Characterization of a homogeneous complex of arginyl- and lysyl-tRNA synthetase: zinc and adenosine 5'-phosphate dependent synthesis of diadenosine 5',5'''-P1,P4-tetraphosphate.

Characterization of a homogeneous complex of arginyl- and lysyl-tRNA synthetase: zinc and adenosine 5'-phosphate dependent synthesis of diadenosine 5',5'''-P1,P4-tetraphosphate.
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精氨酰-和赖氨酰-tRNA 合成酶同质复合物的表征:锌和腺苷 5-磷酸依赖性合成二腺苷 5,5-P1,P4-四磷酸。

DOI:
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发表时间:
1983
期刊:
影响因子:
2.9
通讯作者:
R. H. Hilderman
R. H. Hilderman
中科院分区:
生物学3区
文献类型:
--
作者:
R. H. Hilderman

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锌、腺苷5 '-磷酸(AMP)和焦磷酸酶显著促进大鼠肝赖氨酰-tRNA合成酶合成二腺苷5',5“'-P1,P4-四磷酸(Ap 4A)。Ap 4A的合成不需要赖氨酸;因此不需要赖氨酰-腺苷酸复合物。已确定底物为腺苷5 '-三磷酸(ATP)和AMP,表观Km值分别为2.1 mM和1.5 mM。ATP和AMP的锌依赖性水解已被证明与合成酶有关。在锌的存在下,形成的AMP的量和由赖氨酰-tRNA合成酶合成的Ap 4A的量之间存在直接相关性。Ap 4A在赖氨酰-tRNA合成酶的氨酰化反应中作为ATP的竞争性抑制剂,KI为2.5 μ M。浓度高达12.5 μ M的Ap 4A不会抑制赖氨酰-tRNA合成酶合成Ap 4A。这表明酶上可能有不止一个ATP结合位点。
Zinc, adenosine 5'-phosphate (AMP), and pyrophosphatase greatly stimulate the synthesis of diadenosine 5',5'''-P1,P4-tetraphosphate (Ap4A) by rat liver lysyl-tRNA synthetase. The synthesis of Ap4A does not require lysine; thus the lysyl-adenylate complex is not required. The substrates have been determined to be adenosine 5'-triphosphate (ATP) and AMP with apparent Km values of 2.1 mM and 1.5 mM, respectively. A zinc-dependent hydrolysis of ATP and AMP has been shown to be associated with the synthetase. In the presence of zinc there is a direct correlation between both the amount of AMP formed and the amount of Ap4A synthesized by lysyl-tRNA synthetase. Ap4A acts as a competitive inhibitor for ATP in the aminoacylation reaction of lysyl-tRNA synthetase with a KI of 2.5 microM. Concentrations of Ap4A up to 12.5 microM do not inhibit the synthesis of Ap4A by lysyl-tRNA synthetase. This suggests that there may be more than one binding site for ATP on the enzyme.
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DOI: --
发表时间: 1981
期刊: The Journal of biological chemistry
影响因子: --
作者:
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通讯作者: Baril,EF
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DOI: --
发表时间: 1983
期刊: The Journal of biological chemistry
影响因子: --
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