pH‐dependent Studies of E. coli Methylenetetrahydrofolate Reductase
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چکیده
منابع مشابه
Enzymatic synthesis of the methyl group of methionine. V. Studies with 5, 10-methylenetetrahydrofolate reductase from Escherichia coli.
The mechanism of formation de novo of the methyl group of methionine has been studied in mammalian, avian, and bacterial cell-free systems (l-8). The studies on extracts of various mutant strains of Escherichia coli have shown that, of the common compounds, formaldehyde or the P-carbon atom of serine is the best precursor of the methyl of methionine (5-7). Optimal formation of methionine from s...
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Background: The most common polymorphisms identified in the Methylenetetrahydrofolate reductase (MTHFR) gene, C677T and A1298C lead to defective activity of this enzyme and increase the risk of venous and arterial thrombosis. There are limited investigations regarding the effects of thrombogenic polymorphisms on the clinical phenotypes of rare hereditary hemorrhagic disorders like Glanzmann's t...
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Methylenetetrahydrofolate reductase (MTHFR) catalyzes the reduction of methylenetetrahydrofolate to methyltetrahydrofolate, the methyl donor for the conversion of homocysteine to methionine. Regulation of MTHFR activity is crucial for maintaining cellular concentrations of methionine and S-adenosylmethionine (AdoMet). Purified recombinant human MTHFR expressed in insect cells is multiply phosph...
متن کاملPurification and properties of NADH-dependent 5, 10-methylenetetrahydrofolate reductase (MetF) from Escherichia coli.
A K-12 strain of Escherichia coli that overproduces methylenetetrahydrofolate reductase (MetF) has been constructed, and the enzyme has been purified to apparent homogeneity. A plasmid specifying MetF with six histidine residues added to the C terminus has been used to purify histidine-tagged MetF to homogeneity in a single step by affinity chromatography on nickel-agarose, yielding a preparati...
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ژورنال
عنوان ژورنال: The FASEB Journal
سال: 2012
ISSN: 0892-6638,1530-6860
DOI: 10.1096/fasebj.26.1_supplement.756.13