydrofolate reductase (DHFR) was previously thought to be the only enzyme capable of the reduction of dihydrofolate to tetrahydrofolate; an essential reaction necessary to ensure a continuous supply of biologically active folate. dihydrofolate 6-19 dihydrofolate reductase Homo sapiens 31-35 21876184-7 2011 The K(m) for NADPH is similar for both enzymes but DHFRL1 has a higher K(m) for dihydrofolate when compared to DHFR. dihydrofolate 80-93 dihydrofolate reductase Homo sapiens 51-55 23458706-10 2013 Results from these HHP experiments suggest water release accompanies binding of both the cofactor and DHF to R67 DHFR. dihydrofolate 102-105 dihydrofolate reductase Homo sapiens 113-117 23458706-11 2013 In an additional set of experiments, isothermal titration calorimetry studies in H2O and D2O find that water reorganization dominates the enthalpy associated with binding of DHF to R67 DHFR NADP(+), while no obvious effects occur for cofactor binding. dihydrofolate 174-177 dihydrofolate reductase Homo sapiens 185-189 22734697-1 2012 On the basis of structural analysis of dihydrofolate reductase (DHFR) (cocrystallized separately with NADPH, dihydrofolate and NADPH, trimethoprim), compounds 2 and 3 were optimized for inhibition of DHFR. dihydrofolate 39-52 dihydrofolate reductase Homo sapiens 64-68 22734697-1 2012 On the basis of structural analysis of dihydrofolate reductase (DHFR) (cocrystallized separately with NADPH, dihydrofolate and NADPH, trimethoprim), compounds 2 and 3 were optimized for inhibition of DHFR. dihydrofolate 39-52 dihydrofolate reductase Homo sapiens 200-204 26596739-6 2012 Subsequently, the method is applied to the dihydrofolate reductase (DHFR) catalyzed reduction of 7,8-dihydrofolate by nicotinamide adenine dinucleotide phosphate hydride (NADPH) to yield S-5,6,7,8-tetrahydrofolate and NADP(+). dihydrofolate 97-114 dihydrofolate reductase Homo sapiens 43-66 26596739-6 2012 Subsequently, the method is applied to the dihydrofolate reductase (DHFR) catalyzed reduction of 7,8-dihydrofolate by nicotinamide adenine dinucleotide phosphate hydride (NADPH) to yield S-5,6,7,8-tetrahydrofolate and NADP(+). dihydrofolate 97-114 dihydrofolate reductase Homo sapiens 68-72 22369433-2 2012 To explain these unusual results, weak interactions between DHF and osmolytes were proposed, with a competition between osmolyte and DHFR for DHF. dihydrofolate 60-63 dihydrofolate reductase Homo sapiens 133-137 24300187-1 2012 Trimethoprim (TMP) is a dihydrofolate reductase (DHFR) inhibitor which prevents the conversion of dihydrofolic acid into tetrahydrofolic acid, resulting in the depletion of the latter and leading to bacterial death. dihydrofolate 98-115 dihydrofolate reductase Homo sapiens 24-47 24300187-1 2012 Trimethoprim (TMP) is a dihydrofolate reductase (DHFR) inhibitor which prevents the conversion of dihydrofolic acid into tetrahydrofolic acid, resulting in the depletion of the latter and leading to bacterial death. dihydrofolate 98-115 dihydrofolate reductase Homo sapiens 49-53 21629435-1 2010 Dihydrofolate reductase (DHFR) catalyzes the reduction of dihydrofolate to tetrahydrofolate (THF). dihydrofolate 58-71 dihydrofolate reductase Homo sapiens 0-23 21629435-1 2010 Dihydrofolate reductase (DHFR) catalyzes the reduction of dihydrofolate to tetrahydrofolate (THF). dihydrofolate 58-71 dihydrofolate reductase Homo sapiens 25-29 19697148-2 2010 Dihydrofolate reductase (DHFR) catalyzes the NADPH-dependent reduction of dihydrofolate to tetrahydrofolate that is essential for DNA synthesis. dihydrofolate 74-87 dihydrofolate reductase Homo sapiens 25-29 18804698-1 2008 Dihydrofolate reductase (DHFR) enzyme catalyzes tetrahydrofolate regeneration by reduction of dihydrofolate using NADPH as a cofactor. dihydrofolate 94-107 dihydrofolate reductase Homo sapiens 0-23 18804698-1 2008 Dihydrofolate reductase (DHFR) enzyme catalyzes tetrahydrofolate regeneration by reduction of dihydrofolate using NADPH as a cofactor. dihydrofolate 94-107 dihydrofolate reductase Homo sapiens 25-29 8978793-2 1996 Methotrexate tightly binds to dihydrofolate reductase (DHFR), blocking the reduction of dihydrofolate to tetrahydrofolic acid, the active form of folic acid. dihydrofolate 30-43 dihydrofolate reductase Homo sapiens 55-59 17346178-4 2007 DHFR catalyzes the reduction of dihydrofolate (DHF) to tetrahydrofolate (THF), an essential cofactor in the biosynthesis of thymidylate monophosphate (dTMP). dihydrofolate 32-45 dihydrofolate reductase Homo sapiens 