6a3j
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Levoglucosan dehydrogenase, complex with NADH and L-sorbose== | |
| + | <StructureSection load='6a3j' size='340' side='right' caption='[[6a3j]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6a3j]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6A3J OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6A3J FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=NAI:1,4-DIHYDRONICOTINAMIDE+ADENINE+DINUCLEOTIDE'>NAI</scene>, <scene name='pdbligand=SOE:ALPHA-L-SORBOPYRANOSE'>SOE</scene></td></tr> | ||
| + | <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=6a3j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6a3j OCA], [http://pdbe.org/6a3j PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6a3j RCSB], [http://www.ebi.ac.uk/pdbsum/6a3j PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6a3j ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | A levoglucosan (1,6-anhydro-beta-D-glucopyranose)-using bacterium, isolated from soil, was identified. It was shown to belong to the genus Arthrobacter and tentatively named Arthrobacter sp. I-552. A novel enzyme catalyzed the dehydrogenation of levoglucosan to form 1,6-anhydro-beta-D-ribo-hexopyranos-3-ulose (3-keto levoglucosan), using NAD+ as an electron acceptor, i.e. NAD+: 1,6-anhydro-beta-D-glucopyranose oxidoreductase (trivial name: levoglucosan dehydrogenase). This enzyme was purified and characterized. A possible reaction scheme for the glucose formation was proposed. This pathway for levoglucosan use is distinct from those in yeast and fungi. | ||
| - | + | Levoglucosan dehydrogenase involved in the assimilation of levoglucosan in Arthrobacter sp. I-552.,Nakahara K, Kitamura Y, Yamagishi Y, Shoun H, Yasui T Biosci Biotechnol Biochem. 1994 Dec;58(12):2193-6. doi: 10.1271/bbb.58.2193. PMID:7765713<ref>PMID:7765713</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 6a3j" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Arakawa, T]] | ||
| + | [[Category: Fushinobu, S]] | ||
| + | [[Category: Sugiura, M]] | ||
| + | [[Category: Yamada, C]] | ||
| + | [[Category: Gfo/idh/moca family]] | ||
| + | [[Category: Nadh-dependent dehydrogenase]] | ||
| + | [[Category: Oxidoreductase]] | ||
| + | [[Category: Rossmann fold]] | ||
Revision as of 07:59, 26 September 2018
Levoglucosan dehydrogenase, complex with NADH and L-sorbose
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