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5loc
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of the engineered D-Amino Acid Dehydrogenase (DAADH)== | |
| - | + | <StructureSection load='5loc' size='340' side='right' caption='[[5loc]], [[Resolution|resolution]] 2.04Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[5loc]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"micrococcus_glutamicus"_kinoshita_et_al._1958 "micrococcus glutamicus" kinoshita et al. 1958]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LOC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5LOC FirstGlance]. <br> | |
| - | + | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ddh, Cgl2617, cg2900 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1718 "Micrococcus glutamicus" Kinoshita et al. 1958])</td></tr> | |
| - | [[Category: | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr> |
| - | [[Category: Dunstan, M | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5loc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5loc OCA], [http://pdbe.org/5loc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5loc RCSB], [http://www.ebi.ac.uk/pdbsum/5loc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5loc ProSAT]</span></td></tr> |
| + | </table> | ||
| + | == Function == | ||
| + | [[http://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> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Micrococcus glutamicus kinoshita et al. 1958]] | ||
| + | [[Category: Diaminopimelate dehydrogenase]] | ||
| + | [[Category: Dunstan, M S]] | ||
[[Category: Gahloth, D]] | [[Category: Gahloth, D]] | ||
| + | [[Category: Amino acid]] | ||
| + | [[Category: Asymmetric synthesis]] | ||
| + | [[Category: Biocatalysis]] | ||
| + | [[Category: Daadh]] | ||
| + | [[Category: Enzyme catalysis]] | ||
| + | [[Category: Oxidoreductase]] | ||
Revision as of 23:55, 15 November 2017
Crystal structure of the engineered D-Amino Acid Dehydrogenase (DAADH)
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