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J. Biol. Chem., Vol. 259, Issue 5, 2728-2733, Mar, 1984

Purification and properties of 5,10-methenyltetrahydrofolate synthetase from Lactobacillus casei

CE Grimshaw, GB Henderson, GG Soppe, G Hansen, EJ Mathur and FM Huennekens

5,10-Methenyltetrahydrofolate synthetase (EC 6.3.3.2), which catalyzes the ATP- and Mg2+ -dependent isomerization of 5-formyl- to 5,10- methenyltetrahydrofolate, has been purified 10,000-fold from Lactobacillus casei using sequential affinity chromatography on immobilized 5-formyltetrahydrofolate and ATP. The enzyme is homogeneous when examined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, is monomeric with a molecular mass of 23,000 Da, and contains a high proportion of hydrophobic amino acids and a single cysteine residue. At 30 degrees C, the turnover number is 88 min-1, and the Km values at pH 6 for 5-formyltetrahydrofolate and Mg-ATP are 0.6 and 1.0 microM, respectively. The enzyme is specific for (6S)-5- formyltetrahydrofolate, but ATP can be replaced by other nucleoside 5'- triphosphates with varying efficiency. The purified enzyme is markedly stabilized by the non-ionic detergent, Tween 20.
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