Dihydrofolate Reductase of Streptococcus faecalis
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چکیده
منابع مشابه
Dihydrofolate Reductase of Streptococcus f aecium
From a single amethopterin-resistant organism, Streptococcus faecium var. durans strain A, two different dihydrofolate reductases have been obtained as essentially homogeneous proteins in good yield. One of the reductases has a similar substrate specificity and turnover number (about 8000 moles per min per mole of enzyme) to the single reductase found in the amethopterin-sensitive strain of S. ...
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Preliminary evidence is presented that indicates that the dihydrofolate reductase activity of amethopterin-sensitive Streptococcus faecium var. durans ATCC 8043 is separable into two dihydrofolate reductases, one of which also reduces folate.
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1 The binding of a series of amide derivatives of methotrexate to Lactobacillus casei dihydrofolate reductase has been studied by inhibition constant measurements and by 'H n.m.r. spectroscopy. 2 Amide modification of the a-carboxylate of methotrexate was found to prevent interaction of the y-carboxylate with the imidazole of His 28. 3 Estimates of the contributions to the binding energy from t...
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From a single amethopterin-resistant organism, Streptococcus faecium var. durans strain A, two different dihydrofolate reductases have been obtained as essentially homogeneous proteins in good yield. One of the reductases has a similar substrate specificity and turnover number (about 8000 moles per min per mole of enzyme) to the single reductase found in the amethopterin-sensitive strain of S. ...
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Autoradiograms of total lipid extracts from Streptococcus faecalis ATCC 9790, harvested in the stationary phase from a medium containing (32)P-orthophosphate, showed six major spots. The corresponding compounds were identified as diphosphatidylglycerol (possibly with a penta acyl structure); phosphatidylglycerol; a provisionally identified mixture of alanylphosphatidylglycerol and of the 2'-lys...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1966
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)96488-4