TY - JOUR
T1 - Metabolism of Aldoximes and Nitriles in Plant-Associated Bacteria and Its Potential in Plant–Bacteria Interactions
AU - Rädisch, Robert
AU - Pátek, Miroslav
AU - Křístková, Barbora
AU - Winkler, Margit
AU - Křen, Vladimír
AU - Martínková, Ludmila
N1 - Funding Information:
Funding: This work was funded by the Czech Science Foundation, grant number GF20-23532L, the Charles University Grant Agency, grant number 452120, and by the Austrian Science Fund FWF, grant number I 4607.
Funding Information:
This work was funded by the Czech Science Foundation, grant number GF20-23532L, the Charles University Grant Agency, grant number 452120, and by the Austrian Science Fund FWF, grant number I 4607. Acknowledgments: The authors wish to acknowledge the administrative and technical support by Petr Novotn? (Institute of Microbiology of the Czech Academy of Sciences).
Publisher Copyright:
© 2022 by the authors. Licensee MDPI, Basel, Switzerland.
PY - 2022/3
Y1 - 2022/3
N2 - In plants, aldoximes per se act as defense compounds and are precursors of complex defense compounds such as cyanogenic glucosides and glucosinolates. Bacteria rarely produce aldoximes, but some are able to transform them by aldoxime dehydratase (Oxd), followed by nitrilase (NLase) or nitrile hydratase (NHase) catalyzed transformations. Oxds are often encoded together with NLases or NHases in a single operon, forming the aldoxime–nitrile pathway. Previous reviews have largely focused on the use of Oxds and NLases or NHases in organic synthesis. In contrast, the focus of this review is on the contribution of these enzymes to plant-bacteria interactions. Therefore, we summarize the substrate specificities of the enzymes for plant compounds. We also analyze the taxonomic and ecological distribution of the enzymes. In addition, we discuss their importance in selected plant symbionts. The data show that Oxds, NLases, and NHases are abundant in Actinobacteria and Proteobacteria. The enzymes seem to be important for breaking through plant defenses and utilizing oximes or nitriles as nutrients. They may also contribute, e.g., to the synthesis of the phytohormone indole-3-acetic acid. We conclude that the bacterial and plant metabolism of aldoximes and nitriles may interfere in several ways. However, further in vitro and in vivo studies are needed to better understand this underexplored aspect of plant–bacteria interactions.
AB - In plants, aldoximes per se act as defense compounds and are precursors of complex defense compounds such as cyanogenic glucosides and glucosinolates. Bacteria rarely produce aldoximes, but some are able to transform them by aldoxime dehydratase (Oxd), followed by nitrilase (NLase) or nitrile hydratase (NHase) catalyzed transformations. Oxds are often encoded together with NLases or NHases in a single operon, forming the aldoxime–nitrile pathway. Previous reviews have largely focused on the use of Oxds and NLases or NHases in organic synthesis. In contrast, the focus of this review is on the contribution of these enzymes to plant-bacteria interactions. Therefore, we summarize the substrate specificities of the enzymes for plant compounds. We also analyze the taxonomic and ecological distribution of the enzymes. In addition, we discuss their importance in selected plant symbionts. The data show that Oxds, NLases, and NHases are abundant in Actinobacteria and Proteobacteria. The enzymes seem to be important for breaking through plant defenses and utilizing oximes or nitriles as nutrients. They may also contribute, e.g., to the synthesis of the phytohormone indole-3-acetic acid. We conclude that the bacterial and plant metabolism of aldoximes and nitriles may interfere in several ways. However, further in vitro and in vivo studies are needed to better understand this underexplored aspect of plant–bacteria interactions.
KW - Aldoxime dehydratase
KW - Aldoxime-nitrile pathway
KW - Indole-3-acetic acid
KW - Nitrilase
KW - Nitrile hydratase
KW - Phytohormone
KW - Plant aldoxime
KW - Plant defense
KW - Plant-bacteria interaction
UR - http://www.scopus.com/inward/record.url?scp=85126303384&partnerID=8YFLogxK
U2 - 10.3390/microorganisms10030549
DO - 10.3390/microorganisms10030549
M3 - Review article
AN - SCOPUS:85126303384
VL - 10
JO - Microorganisms
JF - Microorganisms
SN - 2076-2607
IS - 3
M1 - 549
ER -