1H, 13C and 15N resonances of the AlgE62 subunit from Azotobacter vinelandii mannuronan C5-epimerase

Andreassen, Trygve; Buchinger, Edith; Skjåk‐Bræk, Gudmund; Valla, Svein; Aachmann, Finn Lillelund

doi:10.1007/s12104-010-9288-8

Cited by 3 publications

(2 citation statements)

References 11 publications

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“…The cell pellet was stored at Ϫ20°C if purification was not performed immediately. Expression of AlgE6R1, AlgE6R2, and AlgE6R3 for structure determination was described recently (23)(24)(25). AlgE4 was expressed as uniformly deuterated and 15 N-labeled proteins.…”

Section: Methodsmentioning

confidence: 99%

“…Cells containing the plasmid pFA8, pFA12, or pFA13 were grown in M9 medium containing 15 N-and 13 C-labeled nitrogen and carbon sources as described recently (23)(24)(25) Structural Calculations-NOE cross-peaks were assigned and integrated manually using the program NEASY (26). The structural calculations were performed by the program CYANA (27).…”

Section: Methodsmentioning

confidence: 99%

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Structural and Functional Characterization of the R-modules in Alginate C-5 Epimerases AlgE4 and AlgE6 from Azotobacter vinelandii

Buchinger

Knudsen

Behrens

et al. 2014

Journal of Biological Chemistry

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Background: Alginate epimerases consist of catalytic and noncatalytic domains of yet unknown function. Results: The noncatalytic domains of AlgE4 and AlgE6 possess different alginate binding behavior despite highly similar structures. Conclusion: Noncatalytic subunits of AlgE6 and AlgE4 influence the product specificity of the catalytic domain. Significance: This work opens a new route to designing alginate epimerases producing tailored alginates.

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Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Structural and Functional Characterization of the R-modules in Alginate C-5 Epimerases AlgE4 and AlgE6 from Azotobacter vinelandii

Buchinger

Knudsen

Behrens

et al. 2014

Journal of Biological Chemistry

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Properties and potential applications of mannuronan C5-epimerase: A biotechnological tool for modifying alginate

Jiang

Zhang

et al. 2021

International Journal of Biological Macromolecules

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Mannuronan C-5 Epimerases: Review of Activity Assays, Enzyme Characteristics, Structure, and Mechanism

Xiao

Sun

et al. 2022

Catalysts

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Mannuronan C-5 epimerases (ManC5-Es) are produced by brown algae and some bacteria, such as Azotobacter and some Pseudomonas species. It can convert the transformation of β-D-mannuronic acid (M) to α-L-guluronic acid (G) in alginate with different patterns of epimerization. Alginate with different compositions and monomer sequences possess different properties and functions, which have been utilized in industries for various purposes. Therefore, ManC5-Es are key enzymes that are involved in the modifications of alginate for fuel, chemical, and industrial applications. Focusing on ManC5-Es, this review introduces and summarizes the methods of ManC5-Es activity assay especially the most widely used nuclear magnetic resonance spectroscopy method, characterization of the ManC5-Es from different origins especially the research progress of its enzymatic properties and product block distributions, and the catalytic mechanism of ManC5-E based on the resolved enzyme structures. Additionally, some potential future research directions are also outlooked.

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1H, 13C and 15N resonances of the AlgE62 subunit from Azotobacter vinelandii mannuronan C5-epimerase

Abstract: The 17.7 kDa R2 module from Azotobacter vinelandii mannronan C5-epimerase AlgE6 has been isotopically labeled ( 13 C, 15 N) and recombinantly expressed. Here we report the 1 H, 13 C, 15 N resonance assignment of AlgE6R2.

Cited by 3 publications

References 11 publications

Structural and Functional Characterization of the R-modules in Alginate C-5 Epimerases AlgE4 and AlgE6 from Azotobacter vinelandii

Structural and Functional Characterization of the R-modules in Alginate C-5 Epimerases AlgE4 and AlgE6 from Azotobacter vinelandii

Properties and potential applications of mannuronan C5-epimerase: A biotechnological tool for modifying alginate

Mannuronan C-5 Epimerases: Review of Activity Assays, Enzyme Characteristics, Structure, and Mechanism

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