Results 251 to 260 of about 73,229 (276)
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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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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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Activation of calmodulin-dependent NAD+ kinase by trypsin
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1982Sea urchin egg NAD+ kinase (ATP:NAD+ 2'-phosphotransferase, EC 2.7.1.23), a calmodulin-dependent enzyme, can be activated by a moderate treatment with trypsin in a similar fashion to calmodulin. Stimulation by trypsin is dependent on its concentration (half-maximal dose: 1.5 microgram/ml) but independent of the presence of calcium.
L, Meijer, P, Guerrier
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[119] NAD+ kinase in liver tissue
1971Publisher Summary This chapter discusses the assay method, purification procedure, and properties of the enzyme nicotinamide adenine dinucleotide (NAD + ) kinase in frozen rat and calf liver tissue. The nicotinamide adenine dinucleotide phosphate (NADP + ) formed in the reaction mixture is assayed by method based on the measurement of the change in ...
L.S. Dietrich, I.L. Yero
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[ATP and polyphosphate-dependent bacterial NAD+-kinases].
Prikladnaia biokhimiia i mikrobiologiia, 2000Measurable levels of activity of NAD+ kinases of actinomycetes Micrococcus luteus and Corynebacterium ammoniagenes were observed after substituting inorganic tripolyphosphate for ATP, whereas the enzyme from the eubacterium Escherichia coli was not active with this substrate. Gradient PAGE found two molecular isoforms of NAD+ kinase in C.
S Iu, Filippovich +3 more
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