Results 11 to 20 of about 70,171 (129)

NAD Kinase in Higher Plants [PDF]

open access: bronzePlant Physiology, 1966
NAD kinase was exclusively found in the soluble portion of the cell components. The enzyme was purified about 100-fold from sucrose extracts of spinach leaves.Plant NAD kinase catalyzes formation of NADP from NAD, ATP, and Mg(++), but scarcely any formation of NADPH from NADH. NADH was a very potent competitive inhibitor of NAD phosphorylation by plant
Yukio Yamamoto
openaire   +5 more sources

Identification and characterization of a human mitochondrial NAD kinase [PDF]

open access: hybridNature Communications, 2012
NAD kinase is the sole NADP(+) biosynthetic enzyme. Despite the great significance of NADP(+), to date no mitochondrial NAD kinase has been identified in human, and the source of human mitochondrial NADP(+) remains elusive. Here we present evidence demonstrating that a human protein of unknown function, C5orf33, is a human mitochondrial NAD kinase ...
Ohashi, Kazuto   +2 more
openaire   +4 more sources

The Substrate Specificity of Pigeon Liver NAD Kinase [PDF]

open access: bronzeEuropean Journal of Biochemistry, 1969
The specificity of pigeon liver NAD kinase for both substrates and for divalent cations has been investigated. 2. The enzyme is activated by Mg++, Co++, Mn++, and Zn++ only: the ATP‐metal complexes have different Km, values but the maximum velocities of the reactions are the same. 3.
D.K. Apps
openaire   +5 more sources

Molecular characterization of Escherichia coli NAD kinase [PDF]

open access: bronzeEuropean Journal of Biochemistry, 2001
NAD kinase was purified to homogeneity from Escherichia coli MG1655. The enzyme was a hexamer consisting of 30 kDa subunits and utilized ATP or other nucleoside triphosphates as phosphoryl donors for the phosphorylation of NAD, most efficiently at pH 7.5 and 60 °C.
Kousaku Murata   +4 more
openaire   +5 more sources

NAD+ Kinase as a Therapeutic Target in Cancer [PDF]

open access: yesClinical Cancer Research, 2016
Abstract NAD+ kinase (NADK) catalyzes the phosphorylation of nicotinamide adenine dinucleotide (NAD+) to nicotinamide adenine dinucleotide phosphate (NADP+) using ATP as the phosphate donor. NADP+ is then reduced to NADPH by dehydrogenases, in particular glucose-6-phosphate dehydrogenase and the malic enzymes.
Kathleen W. Scotto   +5 more
openaire   +2 more sources

Physiological Significance of NAD Kinases in Cyanobacteria

open access: yesFrontiers in Plant Science, 2019
Unicellular cyanobacteria are thought to be the evolutionary ancestors of plant chloroplasts and are widely used both for chemical production and as model organisms in studies of photosynthesis. Although most research focused on increasing reducing power (that is, NADPH) as target of metabolic engineering, the physiological roles of NAD(P)(H) in ...
Maki Kawai-Yamada, Yuuma Ishikawa
openaire   +4 more sources

Evidence for two NAD kinases in Salmonella typhimurium [PDF]

open access: yesJournal of Bacteriology, 1994
The electron-carrying cofactor NADP is formed by phosphorylation of NAD. A strategy for the isolation of NAD kinase mutants revealed two classes of temperature-sensitive mutations, nadF and nadG, mapping at min 13 and 72 of the Salmonella chromosome.
Weili Cheng, John R. Roth
openaire   +3 more sources

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