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Gene Review:

SCO7147 - ketoreductase

Streptomyces coelicolor A3(2)

McDaniel, R. et al., Hadfield, A.T. et al., Ichinose, K. et al.

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Disease relevance of SCO7147

Functional complementation of pyran ring formation in actinorhodin biosynthesis in Streptomyces coelicolor A3(2) by ketoreductase genes for granaticin biosynthesis [1].

High impact information on SCO7147

They are also consistent with earlier conclusions that the minimal PKS controls chain length as well as the regiospecificity of the first cyclization and that it can do so in the absence of both a ketoreductase and a cyclase [2].
We have determined the 2.5 angstroms crystal structure of an active, tetrameric Streptomyces coelicolor type II polyketide ketoreductase (actIII) with its bound cofactor, NADP+ [3].

References

Functional complementation of pyran ring formation in actinorhodin biosynthesis in Streptomyces coelicolor A3(2) by ketoreductase genes for granaticin biosynthesis. Ichinose, K., Taguchi, T., Bedford, D.J., Ebizuka, Y., Hopwood, D.A. J. Bacteriol. (2001) [Pubmed]
Engineered biosynthesis of novel polyketides: influence of a downstream enzyme on the catalytic specificity of a minimal aromatic polyketide synthase. McDaniel, R., Ebert-Khosla, S., Fu, H., Hopwood, D.A., Khosla, C. Proc. Natl. Acad. Sci. U.S.A. (1994) [Pubmed]
The crystal structure of the actIII actinorhodin polyketide reductase: proposed mechanism for ACP and polyketide binding. Hadfield, A.T., Limpkin, C., Teartasin, W., Simpson, T.J., Crosby, J., Crump, M.P. Structure (Camb.) (2004) [Pubmed]

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