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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.

Biological relevance and broader implications

The protein PL7 alginate lyase AlyC3 plays roles in the degradation of alginate in the ocean

Important amino acids

he 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.

Structural highlights

Alginate lyase 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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