NAD kinase: Difference between revisions
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<StructureSection load='' size=' | <StructureSection load='' size='350' side='right' caption='NAD kinase complex with NADP and sulfate (PDB code [[1z0u]])' scene='71/715900/Cv/1'> | ||
== 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]]. | '''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]]. | ||
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**[[5ejf]], [[5ejg]], [[5ejh]] – LmNADK (mutant) <br /> | **[[5ejf]], [[5ejg]], [[5ejh]] – LmNADK (mutant) <br /> | ||
**[[4hao]] – NADK – ''Yersinia pestis''<br /> | **[[4hao]] – NADK – ''Yersinia pestis''<br /> | ||
**[[ | **[[3pfn]] – NADK – human<br /> | ||
*NAD kinase complex | *NAD kinase complex |
Revision as of 12:00, 12 August 2018
FunctionNAD 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 highlightsin a cleft between the N and C-terminal domains in the dimer interface[2]. Water molecules shown as red spheres.
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3D structures of NAD kinase3D structures of NAD kinase
Updated on 12-August-2018
ReferencesReferences
- ↑ 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
- ↑ 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