Role of adenine deaminase in purine salvage and nitrogen metabolism and characterization of the ade gene in Bacillus subtilis

Role of adenine deaminase in purine salvage and nitrogen metabolism and characterization of the ade gene in Bacillus subtilis
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DOI:
10.1128/jb.178.3.846-853.1996
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发表时间:
1996-02-01
影响因子:
3.2
通讯作者:
Saxild, HH
Saxild, HH
中科院分区:
生物学3区
文献类型:
--
作者:
Nygaard, P;Duckert, P;Saxild, HH

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枯草芽孢杆菌腺嘌呤代谢缺陷突变体的分离提供了一种工具,使得研究腺嘌呤脱氨酶在生长细胞中腺嘌呤代谢中的作用成为可能。腺嘌呤脱氨酶是唯一能使B中腺嘌呤化合物脱氨的酶。枯草杆菌,这是一个反应,这是重要的腺嘌呤利用作为嘌呤,也作为氮源。腺嘌呤的摄取与它的进一步代谢是严格耦合的。腺嘌呤的补救被氨基酸饥饿的严格反应抑制,而腺嘌呤的脱氨基则不受抑制。以外源鸟苷为嘌呤源和谷氨酰胺为氮源时,腺嘌呤脱氨酶水平降低。无论氨或嘌呤作为氮源,酶水平基本相同。减少的水平仅仅在贫碳源上看到。ade基因被克隆,并且核苷酸序列和mRNA分析揭示了编码65-kDa蛋白的单基因操纵子。通过转导杂交,我们在染色体图谱上将ade基因定位在130度处。
The isolation of mutants defective in adenine metabolism in Bacillus subtilis has provided a tool that has made it possible to investigate the role of adenine deaminase in adenine metabolism in growing cells. Adenine deaminase is the only enzyme that can deaminate adenine compounds in B. subtilis, a reaction which is important for adenine utilization as a purine and also as a nitrogen source. The uptake of adenine is strictly coupled to its further metabolism. Salvaging of adenine is inhibited by the stringent response to amino acid starvation, while the deamination of adenine is not. The level of adenine deaminase was reduced when exogenous guanosine served as the purine source and when glutamine served as the nitrogen source. The enzyme level was essentially the same whether ammonia or purines served as the nitrogen source. Reduced levels mere seen on poor carbon sources. The ade gene was cloned, and the nucleotide sequence and mRNA analyses revealed a single-gene operon encoding a 65-kDa protein. By transductional crosses, we have located the ade gene to 130 degrees on the chromosomal map.