4uwm

Type II Baeyer-Villiger monooxygenase.The oxygenating constituent of 3,6-diketocamphane monooxygenase from CAM plasmid of Pseudomonas putida in complex with FMN.Type II Baeyer-Villiger monooxygenase.The oxygenating constituent of 3,6-diketocamphane monooxygenase from CAM plasmid of Pseudomonas putida in complex with FMN.

Structural highlights

4uwm is a 2 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, , ,
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[C16MO_PSEPU] Involved in the degradation of (-)-camphor. Catalyzes the lactonization of the 3,6-diketocamphane via the Baeyer-Villiger oxidation to produce the unstable lactone (-)-5-oxo-1,2-campholide that presumably undergoes spontaneous hydrolysis to form 2-oxo-delta(3)-4,5,5-trimethylcyclopentenylacetic acid. It acts only on bicyclic ketones.^[1] ^[2]

Publication Abstract from PubMed

The oxygenating constituent of the 3,6-diketocamphane monooxygenase isozyme from Pseudomonas putida NCIMB 10007 has been crystallized under two different conditions. Crystals were initially grown from polyethylene glycol (PEG) 8000 and sodium acetate using the vapour-phase diffusion method. The crystals were of orthorhombic P212121 space group, with cell dimensions a = 55.8, b = 94.5 and c = 163.7 A and diffracted to 2.8 A resolution. More recently, improved crystals, which diffracted beyond 2 A, have been grown from ammonium sulfate. These crystals also belong to the orthorhombic P212121 space group, with cell dimensions of a = 54.6, b = 93.2 and c = 154. 1 A. A full native data set to 2.5 A resolution has been collected from the ammonium sulfate grown crystals.

Crystallization and preliminary X-ray diffraction studies of the oxygenating subunit of 3,6-diketocamphane monooxygenase from Pseudomonas putida.,McGhie EJ, Isupov MN, Schroder E, Littlechild JA Acta Crystallogr D Biol Crystallogr. 1998 Sep 1;54(Pt 5):1035-8. PMID:9757131^[3]

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

References

↑ Kadow M, Loschinski K, Sass S, Schmidt M, Bornscheuer UT. Completing the series of BVMOs involved in camphor metabolism of Pseudomonas putida NCIMB 10007 by identification of the two missing genes, their functional expression in E. coli, and biochemical characterization. Appl Microbiol Biotechnol. 2012 Oct;96(2):419-29. PMID:22286514 doi:http://dx.doi.org/10.1007/s00253-011-3859-1
↑ Jones KH, Smith RT, Trudgill PW. Diketocamphane enantiomer-specific 'Baeyer-Villiger' monooxygenases from camphor-grown Pseudomonas putida ATCC 17453. J Gen Microbiol. 1993 Apr;139(4):797-805. PMID:8515237
↑ McGhie EJ, Isupov MN, Schroder E, Littlechild JA. Crystallization and preliminary X-ray diffraction studies of the oxygenating subunit of 3,6-diketocamphane monooxygenase from Pseudomonas putida. Acta Crystallogr D Biol Crystallogr. 1998 Sep 1;54(Pt 5):1035-8. PMID:9757131

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OCA

[1] Kadow M, Loschinski K, Sass S, Schmidt M, Bornscheuer UT. Completing the series of BVMOs involved in camphor metabolism of Pseudomonas putida NCIMB 10007 by identification of the two missing genes, their functional expression in E. coli, and biochemical characterization. Appl Microbiol Biotechnol. 2012 Oct;96(2):419-29. PMID:22286514 doi:http://dx.doi.org/10.1007/s00253-011-3859-1

[2] Jones KH, Smith RT, Trudgill PW. Diketocamphane enantiomer-specific 'Baeyer-Villiger' monooxygenases from camphor-grown Pseudomonas putida ATCC 17453. J Gen Microbiol. 1993 Apr;139(4):797-805. PMID:8515237

[3] McGhie EJ, Isupov MN, Schroder E, Littlechild JA. Crystallization and preliminary X-ray diffraction studies of the oxygenating subunit of 3,6-diketocamphane monooxygenase from Pseudomonas putida. Acta Crystallogr D Biol Crystallogr. 1998 Sep 1;54(Pt 5):1035-8. PMID:9757131

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