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3gsy

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Revision as of 22:02, 24 December 2014

Structure of berberine bridge enzyme in complex with dehydroscoulerine

Structural highlights

3gsy is a 1 chain structure with sequence from Eschscholzia californica. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, , , ,
Related:	3d2d, 3d2h, 3d2j, 3fw9, 3fw7, 3fw8
Gene:	BBE1 (Eschscholzia californica)
Activity:	Reticuline oxidase, with EC number 1.21.3.3
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[RETO_ESCCA] Essential to the formation of benzophenanthridine alkaloids in the response of plants to pathogenic attack. Catalyzes the stereospecific conversion of the N-methyl moiety of (S)-reticuline into the berberine bridge carbon of (S)-scoulerine.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Berberine bridge enzyme catalyzes the stereospecific oxidation and carbon-carbon bond formation of (S)-reticuline to (S)-scoulerine. In addition to this type of reactivity the enzyme can further oxidize (S)-scoulerine to the deeply red protoberberine alkaloid dehydroscoulerine albeit with a much lower rate of conversion. In the course of the four electron oxidation, no dihydroprotoberberine species intermediate was detectable suggesting that the second oxidation step leading to aromatization proceeds at a much faster rate. Performing the reaction in the presence of oxygen and under anoxic conditions did not affect the kinetics of the overall reaction suggesting no strict requirement for oxygen in the oxidation of the unstable dihydroprotoberberine intermediate. In addition to the kinetic characterization of this reaction we also present a structure of the enzyme in complex with the fully oxidized product. Combined with information available for the binding modes of (S)-reticuline and (S)-scoulerine a possible mechanism for the additional oxidation is presented. This is compared to previous reports of enzymes ((S)-tetrahydroprotoberberine oxidase and canadine oxidase) showing a similar type of reactivity in different plant species.

Berberine bridge enzyme catalyzes the six electron oxidation of (S)-reticuline to dehydroscoulerine.,Winkler A, Puhl M, Weber H, Kutchan TM, Gruber K, Macheroux P Phytochemistry. 2009 Jun;70(9):1092-7. Epub 2009 Jun 29. PMID:19570558^[1]

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

References

↑ Winkler A, Puhl M, Weber H, Kutchan TM, Gruber K, Macheroux P. Berberine bridge enzyme catalyzes the six electron oxidation of (S)-reticuline to dehydroscoulerine. Phytochemistry. 2009 Jun;70(9):1092-7. Epub 2009 Jun 29. PMID:19570558 doi:10.1016/j.phytochem.2009.06.005

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3gsy"

@@ Line 9: / Line 9: @@
 <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=3gsy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3gsy OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3gsy RCSB], [http://www.ebi.ac.uk/pdbsum/3gsy PDBsum]</span></td></tr>
 </table>
+== Function ==
+[[http://www.uniprot.org/uniprot/RETO_ESCCA RETO_ESCCA]] Essential to the formation of benzophenanthridine alkaloids in the response of plants to pathogenic attack. Catalyzes the stereospecific conversion of the N-methyl moiety of (S)-reticuline into the berberine bridge carbon of (S)-scoulerine.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

3gsy

From Proteopedia

Revision as of 22:02, 24 December 2014

Structure of berberine bridge enzyme in complex with dehydroscoulerine

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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