Formation of Deoxycytidine Phosphates from Cytidine Phosphates in Extracts from Escherichia coli
نویسندگان
چکیده
منابع مشابه
Formation of deoxycytidine phosphates from cytidine phosphates in extracts from Escherichia coli.
Strong evidence has been obtained from experiments in viva that in different types of cells, deoxyribosyl compounds are formed through a reduction of the corresponding ribosyl compounds (cf. (1)). Recently, enzyme systems have been obtained from avian, mammalian, and bacterial cells, which carry out such transformations with pyrimidine and purine ribonucleotides (2-4). The present paper describ...
متن کاملFormation of Deoxycytidine Phosphates from Cytidine Phosphates in Extracts from Escherichia coZi*
Strong evidence has been obtained from experiments in viva that in different types of cells, deoxyribosyl compounds are formed through a reduction of the corresponding ribosyl compounds (cf. (1)). Recently, enzyme systems have been obtained from avian, mammalian, and bacterial cells, which carry out such transformations with pyrimidine and purine ribonucleotides (2-4). The present paper describ...
متن کاملEnzymatic synthesis of deoxyribonucleotides. I. Formation of deoxycytidine diphosphate from cytidine diphosphate with enzymes from Escherichia coli.
Extracts from Escherichiu coli catalyze the formation of deoxycyticlme phosphates from cytidine 5’-phosphate (1). Optimal formation of deoxynucleotides required the addition of adenosine triphosphate and Mg* ions to the extract, and, after treatment with Dowex 2, a strong stimulation of the reaction by reduced triphosphopyridine nucleotide was observed. Similar results were obtained in extracts...
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Cytidine deaminase (cytidine aminohydrolase, EC 3.5.4.5) has been purified approximately 160-fold from extracts of Escherichia coli B. The enzyme shows constant activity between pH 6 and 11. No significant change in rate is observed when DzO replaces water as the solvent. In addition to the deamination of cytidine, the purified deaminase catalyzes slow hydrolysis of N4-methylcytidine. The enzym...
متن کاملThe kinetics of the reaction of nitrophenyl phosphates with alkaline phosphatase from Escherichia coli.
1. The steady-state rate of hydrolysis of 2,4-dinitrophenyl phosphate catalysed by Escherichia coli phosphatase is identical with that of 4-nitrophenyl phosphate over the pH range 5.5-8.5. 2. The increase in the rate of the enzyme-catalysed decomposition of nitrophenyl phosphates in the presence of tris at pH8.1 and 5.9 is consistent with the hypothesis that tris increases the rate of decomposi...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1961
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)64258-9