Výsledky vyhledávání - "Natalia V. Ermolova"

Expression, purification, and initial characterization of a recombinant form of plant PEP-carboxylase kinase from CAM-induced Mesembryanthemum crystallinum with enhanced solubility in Escherichia coli

Autor: Raymond Chollet, Natalia V. Ermolova, Tahar Taybi, John C. Cushman, Mary Ann Cushman, Shirley A. Condon

Publikováno v: Protein Expression and Purification. 29:123-131

Plant phosphoenolpyruvate-carboxylase kinase (PEPC-kinase [PpcK]) is the smallest Ser/Thr kinase identified to date, having a molecular mass of approximately 32,000. This novel, monomeric kinase is dedicated to the phosphorylation of plant PEPC, ther

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::774c84ed5dbf7dded04c27bf593af5c0
https://doi.org/10.1016/s1046-5928(03)00014-7

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Partial purification and biochemical characterization of a heteromeric protein phosphatase 2A holoenzyme from maize (Zea mays L.) leaves that dephosphorylates C4 phosophoenolpyruvate carboxylase

Autor: Longying Dong, Raymond Chollet, Natalia V. Ermolova

Publikováno v: Planta. 213(3)

The activity and allosteric properties of plant phosphoenolpyruvate carboxylase (PEPC; EC 4.1.1.31) are controlled posttranslationally by specific reversible phosphorylation of a strictly conserved serine residue near the N-terminus. This up/down-reg

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e7e64f85f1ee137e20633bbd1f8a63af
https://pubmed.ncbi.nlm.nih.gov/11506360

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