0-4 16969375-2 2007 The gene dihydrofolate reductase (DHFR) is primarily involved in the reduction of dihydrofolate, generated during thymidylate synthesis, to tetrahydrofolate in order to maintain adequate amounts of folate for DNA synthesis and homocysteine remethylation. dihydrofolate 9-22 dihydrofolate reductase Homo sapiens 34-38 16790925-1 2006 R67 plasmid-encoded dihydrofolate reductase (R67 DHFR) is an NADPH-dependent homotetrameric enzyme that catalyzes the reduction of dihydrofolate to tetrahydrofolate. dihydrofolate 20-33 dihydrofolate reductase Homo sapiens 49-53 15755837-2 2005 Dihydrofolate reductase (DHFR) is required to convert the folic acid used in supplements and for food fortification and the dihydrofolate produced by thymidylate synthase during DNA synthesis to the reduced folate forms used by the cell. dihydrofolate 124-137 dihydrofolate reductase Homo sapiens 0-23 15755837-2 2005 Dihydrofolate reductase (DHFR) is required to convert the folic acid used in supplements and for food fortification and the dihydrofolate produced by thymidylate synthase during DNA synthesis to the reduced folate forms used by the cell. dihydrofolate 124-137 dihydrofolate reductase Homo sapiens 25-29 14978269-1 2004 The interaction of dihydrofolate (H(2)F) and NADPH with a fluorescent derivative of H(2)F reductase (DHFR) was studied by using transient and single-molecule techniques. dihydrofolate 19-32 dihydrofolate reductase Homo sapiens 101-105 12732354-2 2003 In spectrophotometric assays of the kinetics of the reduction of dihydrofolate by DHFR in the presence of NADPH, these compounds had K(i) values ranging from 0.2 to 1.3pM, and thus were not greatly different in potency from the parent drug PT523. dihydrofolate 65-78 dihydrofolate reductase Homo sapiens 82-86 11931624-3 2002 In a spectrophotometric assay of dihydrofolate reductase (DHFR) inhibition using dihydrofolate and NADPH as the cosubstrates, the previously unreported compounds 2 and the mixed 10R and 10S diastereomers of 6 had K(i) values of 0.21 +/- 0.05 pM and 0.60 +/- 0.02 pM, respectively, as compared with previously reported values of 3.70 +/- 0.35 pM for AMT and 0.33 +/- 0.04 pM for PT523. dihydrofolate 33-46 dihydrofolate reductase Homo sapiens 58-62 10584062-1 1999 We have investigated the importance of polarization by the enzyme dihydrofolate reductase (DHFR) on its substrates, folate and dihydrofolate, using a series of quantum mechanical (QM) techniques (Hartree-Fock (HF), Moller-Plesset second-order perturbation theory (MP2), local density approximation (LDA) and generalized gradient approximation (GGA) density functional theory (DFT) calculations) in which the bulk enzyme is included in the calculations as point charges. dihydrofolate 66-79 dihydrofolate reductase Homo sapiens 91-95 10415082-6 1999 This value of 1 nM allowed us to control the conversion from dihydrofolate (H(2)folate) to H(4)folate less than 10% of initial substrate concentrations during assay, when we used a concentration around K(m) values reported for DHFR from various sources. dihydrofolate 61-74 dihydrofolate reductase Homo sapiens 227-231 9543003-9 1997 Substantial substrate and cofactor inhibition are observed during catalysis, consistent with non-productive binding of either two DHF or two NADPH molecules in Q67H R67 DHFR. dihydrofolate 130-133 dihydrofolate reductase Homo sapiens 169-173 8999931-12 1997 These results indicate protonated dihydrofolate (pKa = 2.59) is the productive substrate and that R67 DHFR does not possess a proton donor. dihydrofolate 34-47 dihydrofolate reductase Homo sapiens 102-106 17413111-1 2007 BACKGROUND: Dihydrofolate reductase (DHFR) converts dihydrofolate (DHF) into tetrahydrofolate (THF) and plays an essential role in cell metabolism and cellular growth. dihydrofolate 52-65 dihydrofolate reductase Homo sapiens 12-35 17413111-1 2007 BACKGROUND: Dihydrofolate reductase (DHFR) converts dihydrofolate (DHF) into tetrahydrofolate (THF) and plays an essential role in cell metabolism and cellular growth. dihydrofolate 52-65 dihydrofolate reductase Homo sapiens 37-41 17413111-1 2007 BACKGROUND: Dihydrofolate reductase (DHFR) converts dihydrofolate (DHF) into tetrahydrofolate (THF) and plays an essential role in cell metabolism and cellular growth. dihydrofolate 37-40 dihydrofolate reductase Homo sapiens 12-35 11989624-3 2001 This homotetrameric protein exhibits 222 symmetry, with only a few residues from each chain contributing to the active