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Transcarboxylase. XII. Identification of the metal-containing subunits of transcarboxylase and stability of the binding.

作者信息

Ahmad F, Lygre D G, Jacobson B E, Wood H G

出版信息

J Biol Chem. 1972 Oct 10;247(19):6299-305.

PMID:4631318
Abstract
摘要

相似文献

1
Transcarboxylase. XII. Identification of the metal-containing subunits of transcarboxylase and stability of the binding.
J Biol Chem. 1972 Oct 10;247(19):6299-305.
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Transcarboxylase. XI. Electron microscopy and subunit structure.
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Transcarboxylase. V. The presence of bound zinc and cobalt.
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Electron and nuclear magnetic resonance studies of the interaction of pyruvate with transcarboxylase.丙酮酸与转羧酶相互作用的电子及核磁共振研究
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Purification of the subunits of transcarboxylase by affinity chromatography on avidin-sepharose.
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A new large form of transcarboxylase with six outer subunits and twelve biotinyl carboxyl carrier subunits.一种新的大型转羧酶，具有六个外部亚基和十二个生物素化羧基载体亚基。
J Biol Chem. 1977 Feb 25;252(4):1490-9.
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Phosphoenolpyruvate carboxytransphosphorylase. IV. Requirement for metal cations.
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Magnetic resonance studies of the proximity and spatial arrangement of propionyl coenzyme A and pyruvate on a biotin-metalloenzyme, transcarboxylase.关于生物素金属酶转羧酶上丙酰辅酶A和丙酮酸的接近程度及空间排列的磁共振研究。
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Proc Natl Acad Sci U S A. 1969 Dec;64(4):1315-22. doi: 10.1073/pnas.64.4.1315.
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Protein toxins of Pasteurella pestis. Subunit composition and acid binding.鼠疫耶尔森菌的蛋白质毒素。亚基组成与酸结合
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Transcarboxylase 5S structures: assembly and catalytic mechanism of a multienzyme complex subunit.转羧酶的5S结构：多酶复合体亚基的组装与催化机制
EMBO J. 2004 Sep 15;23(18):3621-31. doi: 10.1038/sj.emboj.7600373. Epub 2004 Aug 26.
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Transcarboxylase 12S crystal structure: hexamer assembly and substrate binding to a multienzyme core.转羧酶12S晶体结构：六聚体组装及底物与多酶核心的结合
EMBO J. 2003 May 15;22(10):2334-47. doi: 10.1093/emboj/cdg244.
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A novel transporter involved in cobalt uptake.一种参与钴摄取的新型转运蛋白。
Proc Natl Acad Sci U S A. 1997 Jan 7;94(1):36-41. doi: 10.1073/pnas.94.1.36.
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Inactivation of chicken liver pyruvate carboxylase by 1,10-phenanthroline.1,10-菲咯啉对鸡肝丙酮酸羧化酶的失活作用。
Biochem J. 1988 Jun 1;252(2):501-7. doi: 10.1042/bj2520501.