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黄素氧还蛋白:来自棕色固氮菌的AMP核苷酶的变构抑制剂。

Flavodoxin: an allosteric inhibitor of AMP nucleosidase from Azotobacter vinelandii.

作者信息

Yoshino M, Murakami K, Tsushima K

出版信息

J Biochem. 1976 Oct;80(4):839-43. doi: 10.1093/oxfordjournals.jbchem.a131345.

Abstract

Flavodoxin, which participates in nitrogen fixation, was found to be a potent allosteric inhibitor of AMP nucleosidase [EC 3.2.2.4] from Azotobacter vinelandii. It inhibited the enzyme by decreasing its affinity for ATP without affecting the maximum velocity. The inhibition constant for flavodoxin was estimated to be 10 muM, which is within the range of physiological concentration in the cells. The concentration of flavodoxin able to alter the activity in vitro suggests that this phenomenon could be of significance in the regulation of flavin biosynthesis in vivo. Flavin mononucleotide (FMN), a prosthetic group of flavodoxin, was also found to act as an allosteric inhibitor. Since no inhibitory action of apo-flavodoxin was observed, it was concluded that the FMN chromophore of the flavodoxin is responsible for the inhibition of the enzyme by this protein.

摘要

参与固氮作用的黄素氧还蛋白被发现是来自棕色固氮菌的AMP核苷酶[EC 3.2.2.4]的一种强效变构抑制剂。它通过降低酶对ATP的亲和力来抑制该酶,而不影响最大反应速度。黄素氧还蛋白的抑制常数估计为10 μM,这在细胞内的生理浓度范围内。能够在体外改变活性的黄素氧还蛋白浓度表明,这种现象可能在体内黄素生物合成的调节中具有重要意义。黄素单核苷酸(FMN)是黄素氧还蛋白的辅基,也被发现可作为变构抑制剂。由于未观察到脱辅基黄素氧还蛋白的抑制作用,因此得出结论,黄素氧还蛋白的FMN发色团是该蛋白质抑制该酶的原因。

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