PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 3190739-8 1988 Together with earlier studies, these data indicate that the potency of FPGS inhibition by an analog containing ornithine closely parallels the relative substrate activity of its glutamate-containing counterpart. Glutamic Acid 178-187 folylpolyglutamate synthase Homo sapiens 71-75 2906805-2 1988 COOH-18O-labeled folate, methotrexate, and dihydropteroate, in addition to [17O]-glutamate, were synthesized and used as substrates for folylpolyglutamate synthetase (FPGS) isolated from Escherichia coli, hog liver, and rat liver and for dihydrofolate synthetase (DHFS) isolated from E. coli. Glutamic Acid 81-90 folylpolyglutamate synthase Homo sapiens 167-171 3431589-1 1987 Replacement of the glutamic acid (Glu) moiety in methotrexate (MTX) and aminopterin (AMT) by 2-amino-4-phosphonobutyric acid (APBA) and ornithine (Orn) has been found to give analogs that retain the ability to inhibit dihydrofolate reductase (DHFR) while also displaying high activity against folylpolyglutamate synthetase (FPGS). Glutamic Acid 34-37 folylpolyglutamate synthase Homo sapiens 293-322 3431589-1 1987 Replacement of the glutamic acid (Glu) moiety in methotrexate (MTX) and aminopterin (AMT) by 2-amino-4-phosphonobutyric acid (APBA) and ornithine (Orn) has been found to give analogs that retain the ability to inhibit dihydrofolate reductase (DHFR) while also displaying high activity against folylpolyglutamate synthetase (FPGS). Glutamic Acid 34-37 folylpolyglutamate synthase Homo sapiens 324-328 31008996-8 2019 Moreover, the UHPLC-MS/MS method also allowed evaluation of FPGS enzyme kinetic parameters revealing Km values for the substrates MTX and L-glutamic acid of 64 micromol/L and 2.2 mmol/L, respectively. Glutamic Acid 138-153 folylpolyglutamate synthase Homo sapiens 60-64 32694622-3 2020 Applying whole-exome sequencing to eight triplicate samples, we identified in one patient relapse-specific mutations in the folylpolyglutamate synthetase (FPGS) gene, whose product catalyzes the addition of multiple glutamate residues (polyglutamation) to methotrexate upon their entry into the cells. Glutamic Acid 133-142 folylpolyglutamate synthase Homo sapiens 155-159 3431589-1 1987 Replacement of the glutamic acid (Glu) moiety in methotrexate (MTX) and aminopterin (AMT) by 2-amino-4-phosphonobutyric acid (APBA) and ornithine (Orn) has been found to give analogs that retain the ability to inhibit dihydrofolate reductase (DHFR) while also displaying high activity against folylpolyglutamate synthetase (FPGS). Glutamic Acid 19-32 folylpolyglutamate synthase Homo sapiens 293-322 3431589-1 1987 Replacement of the glutamic acid (Glu) moiety in methotrexate (MTX) and aminopterin (AMT) by 2-amino-4-phosphonobutyric acid (APBA) and ornithine (Orn) has been found to give analogs that retain the ability to inhibit dihydrofolate reductase (DHFR) while also displaying high activity against folylpolyglutamate synthetase (FPGS). Glutamic Acid 19-32 folylpolyglutamate synthase Homo sapiens 324-328 32256983-3 2020 FPGS adds glutamate residues to folate upon its entry into the cell through a process known as polyglutamylation to enhance folate retention in the cell and to maintain a steady supply of utilizable folate derivatives for folate-dependent enzyme reactions. Glutamic Acid 10-19 folylpolyglutamate synthase Homo sapiens 0-4 16884772-3 2007 We identified in FPGS from CEM-p cells three amino acid substitutions that altered the ATP binding P-loop, glutamate/folate binding, and a conserved domain located at the carboxyl-terminal. Glutamic Acid 107-116 folylpolyglutamate synthase Homo sapiens 17-21 18672898-0 2008 Concentration-dependent processivity of multiple glutamate ligations