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{{enzyme
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| Name = NAD<sup>+</sup> kinase
| EC_number = 2.7.1.23
| CAS_number = 9032-66-0
| IUBMB_EC_number = 2/7/1/23
| GO_code = 0003951
| image = NADK.png
| width =
| caption = Ribbon diagram of NAD<sup>+</sup> kinase in complex with substrates.<ref name="pmid16242716">{{PDB|1SUW}}; {{cite journal | author = Liu J, Lou Y, Yokota H, Adams PD, Kim R, Kim SH | title = Crystal structures of an NAD kinase from Archaeoglobus fulgidus in complex with ATP, NAD, or NADP | journal = J. Mol. Biol. | volume = 354 | issue = 2 | pages = 289–303 |date=November 2005 | pmid = 16242716 | doi = 10.1016/j.jmb.2005.09.026 | url =  }}</ref>
}}
{{PBB|geneid=65220}}
 
'''NAD<sup>+</sup> kinase''' (EC 2.7.1.23, NADK) is an enzyme that converts [[nicotinamide adenine dinucleotide]] (NAD<sup>+</sup>) into NADP<sup>+</sup>, through phosphorylating the NAD<sup>+</sup> [[coenzyme]].<ref>{{cite journal |author=Magni G, Orsomando G, Raffaelli N |title=Structural and functional properties of NAD kinase, a key enzyme in NADP biosynthesis |journal=Mini reviews in medicinal chemistry |volume=6 |issue=7 |pages=739–46 |year=2006 |pmid=16842123 |doi=10.2174/138955706777698688}}</ref> NADP<sup>+</sup> is an essential coenzyme in [[metabolism]] and provides reducing power to biosynthetic processes such as [[fatty acid biosynthesis]].<ref>{{cite journal |author=Pollak N, Dölle C, Ziegler M |title=The power to reduce: pyridine nucleotides – small molecules with a multitude of functions |journal=Biochem. J. |volume=402 |issue=2 |pages=205–18 |year=2007 |pmid=17295611 |doi=10.1042/BJ20061638 |pmc=1798440}}</ref> The structure of the NADK from the [[archaea]]n ''[[Archaeoglobus|Archaeoglobus fulgidus]]'' has been determined.<ref name="pmid16242716"/>
 
In humans, NAD<sup>+</sup> kinase is encoded by the ''NADK'' [[gene]].<ref name="pmid11594753">{{cite journal | author = Lerner F, Niere M, Ludwig A, Ziegler M | title = Structural and functional characterization of human NAD kinase | journal = Biochem. Biophys. Res. Commun. | volume = 288 | issue = 1 | pages = 69–74 |date=October 2001 | pmid = 11594753 | doi = 10.1006/bbrc.2001.5735 | url =  }}</ref>
 
== Reaction ==
 
[[Adenosine triphosphate|ATP]] + [[Nicotinamide adenine dinucleotide|NAD<sup>+</sup>]] <math>\rightleftharpoons</math> [[Adenosine diphosphate|ADP]] + [[Nicotinamide adenine dinucleotide phosphate|NADP<sup>+</sup>]]
 
==See also==
*[[Oxidative phosphorylation]]
*[[Electron transport chain]]
*[[Metabolism]]
 
==References==
{{reflist}}
 
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal  | author=Andersson B, Wentland MA, Ricafrente JY, ''et al.'' |title=A "double adaptor" method for improved shotgun library construction |journal=Anal. Biochem. |volume=236 |issue= 1 |pages= 107–13 |year= 1996 |pmid= 8619474 |doi= 10.1006/abio.1996.0138 }}
*{{cite journal  | author=Yu W, Andersson B, Worley KC, ''et al.'' |title=Large-Scale Concatenation cDNA Sequencing |journal=Genome Res. |volume=7 |issue= 4 |pages= 353–8 |year= 1997 |pmid= 9110174 |doi=  10.1101/gr.7.4.353| pmc=139146  }}
*{{cite journal  | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899  | pmc=139241 }}
*{{cite journal  | author=Ota T, Suzuki Y, Nishikawa T, ''et al.'' |title=Complete sequencing and characterization of 21,243 full-length human cDNAs |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40–5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
*{{cite journal  | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |title=The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC) |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504  | pmc=528928 }}
*{{cite journal  | author=Stelzl U, Worm U, Lalowski M, ''et al.'' |title=A human protein-protein interaction network: a resource for annotating the proteome |journal=Cell |volume=122 |issue= 6 |pages= 957–68 |year= 2005 |pmid= 16169070 |doi= 10.1016/j.cell.2005.08.029 }}
*{{cite journal  | author=Rual JF, Venkatesan K, Hao T, ''et al.'' |title=Towards a proteome-scale map of the human protein-protein interaction network |journal=Nature |volume=437 |issue= 7062 |pages= 1173–8 |year= 2005 |pmid= 16189514 |doi= 10.1038/nature04209 }}
*{{cite journal  | author=Gregory SG, Barlow KF, McLay KE, ''et al.'' |title=The DNA sequence and biological annotation of human chromosome 1 |journal=Nature |volume=441 |issue= 7091 |pages= 315–21 |year= 2006 |pmid= 16710414 |doi= 10.1038/nature04727 }}
*{{cite journal  | author=Ewing RM, Chu P, Elisma F, ''et al.'' |title=Large-scale mapping of human protein–protein interactions by mass spectrometry |journal=Mol. Syst. Biol. |volume=3 |issue=  1|pages= 89 |year= 2007 |pmid= 17353931 |doi= 10.1038/msb4100134  | pmc=1847948 }}
*{{cite journal  | author=Pollak N, Niere M, Ziegler M |title=NAD kinase levels control the NADPH concentration in human cells |journal=J. Biol. Chem. |volume=282 |issue= 46 |pages= 33562–71 |year= 2008 |pmid= 17855339 |doi= 10.1074/jbc.M704442200 }}
}}
{{refend}}
 
==External links==
*[http://au.expasy.org/enzyme/2.7.1.23 ENZYME entry on EC 2.7.1.23]
*[http://www.brenda-enzymes.org/php/result_flat.php4?ecno=2.7.1.23 BRENDA entry on EC 2.7.1.23]
 
{{Kinases}}
 
{{DEFAULTSORT:Nad+ Kinase}}
[[Category:EC 2.7.1]]
[[Category:Cellular respiration]]
[[Category:Metabolism]]
[[Category:Human proteins]]
 
 
{{transferase-stub}}
{{metabolism-stub}}

Latest revision as of 08:05, 20 February 2014

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