来自蓝藻聚球藻属的核酮糖二磷酸羧化酶加氧酶的动力学及亚基相互作用 - Suppr

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Kinetics and subunit interactions of ribulose bisphosphate carboxylase-oxygenase from the cyanobacterium, Synechococcus sp.

作者信息

Andrews T J, Abel K M

出版信息

J Biol Chem. 1981 Aug 25;256(16):8445-51.

PMID:6790541

Abstract

摘要

相似文献

Kinetics and subunit interactions of ribulose bisphosphate carboxylase-oxygenase from the cyanobacterium, Synechococcus sp.来自蓝藻聚球藻属的核酮糖二磷酸羧化酶加氧酶的动力学及亚基相互作用

J Biol Chem. 1981 Aug 25;256(16):8445-51.

Chemosynthetic, photosynthetic, and cyanobacterial ribulose bisphosphate carboxylase.化学合成、光合作用及蓝细菌中的核酮糖二磷酸羧化酶。

Basic Life Sci. 1978;11:179-207. doi: 10.1007/978-1-4684-8106-8_13.

The function of the small subunits of ribulose bisphosphate carboxylase-oxygenase.核酮糖二磷酸羧化酶-加氧酶小亚基的功能。

J Biol Chem. 1983 Jun 25;258(12):7514-8.

Presence of two subunit types in ribulose-1,5-bisphosphate carboxylase from blue-green algae.蓝藻中1,5-二磷酸核酮糖羧化酶的两种亚基类型的存在。

Biochem Biophys Res Commun. 1976 Jan 26;68(2):537-44. doi: 10.1016/0006-291x(76)91179-7.

Ribulose-1,5-bisphosphate carboxylase-oxygenase.核酮糖-1,5-二磷酸羧化酶加氧酶

Annu Rev Biochem. 1983;52:507-35. doi: 10.1146/annurev.bi.52.070183.002451.

Role of the large and small subunits of ribulose-1,5-bisphosphate carboxylase in the activation by CO2 and Mg2+.1,5-二磷酸核酮糖羧化酶的大亚基和小亚基在二氧化碳和镁离子激活过程中的作用。

J Biochem. 1979 Apr;85(4):923-30. doi: 10.1093/oxfordjournals.jbchem.a132424.

Activation and regulation of ribulose bisphosphate carboxylase-oxygenase in the absence of small subunits.在缺乏小亚基的情况下核酮糖二磷酸羧化酶-加氧酶的激活与调控

J Biol Chem. 1979 Oct 25;254(20):10184-9.

Modification of histidine at the active site of spinach ribulose bisphosphate carboxylase.菠菜核酮糖二磷酸羧化酶活性位点上组氨酸的修饰

Biochem Biophys Res Commun. 1980 Jun 30;94(4):1091-7. doi: 10.1016/0006-291x(80)90531-8.

The activation of ribulose 1,5-bisphosphate carboxylase/oxygenase.1,5-二磷酸核酮糖羧化酶/加氧酶的激活

Basic Life Sci. 1978;11:283-306. doi: 10.1007/978-1-4684-8106-8_18.

On the mechanism of effector-mediated activation of ribulose bisphosphate carboxylase/oxygenase.关于效应物介导的1,5-二磷酸核酮糖羧化酶/加氧酶激活机制

J Biol Chem. 1981 Jul 10;256(13):6623-8.

引用本文的文献

The Diverse AAA+ Machines that Repair Inhibited Rubisco Active Sites.修复受抑制的核酮糖-1,5-二磷酸羧化酶/加氧酶（Rubisco）活性位点的多种AAA+机器

Front Mol Biosci. 2017 May 19;4:31. doi: 10.3389/fmolb.2017.00031. eCollection 2017.

Uptake and utilization of inorganic carbon by cyanobacteria.蓝藻对无机碳的摄取和利用。

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Synthesis and assembly of bacterial and higher plant Rubisco subunits in Escherichia coli.在大肠杆菌中细菌和高等植物 Rubisco 亚基的合成和组装。

Photosynth Res. 1988 Jul;17(1-2):145-57. doi: 10.1007/BF00047686.

Ribulose bisphosphate carboxylase in algae: synthesis, enzymology and evolution.藻类中的核酮糖二磷酸羧化酶：合成、酶学和进化。

Photosynth Res. 1990 Nov;26(2):69-85. doi: 10.1007/BF00047078.

Activity expressed from cloned Anacystis nidulans large and small subunit ribulose bisphosphate carboxylase genes.从克隆的鱼腥藻大、小亚基核酮糖二磷酸羧化酶基因表达的活性。

Plant Mol Biol. 1985 Jul;5(4):257-63. doi: 10.1007/BF00020643.

Ribulose 1,5-bisphosphate carboxylase and phosphoribulokinase in Prochloron.鱼腥藻中的核酮糖 1,5-二磷酸羧化酶和磷酸核酮糖激酶。

Planta. 1983 Aug;158(4):281-7. doi: 10.1007/BF00397328.

Molar absorptivity and A1 cm (1%) values for proteins at selected wavelengths of the ultraviolet and visible regions. XXII.紫外和可见光区各选定波长下蛋白质摩尔消光系数和 A1cm（1%）值。XXII.

Appl Biochem Biotechnol. 1982 Nov;7(6):475-95. doi: 10.1007/BF02799179.

Maintaining photosynthetic CO2 fixation via protein remodelling: the Rubisco activases.通过蛋白质重塑维持光合 CO2 固定：Rubisco 激活酶。

Photosynth Res. 2014 Feb;119(1-2):191-201. doi: 10.1007/s11120-013-9819-0. Epub 2013 Mar 31.

Catalytic by-product formation and ligand binding by ribulose bisphosphate carboxylases from different phylogenies.不同系统发育来源的核酮糖二磷酸羧化酶的催化副产物形成及配体结合

Biochem J. 2006 Nov 1;399(3):525-34. doi: 10.1042/BJ20060430.

Expression of foreign type I ribulose-1,5-bisphosphate carboxylase/ oxygenase (EC 4.1.1.39) stimulates photosynthesis in cyanobacterium Synechococcus PCC7942 cells.外源I型核酮糖-1,5-二磷酸羧化酶/加氧酶（EC 4.1.1.39）的表达刺激了集胞藻PCC7942细胞中的光合作用。

Photosynth Res. 2006 Jun;88(3):287-97. doi: 10.1007/s11120-006-9048-x. Epub 2006 May 12.

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