site, so related sites must be used to bind both substrate (dihydrofolate) and cofactor (NADPH) in the productive R67 DHFR.NADPH.dihydrofolate complex. dihydrofolate 179-192 dihydrofolate reductase Homo sapiens 237-241 11989624-3 2001 This homotetrameric protein exhibits 222 symmetry, with only a few residues from each chain contributing to the active site, so related sites must be used to bind both substrate (dihydrofolate) and cofactor (NADPH) in the productive R67 DHFR.NADPH.dihydrofolate complex. dihydrofolate 248-261 dihydrofolate reductase Homo sapiens 237-241 11560482-16 2001 For example, the Y69F R67 DHFR displays an 8-fold increase in the K(m) for dihydrofolate and a 20-fold increase in the K(m) for NADPH. dihydrofolate 75-88 dihydrofolate reductase Homo sapiens 26-30 10683342-5 2000 The K(m) of KSHV-DHFR for dihydrofolate (FH(2)) was 2.4 microM, which is significantly higher than the K(m) of recombinant hDHFR (rhDHFR) for FH(2) (390 nM). dihydrofolate 26-39 dihydrofolate reductase Homo sapiens 17-21 8845002-1 1996 The bifunctional enzyme dihydrofolate reductase-thymidylate synthase (DHFR-TS) carries out two distinct reactions, with the dihydrofolate produced by the TS-catalyzed reaction acting as the substrate for the DHFR-catalyzed reaction. dihydrofolate 24-37 dihydrofolate reductase Homo sapiens 70-74 8845002-1 1996 The bifunctional enzyme dihydrofolate reductase-thymidylate synthase (DHFR-TS) carries out two distinct reactions, with the dihydrofolate produced by the TS-catalyzed reaction acting as the substrate for the DHFR-catalyzed reaction. dihydrofolate 24-37 dihydrofolate reductase Homo sapiens 208-212 1637816-1 1992 The kinetics of the NADPH-dependent reduction of 7,8-dihydrofolate, folate, and 7,8-dihydrobiopterin by human dihydrofolate reductase have been examined over the pH range from 4.0 to 9.5. dihydrofolate 49-66 dihydrofolate reductase Homo sapiens 110-133 8852336-2 1995 The primary target of MTX is the enzyme dihydrofolate reductase (DHFR) which catalyzes the reduction of folate and 7,8-dihydrofolate to 5,6,7,8-tetrahydrofolate. dihydrofolate 115-132 dihydrofolate reductase Homo sapiens 40-63 8852336-2 1995 The primary target of MTX is the enzyme dihydrofolate reductase (DHFR) which catalyzes the reduction of folate and 7,8-dihydrofolate to 5,6,7,8-tetrahydrofolate. dihydrofolate 115-132 dihydrofolate reductase Homo sapiens 65-69 8226776-8 1993 The protein product, R67 DHFRdouble, is twice the molecular mass of native R67 DHFR and is fully active with kcat = 1.2 s-1, Km(NADPH) = 2.7 microM and Km(dihydrofolate) = 6.3 microM. dihydrofolate 155-168 dihydrofolate reductase Homo sapiens 25-29 8490020-3 1993 Incubation of DHFR protein with either its substrates, dihydrofolate or NADPH, or with an inhibitor, methotrexate, repressed its ability to interact with DHFR mRNA. dihydrofolate 55-68 dihydrofolate reductase Homo sapiens 14-18 8490020-3 1993 Incubation of DHFR protein with either its substrates, dihydrofolate or NADPH, or with an inhibitor, methotrexate, repressed its ability to interact with DHFR mRNA. dihydrofolate 55-68 dihydrofolate reductase Homo sapiens 154-158 1314649-4 1992 koff for dissociation of folate, dihydrofolate (H2folate), and H4folate from their binary complexes with hDHFR is similarly pH dependent. dihydrofolate 33-46 dihydrofolate reductase Homo sapiens 105-110 1904273-9 1991 The Km value for human DHFR for the dihydrofolate analogue is 2.0 microM. dihydrofolate 36-49 dihydrofolate reductase Homo sapiens 23-27 1907850-5 1991 At this pH, the KD value for dihydrofolate (FAH2) for the R70K enzyme shows only a 7-fold increase over that for the wild-type hDHFR. dihydrofolate 29-42 dihydrofolate reductase Homo sapiens 127-132 1929292-5 1991 The standard assay for P. carinii dihydrofolate reductase contained 0.12 mM NADPH and 92 microM dihydrofolic acid. dihydrofolate 96-113 dihydrofolate reductase Homo sapiens 34-57 34788822-3 2022 The reduction of FA to dihydrofolate by dihydrofolate reductase (DHFR) is slow in humans. dihydrofolate 23-36 dihydrofolate reductase Homo sapiens 40-63 2271620-9 1990 RBG200 DHFR was found to specifically transfer the pro-R hydrogen of NADPH to dihydrofolate, making it a member of the A-stereospecific class of dehydrogenases. dihydrofolate 78-91 dihydrofolate reductase Homo sapiens 7-11 34788822-3 2022 The reduction of FA to dihydrofolate by dihydrofolate reductase (DHFR) is slow in humans. dihydrofolate 23-36 dihydrofolate reductase Homo sapiens 65-69