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Function of your protein

AlyC3 is an present in Psychromonas sp. C-3 that plays a role in β-elimination at the glycosidic 1,4-O-linkage in alginate. AlyC3 uses tetramannuronate or polymannuronate as its substrate and converts the polymer into its substituent monomers, shorter PM chains, and 4-deoxy-L-erythro-hex-4-enopyranosyluronic acid. This facilitates alginate degradation and recycling in marine ecosystems.

Biological relevance and broader implications

Alginate lyases are made by bacteria, viruses, fungi, marine algae, and marine molusks. The protein PL7 alginate lyase AlyC3 plays roles in the degradation and recycling of alginate in ocean ecosystems. Alginate lyases have a variety of potential applications in the food, agriculture, and pharmaceutical industries. They may even be used to treat chronic lung infections by Pseudomonas aeruginosa. Exolytic and endolytic alginate lyases working in conjunction also have the potential to produce biofuels by breaking down alginate-rich algal cell walls into its substituent monosaccharides.

Important amino acids

The residues His127, and Tyr244 are important for the catalytic function of AlyC3 as mutating either or both amino acids to an alanine resulted in an almost inactive enzyme. It is believed that Arg82 and Tyr190 at the two ends of the catalytic canyon are the most important residues for binding and positioning the alginate substrate in AlyC3’s active site. The shown is dimannuronate complexed with a malonate ion. This fits in the groove of a β sheet on the enzyme where H127 deprotonates the substrate and Y244 is deprotonated by the oxygen in the 1,4-O-linkage between monomers degrading the substrate.

Structural highlights

AlyC3 has two domains with Cyclic – C2 symmetry. Its secondary structure is approximately 14% helices and 44% beta strands. Both domains each consist of 7 helices and 15 strands with one disulfide bridge. The most for binding substrate as well as those involved in catalysis all lie on beta strands in both domains.

Other important features

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