catalyzed by folylpoly-gamma-glutamate synthetase. Glutamic Acid 49-58 folylpolyglutamate synthase Homo sapiens 82-118 18672898-5 2008 Together, the results of these experiments indicate that hFPGS can catalyze the processive addition of approximately four glutamate residues to DDAH 4PteGlu 1. Glutamic Acid 122-131 folylpolyglutamate synthase Homo sapiens 57-62 20350571-3 2010 The DHFS activity of recombinant PfDHFS-FPGS exhibited non-standard kinetics at high co-substrate (glutamate and ATP) concentrations, being partially inhibited by increasing concentrations of its principal substrate, dihydropteroate (DHP). Glutamic Acid 99-108 folylpolyglutamate synthase Homo sapiens 40-44 20025500-2 2009 The role of FPGS is to add glutamate residues to folates and antifolates, trapping them in the cell and increasing their affinity for subsequent enzymatic reactions. Glutamic Acid 27-36 folylpolyglutamate synthase Homo sapiens 12-16 19131550-1 2009 Folylpoly-gamma-gluatamate synthetase (FPGS) catalyzes the polyglutamylation and thus intracellular retention of folates and antifolates (eg, methotrexate; MTX) through the addition of multiple glutamate equivalents to their gamma-carboxyl residue. Glutamic Acid 194-203 folylpolyglutamate synthase Homo sapiens 0-37 19131550-1 2009 Folylpoly-gamma-gluatamate synthetase (FPGS) catalyzes the polyglutamylation and thus intracellular retention of folates and antifolates (eg, methotrexate; MTX) through the addition of multiple glutamate equivalents to their gamma-carboxyl residue. Glutamic Acid 194-203 folylpolyglutamate synthase Homo sapiens 39-43 16132101-0 2005 Synthesis of (6R)- and (6S)-5,10-dideazatetrahydrofolate oligo-gamma-glutamates: kinetics of multiple glutamate ligations catalyzed by folylpoly-gamma-glutamate synthetase. Glutamic Acid 69-78 folylpolyglutamate synthase Homo sapiens 135-171 15705579-1 2005 In some bacteria, such as Escherichia coli, the addition of L-glutamate to dihydropteroate (dihydrofolate synthetase activity) and the subsequent additions of L-glutamate to tetrahydrofolate (folylpolyglutamate synthetase (FPGS) activity) are catalyzed by the same enzyme, FolC. Glutamic Acid 60-71 folylpolyglutamate synthase Homo sapiens 223-227 15705579-1 2005 In some bacteria, such as Escherichia coli, the addition of L-glutamate to dihydropteroate (dihydrofolate synthetase activity) and the subsequent additions of L-glutamate to tetrahydrofolate (folylpolyglutamate synthetase (FPGS) activity) are catalyzed by the same enzyme, FolC. Glutamic Acid 159-170 folylpolyglutamate synthase Homo sapiens 223-227 12678736-1 2002 The importance of folylpoly-gamma-glutamate synthetase (FPGS) in cancer chemotherapy arises from its function of adding gamma-L-glutamate moieties to classical antifolates which contain an L-glutamate. Glutamic Acid 126-137 folylpolyglutamate synthase Homo sapiens 18-54 12494465-8 2003 This was consistent with a 23-fold decreased affinity of the mutant Cys346Phe FPGS for L-glutamate. Glutamic Acid 87-98 folylpolyglutamate synthase Homo sapiens 78-82 12678736-1 2002 The importance of folylpoly-gamma-glutamate synthetase (FPGS) in cancer chemotherapy arises from its function of adding gamma-L-glutamate moieties to classical antifolates which contain an L-glutamate. Glutamic Acid 126-137 folylpolyglutamate synthase Homo sapiens 56-60 8255099-6 1993 Cross-resistance during continuous exposure that did correlate with FPGS level was noted, however, to glutamate-containing thymidylate synthase inhibitors (including ICI D1694) and, to a minor extent, to 6-mercaptopurine and 5-fluorodeoxyuridine. Glutamic Acid 102-111 folylpolyglutamate synthase Homo sapiens 68-72 9306433-2 1997 The steady-state level of long-chain MTX polyglutamates