Fusion of dioxygenase and lignin-binding domains in a novel secreted enzyme from cellulolytic streptomyces sp. SIRexaa-e

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Abstract

Background: Fusions of dioxygenase and CBMs have been predicted in cellulolytic microbes. Results: SACTE-2871 is unique two-domain enzyme that reacts with caffeoyl-CoA and shows preferential binding to synthetic lignins. Conclusion: SACTE-2871 is an intradiol dioxygenase that is targeted to growing surfaces of lignin. Significance: SACTE-2871 can destroy precursors needed by the plant for de novo lignin biosynthesis as part of its natural wounding response. © 2013 by The American Society.

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CITATION STYLE

APA

Bianchetti, C. M., Harmann, C. H., Takasuka, T. E., Hura, G. L., Dyer, K., & Fox, B. G. (2013). Fusion of dioxygenase and lignin-binding domains in a novel secreted enzyme from cellulolytic streptomyces sp. SIRexaa-e. Journal of Biological Chemistry, 288(25), 18574–18587. https://doi.org/10.1074/jbc.M113.475848

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