1dap

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[[Image:1dap.gif|left|200px]]<br />
 
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<applet load="1dap" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1dap, resolution 2.2&Aring;" />
 
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'''C. GLUTAMICUM DAP DEHYDROGENASE IN COMPLEX WITH NADP+'''<br />
 
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==Overview==
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==C. GLUTAMICUM DAP DEHYDROGENASE IN COMPLEX WITH NADP+==
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Diaminopimelate dehydrogenase catalyzes the NADPH-dependent reduction of, ammonia and L-2-amino-6-ketopimelate to form meso-diaminopimelate, the, direct precursor of L-lysine in the bacterial lysine biosynthetic pathway., Since mammals lack this metabolic pathway inhibitors of enzymes in this, pathway may be useful as antibiotics or herbicides. Diaminopimelate, dehydrogenase catalyzes the only oxidative deamination of an amino acid of, D configuration and must additionally distinguish between two chiral amino, acid centers on the same symmetric substrate. The Corynebacterium, glutamicum enzyme has been cloned, expressed in Escherichia coli, and, purified to homogeneity using standard biochemical procedures [Reddy, S., G., Scapin, G., &amp; Blanchard, J. S. (1996) Proteins: Structure, ... [[http://ispc.weizmann.ac.il/pmbin/getpm?8885833 (full description)]]
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<StructureSection load='1dap' size='340' side='right'caption='[[1dap]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1dap]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Corynebacterium_glutamicum Corynebacterium glutamicum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DAP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DAP FirstGlance]. <br>
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1DAP is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Corynebacterium_glutamicum Corynebacterium glutamicum]] with ACT and NDP as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/Diaminopimelate_dehydrogenase Diaminopimelate dehydrogenase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.1.16 1.4.1.16]]. Structure known Active Sites: ACE, N1 and N2. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DAP OCA]].
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene></td></tr>
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==Reference==
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1dap FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dap OCA], [https://pdbe.org/1dap PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dap RCSB], [https://www.ebi.ac.uk/pdbsum/1dap PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dap ProSAT]</span></td></tr>
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Three-dimensional structure of meso-diaminopimelic acid dehydrogenase from Corynebacterium glutamicum., Scapin G, Reddy SG, Blanchard JS, Biochemistry. 1996 Oct 22;35(42):13540-51. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8885833 8885833]
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/DAPDH_CORGL DAPDH_CORGL] Catalyzes the reversible NADPH-dependent reductive amination of L-2-amino-6-oxopimelate, the acyclic form of L-tetrahydrodipicolinate, to generate the meso compound, D,L-2,6-diaminopimelate. Probably plays a role in lysine biosynthesis. Exhibits a high substrate specificity for meso-2,6-diaminopimelate, since L,L-2,6-diaminopimelate, D,D-2,6-diaminopimelate, L-glutamate, L-alanine, L-leucine, L-valine, L-aspartate, L-threonine, L-homoserine, L-methionine, L-lysine, L-serine, L-phenylalanine, L-tyrosine, L-tryptophan, L-ornithine, L-histidine, L-arginine, D-glutamate, and D-alanine are not substrates for the oxidative deamination reaction. Can use NAD(+) only poorly since the activity observed in the presence of NAD(+) is about 3% of that with NADP(+).<ref>PMID:8865347</ref> <ref>PMID:8865347</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/da/1dap_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1dap ConSurf].
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<div style="clear:both"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Corynebacterium glutamicum]]
[[Category: Corynebacterium glutamicum]]
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[[Category: Diaminopimelate dehydrogenase]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Blanchard JS]]
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[[Category: Blanchard, J.S.]]
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[[Category: Reddy SG]]
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[[Category: Reddy, S.G.]]
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[[Category: Scapin G]]
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[[Category: Scapin, G.]]
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[[Category: ACT]]
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[[Category: NDP]]
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[[Category: asymmetric dimer]]
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[[Category: d-amino acid dehydrogenase]]
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[[Category: dehydrogenase]]
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[[Category: lysine biosynthesis]]
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[[Category: nadp]]
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[[Category: oxidoreductase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 13:46:40 2007''
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Current revision

C. GLUTAMICUM DAP DEHYDROGENASE IN COMPLEX WITH NADP+

PDB ID 1dap

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