depends on the balance of activities of two enzymes: folylpolyglutamate synthetase (FPGS), which adds glutamates to MTX in a gamma-carboxyl linkage, and gamma-glutamyl hydrolase (GGH) or conjugase, which sequentially removes the terminal glutamate residue of MTX polyglutamates. Glutamic Acid 45-54 folylpolyglutamate synthase Homo sapiens 109-138 9306433-2 1997 The steady-state level of long-chain MTX polyglutamates depends on the balance of activities of two enzymes: folylpolyglutamate synthetase (FPGS), which adds glutamates to MTX in a gamma-carboxyl linkage, and gamma-glutamyl hydrolase (GGH) or conjugase, which sequentially removes the terminal glutamate residue of MTX polyglutamates. Glutamic Acid 45-54 folylpolyglutamate synthase Homo sapiens 140-144 7565626-5 1995 It was observed that RFC exhibited an efficient substrate affinity for all analogues except CB3717, 2-NH2-ZD1694, and glutamate side-chain-modified FPGS inhibitors. Glutamic Acid 118-127 folylpolyglutamate synthase Homo sapiens 148-152 7646057-11 1995 These data suggest that the effect of beta,beta-F2Glu on polyglutamylation by FPGS is dependent on its position relative to the point of L-Glu ligation. Glutamic Acid 137-142 folylpolyglutamate synthase Homo sapiens 78-82 11389096-2 2001 Steady-state accumulation of MTXPG seems to depend on the activity of two enzymes: folylpolyglutamate synthetase (FPGS), which adds glutamate residues, and gamma-glutamyl hydrolase (GGH), which removes them. Glutamic Acid 92-101 folylpolyglutamate synthase Homo sapiens 114-118 10479284-0 1999 5-deazafolate analogues with a rotationally restricted glutamate or ornithine side chain: synthesis and binding interaction with folylpolyglutamate synthetase. Glutamic Acid 55-64 folylpolyglutamate synthase Homo sapiens 129-158 10598551-1 1999 Folylpoly-gamma-glutamate synthetase (FPGS) catalyzes the addition of several equivalents of glutamic acid to the gamma-carboxyl group in the side chain of folate cofactors and analogs. Glutamic Acid 93-106 folylpolyglutamate synthase Homo sapiens 0-36 10598551-1 1999 Folylpoly-gamma-glutamate synthetase (FPGS) catalyzes the addition of several equivalents of glutamic acid to the gamma-carboxyl group in the side chain of folate cofactors and analogs. Glutamic Acid 93-106 folylpolyglutamate synthase Homo sapiens 38-42 8958187-11 1996 The data indicate that substitution for Glu in an antifolate by some Glu analogs in which the gamma-COOH is either altered or replaced (e.g., gamma-tetrazole-Glu) leads to loss of both FPGS substrate activity and binding; antifolate target specificity is unchanged, while uptake is actually enhanced. Glutamic Acid 40-43 folylpolyglutamate synthase Homo sapiens 185-189 8958187-11 1996 The data indicate that substitution for Glu in an antifolate by some Glu analogs in which the gamma-COOH is either altered or replaced (e.g., gamma-tetrazole-Glu) leads to loss of both FPGS substrate activity and binding; antifolate target specificity is unchanged, while uptake is actually enhanced. Glutamic Acid 69-72 folylpolyglutamate synthase Homo sapiens 185-189 8958187-11 1996 The data indicate that substitution for Glu in an antifolate by some Glu analogs in which the gamma-COOH is either altered or replaced (e.g., gamma-tetrazole-Glu) leads to loss of both FPGS substrate activity and binding; antifolate target specificity is unchanged, while uptake is actually enhanced. Glutamic Acid 69-72 folylpolyglutamate synthase Homo sapiens 185-189 8217815-6 1993 After 48 h of mitogen stimulation there was a 4-10-fold increase in FPGS mRNA and folypolyglutamate formation (Glu > or = 5) was essentially simultaneous with 5CH3[3H]FH4 transport. Glutamic Acid 111-114 folylpolyglutamate synthase Homo sapiens 68-72