Mannuronan C-5 Epimerases: Review of Activity Assays, Enzyme Characteristics, Structure, and Mechanism
نویسندگان
چکیده
Mannuronan C-5 epimerases (ManC5-Es) are produced by brown algae and some bacteria, such as Azotobacter Pseudomonas species. It can convert the transformation of β-D-mannuronic acid (M) to α-L-guluronic (G) in alginate with different patterns epimerization. Alginate compositions monomer sequences possess properties functions, which have been utilized industries for various purposes. Therefore, ManC5-Es key enzymes that involved modifications fuel, chemical, industrial applications. Focusing on ManC5-Es, this review introduces summarizes methods activity assay especially most widely used nuclear magnetic resonance spectroscopy method, characterization from origins research progress its enzymatic product block distributions, catalytic mechanism ManC5-E based resolved enzyme structures. Additionally, potential future directions also outlooked.
منابع مشابه
Construction and analyses of hybrid Azotobacter vinelandii mannuronan C-5 epimerases with new epimerization pattern characteristics.
The secreted mannuronan C-5 epimerases from Azotobacter vinelandii form a family of seven homologous modular type enzymes, which appear to have evolved through duplications and point mutations in the individual modules. The catalytic A modules of these enzymes are responsible for generating the characteristic sequence distribution patterns of G residues in the industrially important polymer alg...
متن کاملMode of action and subsite studies of the guluronan block-forming mannuronan C-5 epimerases AlgE1 and AlgE6.
AlgE1, AlgE5 and AlgE6 are members of a family of mannuronan C-5 epimerases encoded by the bacterium Azotobacter vinelandii, and are active in the biosynthesis of alginate, where they catalyse the post-polymerization conversion of beta-D-mannuronic acid (M) residues into alpha-L-guluronic acid residues (G). All enzymes show preference for introducing G-residues neighbouring a pre-existing G. Th...
متن کاملBiochemical analysis of the processive mechanism for epimerization of alginate by mannuronan C-5 epimerase AlgE4.
The enzymes mannuronan C-5 epimerases catalyse the in-chain epimerisation of beta-D-mannuronic acid to alpha-L-guluronic acid in the last step of alginate biosynthesis. The recombinant C-5 epimerase AlgE4, encoded by the soil bacteria Azotobacter vinelandii and expressed in Escherichia coli, exhibits a non-random mode of action when acting on mannuronan and alginates of various monomeric compos...
متن کاملEnzyme Structure and Mechanism
This book explores the mechanisms of enzyme catalysis and specificity, from both the theoretical and experimental points of view. The emphasis is on kinetics and chemical thermodynamics as methods for establishing mechanisms at the atomic level for enzymes whose tertiary structure has already been solved by X-ray crystallography. Those with a good grasp of first-year organic chemistry, physical...
متن کاملCharacterization of mannuronan C-5-epimerase genes from the brown alga Laminaria digitata.
Alginate is an industrially important polysaccharide obtained commercially by harvesting brown algae. The final step in alginate biosynthesis, the epimerization of beta-1,4-d-mannuronic acid to alpha-1,4-l-guluronic acid, a structural change that controls the physicochemical properties of the alginate, is catalyzed by the enzyme mannuronan C-5-epimerase. Six different cDNAs with homology to bac...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Catalysts
سال: 2022
ISSN: ['2073-4344']
DOI: https://doi.org/10.3390/catal13010028