Výsledky vyhledávání

Phosphorylation of Phosphoenolpyruvate Carboxylase Is Not Essential for High Photosynthetic Rates in the C4 Species Flaveria bidentis

Autor: Vanda Quinn, Robert T. Furbank, Katsura Izui, Tsuyoshi Furumoto, Susanne von Caemmerer

Publikováno v: Plant Physiology. 144:1936-1945

Phosphoenolpyruvate carboxylase (PEPC; EC4.1.1.31) plays a key role during C(4) photosynthesis. The enzyme is activated by metabolites such as glucose-6-phosphate and inhibited by malate. This metabolite sensitivity is modulated by the reversible pho

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::aae2d8aa93bf3df0777f1c7526e55f97
https://doi.org/10.1104/pp.107.102541

Zobrazit plný text záznamu

Carbonic anhydrase and C4 photosynthesis: a transgenic analysis

Autor: N.C. Hancock, Vanda Quinn, S. von Caemmerer, Robert T. Furbank, G. D. Price, Martha Ludwig

Publikováno v: ResearcherID

Carbonic anhydrase (CA, EC 4.2.1.1) catalyses the first reaction in the C4 photosynthetic pathway, the conversion of atmospheric CO2 to bicarbonate in the mesophyll cytosol. To examine the importance of the enzyme to the functioning of the C4 photosy

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7746e84406437cccf9f6c1e7b2827962
https://doi.org/10.1111/j.1365-3040.2003.01157.x

Zobrazit plný text záznamu

Binding of an invariant-chain peptide, CLIP, to I-A major histocompatibility complex class II molecules

Autor: Anand Gautam, Vanda Quinn, Peter J. Milburn, C.I. Pearson, Hugh O. McDevitt

Publikováno v: Proceedings of the National Academy of Sciences. 92:335-339

Invariant chain (Ii) associates with major histocompatibility complex (MHC) class II molecules and is crucial for antigen presentation by class II molecules. The exact nature of Ii interaction with MHC class II molecules remains undefined. A nested s

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2361d97bce118bf0a308213bf3733f2a
https://doi.org/10.1073/pnas.92.1.335

Zobrazit plný text záznamu

Reductions of Rubisco activase by antisense RNA in the C4 plant Flaveria bidentis reduces Rubisco carbamylation and leaf photosynthesis

Autor: Vanda Quinn, Susanne von Caemmerer, A G Millgate, Luke Hendrickson, N Vella, Robert T. Furbank

Publikováno v: Plant physiology. 137(2)

To function, the catalytic sites of Rubisco (EC 4.1.1.39) need to be activated by the reversible carbamylation of a lysine residue within the sites followed by rapid binding of magnesium. The activation of Rubisco in vivo requires the presence of the

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ce580f0d2a5f4d556e180d4c9b124299
https://pubmed.ncbi.nlm.nih.gov/15665240

Zobrazit plný text záznamu

Vyhledávací nástroje:

Upřesnit hledání