NAD synthase: Difference between revisions

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<StructureSection load='1xng' size='350' side='right' caption='NAD+ synthase complex with Mg+2 (green), ATP (stick model) and deamino-NAD (PDB entry [[1xng]])' scene=''>


{{STRUCTURE_1ee1|  PDB=1ee1  | SIZE=350| SCENE= |right|CAPTION= NAD+ synthase complex with Mg+2 (green), ATP (stick model) and deamino-NAD [[1ee1]] }}
== Function ==
'''NAD+ synthase''' (NADS) catalyzes the conversion of ATP, deamino-NAD+ and NH<sub>3</sub> to AMP, NAD+ and diphosphate (PP).  NADS is part of the NAD synthesis pathway<ref>PMID:12898714</ref> .  See [[NAD]].


'''NAD+ synthase''' (NADS) catalyzes the conversion of ATP, deamino-NAD+ and NH<sub>3</sub> to AMP, NAD+ and diphosphate (PP)NADS is part of the NAD synthesis pathway<ref>PMID:12898714</ref> .  See [[NAD]].
== Structural highlights ==
The ATP binding site contains Mg+2 ionThe NAD binding site is located in the interface of the 2 subunits<ref>PMID:15645437</ref>.


== 3D Structures of NAD+ synthase ==
== 3D Structures of NAD+ synthase ==

Revision as of 13:43, 4 May 2016

<StructureSection load='1xng' size='350' side='right' caption='NAD+ synthase complex with Mg+2 (green), ATP (stick model) and deamino-NAD (PDB entry 1xng)' scene=>

FunctionFunction

NAD+ synthase (NADS) catalyzes the conversion of ATP, deamino-NAD+ and NH3 to AMP, NAD+ and diphosphate (PP). NADS is part of the NAD synthesis pathway[1] . See NAD.

Structural highlightsStructural highlights

The ATP binding site contains Mg+2 ion. The NAD binding site is located in the interface of the 2 subunits[2].

3D Structures of NAD+ synthase3D Structures of NAD+ synthase

Updated on 04-May-2016

ReferencesReferences

  1. Suda Y, Tachikawa H, Yokota A, Nakanishi H, Yamashita N, Miura Y, Takahashi N. Saccharomyces cerevisiae QNS1 codes for NAD(+) synthetase that is functionally conserved in mammals. Yeast. 2003 Aug;20(11):995-1005. PMID:12898714 doi:http://dx.doi.org/10.1002/yea.1008
  2. Kang GB, Kim YS, Im YJ, Rho SH, Lee JH, Eom SH. Crystal structure of NH3-dependent NAD+ synthetase from Helicobacter pylori. Proteins. 2005 Mar 1;58(4):985-8. PMID:15645437 doi:10.1002/prot.20377

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, Joel L. Sussman