Results 301 to 310 of about 133,635 (341)
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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.
James R. Butler, Eugene T. McGuinness
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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.
James R. Butler, Eugene T. McGuinness
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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
François Graham +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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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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THE INDUCTION OF NAD KINASE BY DDT IN TRIATOMA INFESTANS
Canadian Journal of Biochemistry, 1967The NAD kinase (EC 2.7.1.23) from Triatoma infestans has been purified and a specific antiserum against it prepared. Immunochemical techniques have shown that the increase in the levels of NAD kinase in nymphs of T. infestans is accompanied by an increase in the amount of enzyme protein.
Moises Agosin +2 more
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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.
Toru Hayashi +2 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
Mary B. Williams, Harold P. Jones
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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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Developmental Ontogeny of NAD+ Kinase in the Rat Conceptus
Toxicology and Applied Pharmacology, 2001The ubiquitous NAD+ kinase (NADK) is the only known enzyme to catalyze formation of NADP+ from NAD+. The capacity to maintain an adequate supply of NADP(H) has important implications for development because of its requirement as a cofactor and electron donor in biosynthesis and detoxication reactions.
Surekha S. Akella, Craig Harris
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Production of NADP by immobilized cells with NAD kinase
Biotechnology and Bioengineering, 1982AbstractBy the radiation‐copolymerization method with polyethylene glycoldimethacrylate (PGD) as a main polymerizable reagent, microbial cells of Brevibacterium ammoniagenes were immobilized with high specific activity of NAD kinase and high mechanical strength.
Toshio Watanabe +4 more
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