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4cnk

From Proteopedia

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L-Aminoacetone oxidase from Streptococcus oligofermentans belongs to a new 3-domain family of bacterial flavoproteins

Structural highlights

4cnk is a 2 chain structure with sequence from Streptococcus cristatus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2Å
Ligands:	, , ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

B1PUC6_STRCR

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Molla G, Nardini M, Motta P, D'Arrigo P, Panzeri W, Pollegioni L. Aminoacetone oxidase from Streptococcus oligofermentas belongs to a new three-domain family of bacterial flavoproteins. Biochem J. 2014 Sep 30. PMID:25269103 doi:http://dx.doi.org/10.1042/BJ20140972

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4cnk"

@@ Line 4: / Line 4: @@
 == Structural highlights ==
 <table><tr><td colspan='2'>[[4cnk]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_cristatus Streptococcus cristatus]. 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 [https://proteopedia.org/fgij/fg.htm?mol=4CNK FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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>
+</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&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4cnk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cnk OCA], [https://pdbe.org/4cnk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4cnk RCSB], [https://www.ebi.ac.uk/pdbsum/4cnk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4cnk ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/B1PUC6_STRCR B1PUC6_STRCR]]
+[https://www.uniprot.org/uniprot/B1PUC6_STRCR B1PUC6_STRCR]
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==

4cnk

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Current revision

L-Aminoacetone oxidase from Streptococcus oligofermentans belongs to a new 3-domain family of bacterial flavoproteins

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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