The mechanism of Rubisco activase: Insights from studies of the properties and structure of the enzyme
โ Scribed by Michael E. Salvucci; William L. Ogren
- Publisher
- Springer
- Year
- 1996
- Tongue
- English
- Weight
- 993 KB
- Volume
- 47
- Category
- Article
- ISSN
- 0166-8595
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โฆ Synopsis
Rubisco, the primary carboxylating enzyme in photosynthesis, must be activated to catalyze CO2 fixation. The concept of an 'activase', a specific protein for activating Rubisco, was first introduced in 1985 based largely on biochemical and genetic studies of a high CO2-requiring mutant ofArabidopsis (Salvucci et al. (1985) Photosynth Res 7: 193-201). Over the past ten years, details about the occurrence, structure, and properties of Rubisco activase have been elucidated. However, the mechanism of action of Rubisco activase remains elusive. This review discusses the need for and function of Rubisco activase and summarizes information about the properties and structure of Rubisco activase. The information is evaluated in the context of the mechanism of Rubisco activase.
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In the multicellular red alga Antithamnion spec. both rubisco genes (rbcL and rbcS) are encoded on the plastid DNA (ptDNA). Both genes are separated by a short A/T-rich spacer of 100 bp and are cotranscribed into an mRNA of approximately 2.7 kb. These findings are in extensive agreement with those o
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