Structure, mechanism and function in the ribulose-1,5-bisphosphate carboxylase/oxygenase (RubisCO) superfamily

核酮糖-1,5-二磷酸羧化酶/加氧酶 (RubisCO) 超家族的结构、机制和功能

• 批准号: 164660691
• 负责人: Professor Dr. Tobias Erb
• 金额: --
• 依托单位: Dept. of Biochemistry
• 依托单位国家: 德国
• 项目类别: Research Fellowships
• 财政年份: 2009
• 资助国家: 德国
• 起止时间: 2008-12-31 至 2010-12-31
• 项目状态: 已结题
• 来源: https://gepris.dfg.de/gepris/projekt/164660691?language=en
• 关键词: Structure; mechanism; function; ribulose; bisphosphate

D-Ribulose 1,5-bisphosphate carboxylase/oxygenase (RubisCO) is one of the most abundant en-zymes in the biosphere and catalyzes the key reaction of the Calvin cycle, the major process of CO2-fixation on earth. The RubisCO superfamily includes four distinct types of proteins. TYPE I, II and III RubisCOs are true CO2-fixing enzymes that operate in plants (TYPE I), bacteria (TYPE I and II), and archaea (TYPE III), respectively. In contrast to that, TYPE IV proteins (bacterial) miss residues essen-tial for a carboxylation reaction and consequently lack the ability to fix CO2. These “RUBISCO-LIKE PROTEINS” (RLP) fall into six divergent clades that are expected to catalyze different reactions. This study aims at identifying the reactions catalyzed by RLPs of different clades and deciphering their biological function. A combined approach of structural and biochemical methods will be used to ex-plore the substrate and reaction specificity of individual RLPs. The physiological role of RLPs will be tested by cell extract experiments and mutagenic studies that may unravel novel metabolic pathways. The diversification of catalytical functions within the RubisCO superfamily will be investigated by structural studies and site directed mutagenesis to modify and to introduce “novel” functions into the enzyme scaffold. The results of this study may extend our knowledge on the biological significance of this important superfamily of enzymes, as well as on the evolution and diversification of the reactions catalyzed by its single members. This might also be of relevance for an (agriculturally important) engineering of RubisCO, or the development of biotechnologically applicable carboxylases.

D-核酮糖 1,5-二磷酸羧化酶/加氧酶 (RubisCO) 是生物圈中最丰富的酶之一，催化卡尔文循环的关键反应，这是地球上二氧化碳固定的主要过程。 RubisCO 超家族包括。四种不同类型的蛋白质 I、II 和 III 型 Rub​​isCO 是真正的二氧化碳固定酶，可在植物（I 型）、细菌（I 型和 I 型）中发挥作用。与此相反，IV 型蛋白（细菌）缺少羧化反应所必需的残基，因此缺乏固定 CO2 的能力。 ）分为六个不同的分支，预计它们会催化不同的反应。本研究旨在识别不同分支的 RLP 催化的反应并破译它们的生物学特性。将采用结构和生化方法相结合的方法来探索单个 RLP 的底物和反应特异性，并通过细胞提取物实验和诱变研究来测试，从而揭示新的代谢途径。我们将通过结构研究和定点诱变来研究 RubisCO 超家族中催化功能的功能，以修改酶支架并将“新”功能引入其中。这项研究的结果可能会扩展我们对其生物学意义的认识。重要的酶超家族，以及其单一成员催化的反应的进化和多样化，这也可能与 RubisCO 的（农业上重要的）工程或生物技术上适用的羧化酶的开发相关。