addenda and errata\(\def\hfill{\hskip 5em}\def\hfil{\hskip 3em}\def\eqno#1{\hfil {#1}}\)

Journal logoSTRUCTURAL
BIOLOGY
ISSN: 2059-7983

The oxygenating constituent of 3,6-diketocamphane monooxygenase from the CAM plasmid of Pseudomonas putida: the first crystal structure of a type II Baeyer–Villiger monooxygenase. Corrigendum

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aThe Henry Wellcome Building for Biocatalysis, Biosciences, College of Life and Environmental Sciences, University of Exeter, Stocker Road, Exeter EX4 4QD, England, bBiotechnology Research Institute, National Research Council Canada, 6100 Royalmount Avenue, Montreal, QC H4P 2R2, Canada, cDepartment of Biotechnology, Faculty of Engineering, Kansai University, Japan, dDepartment of Biotechnology and Enzyme Catalysis, Institute of Biochemistry, Greifswald University, Felix-Hausdorff-Strasse 4, 17487 Greifswald, Germany, and eEuropean Molecular Biology Laboratory (EMBL), Hamburg Outstation, Notkestrasse 85, 22607 Hamburg, Germany
*Correspondence e-mail: j.a.littlechild@exeter.ac.uk

A statement is amended in the article by Isupov et al. [(2015[Isupov, M. N., Schröder, E., Gibson, R. P., Beecher, J., Donadio, G., Saneei, V., Dcunha, S. A., McGhie, E. J., Sayer, C., Davenport, C. F., Lau, P. C., Hasegawa, Y., Iwaki, H., Kadow, M., Balke, K., Bornscheuer, U. T., Bourenkov, G. & Littlechild, J. A. (2015). Acta Cryst. D71, 2344-2353.]). Acta Cryst. D71, 2344–2353].

In the article by Isupov et al. (2015[Isupov, M. N., Schröder, E., Gibson, R. P., Beecher, J., Donadio, G., Saneei, V., Dcunha, S. A., McGhie, E. J., Sayer, C., Davenport, C. F., Lau, P. C., Hasegawa, Y., Iwaki, H., Kadow, M., Balke, K., Bornscheuer, U. T., Bourenkov, G. & Littlechild, J. A. (2015). Acta Cryst. D71, 2344-2353.]), the statement in §3.10 `Partial sequencing of the large CAM plasmid has now identified a flavin reductase adjacent to the 3,6-DKMO gene on the CAM plasmid (Littlechild & Isupov, unpublished data)' is withdrawn. The following statement is added: `A cognate flavin reductase (Fred) from the genome of Pseudomonas putida (strain PpCam), which provides the required FMNH2 for the 3,6-DKMO activity, has been described by Iwaki et al. (2013[Iwaki, H., Grosse, S., Bergeron, H., Leisch, H., Morley, K., Hasegawa, Y. & Lau, P. C. K. (2013). Appl. Environ. Microbiol. 79, 3282-3293.]). Other non-cognate reductases have been reported which can partially support the DKMO activity but not as efficiently as the cognate Fred'.

References

First citationIsupov, M. N., Schröder, E., Gibson, R. P., Beecher, J., Donadio, G., Saneei, V., Dcunha, S. A., McGhie, E. J., Sayer, C., Davenport, C. F., Lau, P. C., Hasegawa, Y., Iwaki, H., Kadow, M., Balke, K., Bornscheuer, U. T., Bourenkov, G. & Littlechild, J. A. (2015). Acta Cryst. D71, 2344–2353.  CrossRef IUCr Journals Google Scholar
First citationIwaki, H., Grosse, S., Bergeron, H., Leisch, H., Morley, K., Hasegawa, Y. & Lau, P. C. K. (2013). Appl. Environ. Microbiol. 79, 3282–3293.  CrossRef CAS Google Scholar

© International Union of Crystallography. Prior permission is not required to reproduce short quotations, tables and figures from this article, provided the original authors and source are cited. For more information, click here.

Journal logoSTRUCTURAL
BIOLOGY
ISSN: 2059-7983
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