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NAD Kinase Is an AKT Substrate.
Cancer Discovery, 2019AKT-mediated phosphorylation of NAD kinase induces synthesis of NADP+ and NADPH.
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Probing binding requirements of NAD kinase with modified substrate (NAD) analogues
Bioorganic and 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.
Krzysztof Felczak +2 more
exaly +3 more sources
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. McGuinness, J. R. G. 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. McGuinness, J. R. G. Butler
semanticscholar +3 more sources
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 +2 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 +2 more
exaly +3 more sources
Activation of calmodulin-dependent NAD+ kinase by trypsin
BBA - Proteins and Proteomics, 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.
Laurent Meijer, Pierre Guerrier
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Compact NAD mimics as selective inhibitors of NAD kinases
, 2009 We have examined sequence diversity of 147 co-crystal structures of proteins utilizing NAD as a cofactor or as a substrate. Most of these proteins bind NAD in an extended conformation (e.g. the distance between the adenine 6-amino group of NAD and the nicotinamide amide carbon is 16 Å or more). However, there are clear exceptions to this general trend.
PETRELLI, Riccardo +6 more
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PROBING BINDING REQUIREMENTS OF NAD KINASE WITH MODIFIED NAD ANALOGUES
, 2012 NAD kinase (NADK) catalyzes a magnesium-dependent phosphorylation of the 2′-hydroxyl group of the adenosine ribose moiety of nicotinamide adenine dinucleotide (NAD) using ATP or inorganic polyphosphates as phosphoryl donors to give NADP. There are two classes of the enzyme, one is specific for NAD+ and the other also phosphorylates NADH.
PETRELLI, Riccardo +9 more
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NMN-Adenylyltransferase und NAD+-Kinase [PDF]
, 2003 Die beiden Nukleotide NAD+ und NADP+ sind essentielle Coenzyme für zahlreiche Redoxreaktionen in allen bekannten Organismen. Sie sind außerdem Vorstufen für Signalmoleküle und Substrate für kovalente Proteinmodifikationen in höheren Eukaryoten. Bislang lagen zu den essentiellen Enzymen der NAD(P)+-Synthese, der NMNAT und der NAD+-Kinase, keine ...
Berger, Felicitas
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Enzymatic Characteristics of a Polyphosphate/ATP-NAD Kinase, PanK, from Myxococcus xanthus
Current Microbiology, 2019Yoshio Kimura +2 more
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Current Medicinal Chemistry, 2011 Nicotinamide adenine dinucleotide (NAD+) has a crucial role in many cellular processes, both as a coenzyme for redox reactions and as a substrate to donate ADP-ribose units.
R. Petrelli, K. Felczak, L. Cappellacci
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