2-Aminoethylarsonic acid as an analogue of ethanolamine phosphate. Endowment of ethanolamine-phosphate cytidylyltransferase with CTP pyrophosphatase activity

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2-Aminoethylarsonic acid as an analogue of ethanolamine phosphate. Endowment of ethanolamine-phosphate cytidylyltransferase with CTP pyrophosphatase activity.

2-Aminoethylarsonic acid was tested for its ability to act as a substrate for ethanolamine-phosphate cytidylytransferase as a cytidylyl acceptor in place of ethanolamine phosphate. The expected product, like all mixed anhydrides of arsonic acids, should hydrolyse spontaneously with regeneration of the substrate analogue and CMP formation; such CMP production was observed. The limiting velocity ...

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Ethanolamine phosphate excretion in a family with hypophosphatasia.

Hypophosphatasia is an inherited disorder of bone, which is thought to be transmitted by a recessive gene. The homozygous form of the disease presents with a well-defined clinical picture and two biochemical abnormalities: lowered serum alkaline phosphatase and excessive urinary excretion of ethanolamine phosphate (EAP). Heterozygous carriers are usually not manifest clinically, but it has been...

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Synthesis of an unsaturated diether analogue of phosphatidyl ethanolamine.

A synthesis of racemic diether analogues of glyceryl phosphatides is reported which is applicable to unsaturated aliphatic substituents. The "oleyl" diether analogue of phosphatidyl ethanolamine has been synthesized.

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Use of 3-aminopropanol as an ethanolamine analogue in the study of phospholipid metabolism in Tetrahymena.

About 50% of the ethanolamine in phosphatidylethanolamine in Tetrahymena is replaced by 3-aminopropan-1-ol when the compound is added to the growth medium. The phosphatidylpropanolamine which is formed is not converted into the corresponding phosphatidylcholine analogue by methylation. There is an increase in phosphatidylcholine formed by the phosphotransferase pathway from free [3H]choline and...

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Interaction of N-substituted ethanolamine analogs with ethanolamine ammonia-lyase, an adenosylcobalamin-requiring enzyme.

A number of N-substituted ethanolamine derivatives have been found to interact productively with ethanolamine ammonia-lyase, an adenosylcobalamin (AdoCbl) requiring enzyme that catalyzes the conversion of vicinal amino alcohols to oxo compounds. Inhibition, inactivation, cleavage of AdoCbl, and exchange of tritium out of [5'-3H]AdoCbl were all observed, the effects varying from analog to analog...

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ژورنال

عنوان ژورنال: Biochemical Journal

سال: 1989

ISSN: 0264-6021,1470-8728

DOI: 10.1042/bj2600299