NAD kinase: Difference between revisions

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<StructureSection load='1z0u' size='340' side='right' caption='NAD kinase complex with NADP and sulfate (PDB code [[1z0u]]' scene=''>
<StructureSection load='1z0u' size='340' side='right' caption='NAD kinase complex with NADP and sulfate (PDB code [[1z0u]]' scene=''>
'''NAD kinase''' (NADK) catalyzes the conversion of ATP and [[NAD]] to ADP and NADP.  NADP is critical for metabolism, calcium signaling and anti-inflammatory processes.  NADK is regulated by calmodulin-dependent mechanism. See [[NAD]] and [[NAD(P)H]].
== Function ==
== Function ==
 
'''NAD kinase''' (NADK) catalyzes the conversion of ATP and [[NAD]] to ADP and NADP.  NADP is critical for metabolism, calcium signaling and anti-inflammatory processes.  NADK is regulated by calmodulin-dependent mechanism<ref>PMID:23212377</ref>. See [[NAD]] and [[NAD(P)H]].
== Disease ==
 
== Relevance ==


== Structural highlights ==
== Structural highlights ==
 
NADP is bound to NADK in a cleft between the N and C-terminal domains in the dimer interface<ref>PMID:16242716</ref>.


</StructureSection>
</StructureSection>

Revision as of 12:38, 4 May 2016

Function

NAD kinase (NADK) catalyzes the conversion of ATP and NAD to ADP and NADP. NADP is critical for metabolism, calcium signaling and anti-inflammatory processes. NADK is regulated by calmodulin-dependent mechanism[1]. See NAD and NAD(P)H.

Structural highlights

NADP is bound to NADK in a cleft between the N and C-terminal domains in the dimer interface[2].


NAD kinase complex with NADP and sulfate (PDB code 1z0u

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3D structures of NAD kinase3D structures of NAD kinase

Updated on 04-May-2016

ReferencesReferences

  1. Ohashi K, Kawai S, Murata K. Identification and characterization of a human mitochondrial NAD kinase. Nat Commun. 2012;3:1248. doi: 10.1038/ncomms2262. PMID:23212377 doi:http://dx.doi.org/10.1038/ncomms2262
  2. Liu J, Lou Y, Yokota H, Adams PD, Kim R, Kim SH. Crystal structures of an NAD kinase from Archaeoglobus fulgidus in complex with ATP, NAD, or NADP. J Mol Biol. 2005 Nov 25;354(2):289-303. Epub 2005 Sep 30. PMID:16242716 doi:10.1016/j.jmb.2005.09.026

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Michal Harel, Alexander Berchansky, Joel L. Sussman