This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
4cnk
From Proteopedia
(Difference between revisions)
m (Protected "4cnk" [edit=sysop:move=sysop]) |
|||
| Line 1: | Line 1: | ||
| - | ''' | + | ==L-Aminoacetone oxidase from Streptococcus oligofermentans belongs to a new 3-domain family of bacterial flavoproteins== |
| + | <StructureSection load='4cnk' size='340' side='right' caption='[[4cnk]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4cnk]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CNK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CNK FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MEU:O-METHYL-GLYCINE'>MEU</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4cnj|4cnj]]</td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Lactate_2-monooxygenase Lactate 2-monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.13.12.4 1.13.12.4] </span></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=4cnk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cnk OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4cnk RCSB], [http://www.ebi.ac.uk/pdbsum/4cnk PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The aaoso gene from Streptococcus oligofermentas encodes for a 43 kDa flavoprotein (SoAAO), which was reported to possess a low catalytic activity versus several different L-amino acids: accordingly, it was classified as an L-amino acid oxidase. Subsequently, SoAAO was demonstrated to oxidize aminoacetone (a prooxidant metabolite), with an activity about 25-folds higher than the activity displayed on L-lysine this yielding support to the assumption of aminoacetone as the preferred substrate. In this work we present a characterization of the SoAAO structure-function relationships. SoAAO is a FAD-containing enzyme that does not possess the classical properties of oxidase/dehydrogenase class of flavoproteins (i.e., no flavin semiquinone formation is observed during anaerobic photoreduction as well as no reaction with sulfite) and does not show a true L-amino acid oxidase activity. From a structural point of view, SoAAO belongs to a novel protein family composed of three domains: an alpha/beta domain corresponding to the FAD-binding domain, a beta-domain partially modulating accessibility to the coenzyme, and an additional alpha-domain. Analysis of the reaction products of SoAAO on aminoacetone showed 2,5-dimethylpyrazine as the main product: we propose that condensation of two aminoacetone molecules yields 3,6-dimethyl-2,5-dihydropyrazine that is subsequently oxidized to 2,5-dimethylpyrazine. The ability of SoAAO to bind two molecules of the substrate-analogue O-methylglycine ligand is held to facilitate the condensation reaction. A specialized role for SoAAO in the microbial defence mechanism related to aminoacetone catabolism through a mechanism yielding dimethylpyrazine derivatives instead of methylglyoxal can be proposed. | ||
| - | + | Aminoacetone oxidase from Streptococcus oligofermentas belongs to a new three-domain family of bacterial flavoproteins.,Molla G, Nardini M, Motta P, D'Arrigo P, Panzeri W, Pollegioni L Biochem J. 2014 Sep 30. PMID:25269103<ref>PMID:25269103</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Lactate 2-monooxygenase]] | ||
| + | [[Category: Arrigo, P D.]] | ||
| + | [[Category: Bolognesi, M.]] | ||
| + | [[Category: Molla, G.]] | ||
| + | [[Category: Motta, P.]] | ||
| + | [[Category: Nardini, M.]] | ||
| + | [[Category: Pollegioni, L.]] | ||
| + | [[Category: Flavoprotein]] | ||
| + | [[Category: Oxidoreductase]] | ||
Revision as of 10:37, 20 October 2014
L-Aminoacetone oxidase from Streptococcus oligofermentans belongs to a new 3-domain family of bacterial flavoproteins
| |||||||||||
