Direct stimulation of NADP + synthesis through Akt-mediated phosphorylation of NAD kinase
Author(s) -
Gerta Hoxhaj,
Issam BenSahra,
Sophie E. Lockwood,
Rebecca C. Timson,
Vanessa Byles,
Graham T. Henning,
Peng Gao,
Laura M. Selfors,
John M. Asara,
Brendan D. Manning
Publication year - 2019
Publication title -
science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 12.556
H-Index - 1186
eISSN - 1095-9203
pISSN - 0036-8075
DOI - 10.1126/science.aau3903
Subject(s) - nad+ kinase , nicotinamide adenine dinucleotide phosphate , protein kinase b , cofactor , phosphorylation , nicotinamide adenine dinucleotide , biochemistry , nicotinamide , chemistry , kinase , biology , enzyme , oxidase test
Akt produces reducing power The protein kinase Akt provides a link from growth factors to the production of metabolic reducing power within the cell. Hoxhajet al. discovered that Akt directly phosphorylates nicotinamide adenine dinucleotide kinase (NADK). Catalytic activity of NADK is normally inhibited by its own amino-terminal domain, and phosphorylation by Akt relieved this inhibition. Active NADK produces nicotinamide adenine dinucleotide phosphate (NADP+ ). NADP+ in turn is required to produce the reduced form of NADP+ (NADPH), which is the primary cofactor for reductive metabolism in the cell.Science , this issue p.1088
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