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• W2011989156 abstract "Methenyltetrahydrofolate synthetase (5-formyltetrahydrofolate cyclodehydrase (cyclo-ligase) (ADP-forming) EC 6.3.3.2) catalyzes the ATP- and Mg2+-dependent transformation of 5-formyltetrahydrofolate (leucovorin) to 5,10-methenyltetrahydrofolate. The enzyme has been purified 49 000-fold from human liver by a two-column procedure with Blue Sepharose followed by folinate-Sepharose chromatography. It appears as a single band both on SDS-polyacrylamide gel electrophoresis (Mr 27 000) and on isoelectric focusing (pI = 7.0) and is monomeric, with a molecular weight of 27 000 on gel filtration. Initial-velocity studies suggest that the enzyme catalyzes a sequential mechanism and at 30°C and pH 6.0 the turnover number is 1000 min−1. The enzyme has a higher affinity for its pentaglutamate substrate (Km = 0.6 μM) than for the monoglutamate (Km = 2 μM). The antifolate methotrexate has no inhibitory effect at concentrations up to 350 μM, while methotrexate pentaglutamate is a competitive inhibitor with a Km = 15 μM. Similarly, dihydrofolate monoglutamate is a weak inhibitor with a Kt = 50 μM, while the pentaglutamate is a potent competitive inhibitor with a Ki of 3.8 μM. Thus, dihydrofolate and methotrexate pentaglutamates could regulate enzyme activity and help explain why leucovorin fails to rescue cells from high concentrations of methotrexate." @default.
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• W2011989156 date "1987-01-01" @default.
• W2011989156 modified "2023-10-14" @default.
• W2011989156 title "Human liver methenyltetrahydrofolate synthetase: improved purification and increased affinity for folate polyglutamate substrates" @default.
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• W2011989156 doi "https://doi.org/10.1016/0167-4838(87)90004-5" @default.
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