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Protein kinase C activates NAD kinase in human neutrophils
Free Radical Biology and Medicine, 2020NAD kinase (NADK) is required for the de novo synthesis of NADP+ from NAD+. In neutrophils, NADK plays an essential role by providing sufficient levels of NADPH to support a robust oxidative burst. Activation of NADPH oxidase-2 (NOX-2) in neutrophils by stimulators of protein kinase C (PKC), such as phorbol myristate acetate (PMA), results in the rapid
Razieh, Rabani +3 more
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International Journal of Biochemistry, 1985
NAD+ kinase catalyzes the only (known) biochemical reaction leading to the production of NADP+ from NAD+. Most evidence indicates it is found in the cytoplasm, but reports of its presence in (other) cell bodies can not be discounted. Viewed as a protein, our knowledge of NADK composition and architecture is rudimentary.
E T, McGuinness, J R, Butler
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NAD+ kinase catalyzes the only (known) biochemical reaction leading to the production of NADP+ from NAD+. Most evidence indicates it is found in the cytoplasm, but reports of its presence in (other) cell bodies can not be discounted. Viewed as a protein, our knowledge of NADK composition and architecture is rudimentary.
E T, McGuinness, J R, Butler
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Trends in Biochemical Sciences, 2002
Diacylglyceride kinases, sphingosine kinases, NAD kinases and 6-phosphofructokinases are thought to be related despite large evolution of their sequences. Discovery of a common signature has led to the suggestion that they possess a similar phosphate-donor-binding site and a similar phosphorylation mechanism. The substrate- and allosteric-binding sites
Labesse, Gilles +3 more
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Diacylglyceride kinases, sphingosine kinases, NAD kinases and 6-phosphofructokinases are thought to be related despite large evolution of their sequences. Discovery of a common signature has led to the suggestion that they possess a similar phosphate-donor-binding site and a similar phosphorylation mechanism. The substrate- and allosteric-binding sites
Labesse, Gilles +3 more
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Probing binding requirements of NAD kinase with modified substrate (NAD) analogues
Bioorganic & Medicinal Chemistry Letters, 2007Synthesis of novel NAD(+) analogues that cannot be phosphorylated by NAD kinase is reported. In these analogues the C2' hydroxyl group of the adenosine moiety was replaced by fluorine in the ribo or arabino configuration (1 and 2, respectively) or was inverted into arabino configuration to give compound 3.
Laurent, Bonnac +11 more
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Calmodulin-dependent NAD kinase of human neutrophils
Archives of Biochemistry and Biophysics, 1985NAD kinase from human neutrophils has been partially purified by sequential application of Red Agarose, ion-exchange, and gel-filtration chromatography. The enzyme has a broad pH optimum, 7.0-9.5, is strictly dependent upon the presence of Mg2+, and in the absence of calcium exhibits Km values of 0.6 and 0.9 mM for NAD and ATP, respectively. NAD kinase
M B, Williams, H P, Jones
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Immobilization of microbial cells containing NAD‐kinase
Biotechnology and Bioengineering, 1979AbstractMicrobial cells having NAD‐kinase activity, Brevibacterium ammoniagenes, were immobilized by the radiation‐copolymerization method under low temperature with the activity recovery of more than 80%. Compared to the native microbial cells the immobilized cells were more stable against heat and pH change.
T, Hayashi, Y, Tanaka, K, Kawashima
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PROPERTIES OF RAT BRAIN NAD‐KINASE
Journal of Neurochemistry, 1970Abstract— NAD‐kinase was purified from rat brain acetone powder according to the method of Wang and Kaplan (1954). The acetate buffer supernatant showed only very low specific activity but was largely free of the factors that interfere with the enzyme assay. The Michaelis constants for both substrates were determined, the values were 0·5 mm for NAD and
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Journal of Bioscience and Bioengineering, 2004
NAD kinase from Mycobacterium tuberculosis (Ppnk) uses ATP or inorganic polyphosphate [poly(P)]. Ppnk overexpressed in Escherichia coli was purified and crystallized in the presence of NAD. Preliminary X-ray analysis of the resultant crystal indicate that the crystal belongs to hexagonal space group P6(2)22 and is holo-Ppnk complexed with NAD.
Shigetarou, Mori +7 more
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NAD kinase from Mycobacterium tuberculosis (Ppnk) uses ATP or inorganic polyphosphate [poly(P)]. Ppnk overexpressed in Escherichia coli was purified and crystallized in the presence of NAD. Preliminary X-ray analysis of the resultant crystal indicate that the crystal belongs to hexagonal space group P6(2)22 and is holo-Ppnk complexed with NAD.
Shigetarou, Mori +7 more
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Developmental regulation of NAD+ kinase in Neurospora crassa
Archives of Microbiology, 1982The specific activity of NAD+ kinase (ATP:NAD+ 2'-phosphotransferase, EC 2.7.1.23) from Neurospora crassa shows sharp peaks when the organism enters a new developmental stage of the asexual life cycle: the peaks are observed during hydration and germination of conidia, at the transition from exponential to stationary growth and at the photostimulated ...
T P, Afanasieva +3 more
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Structural and Functional Characterization of Human NAD Kinase
Biochemical and Biophysical Research Communications, 2001NADP is essential for biosynthetic pathways, energy, and signal transduction. Its synthesis is catalyzed by NAD kinase. Very little is known about the structure, function, and regulation of this enzyme from multicellular organisms. We identified a human NAD kinase cDNA and the corresponding gene using available database information.
F, Lerner +3 more
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