CONTROL OF ESCHERICHIA COLI CARBAMYL PHOSPHATE SYNTHETASE BY PURINE AND PYRIMIDINE NUCLEOTIDES
CONTROL OF ESCHERICHIA COLI CARBAMYL PHOSPHATE SYNTHETASE BY PURINE AND PYRIMIDINE NUCLEOTIDES
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DOI:
10.1021/bi00874a013
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发表时间:
1966-01-01
期刊:
影响因子:
2.9
通讯作者:
MEISTER, A
中科院分区:
文献类型:
--
作者:
ANDERSON, PM;MEISTER, A
Carbamyl phosphate synthetase activity is significantly affected by a number of purine and pyrimidine nucleotides. Purine nucleotides (e.g., inosine monophosphate) stimulated activity and pyrimidine nucleotides were inhibitory (uridine nucleotides) or had no effect (cytidine nucleotides); these effects are exerted maximally by the first nucleotides synthesized in each pathway and decrease as the number of steps required to synthesize the various nucleotides from inosine 5[image]-monophosphate or uridine 5[image]-monophosphate, respectively, increases. The nucleotides apparently affect activity by altering the affinity of the enzyme for adenosine triphosphate (ATP). The relationship of these findings to these findings to the regulation of pyrimidine and arginine biosynthesis and of purine nucleotide biosynthesis is considered. The effects of the various nucleotides on the several additional reactions catalyzed by carbamyl phosphate synthetase (bicarbonate-dependent adenosine triphosphatase, hydrolysis of [gamma]-glutamyl hydroxamate, synthesis of ATP from carbamyl phosphate and adenosine diphosphate) were also examined; only the last 2 of these reactions were significantly affected, suggesting that the first step in carbamyl phosphate synthesis (activation of carbon dioxide) is not directly involved in this type of control.