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Resolving Confusion Surrounding d‐Ala‐d‐Ala Ligase Catalysis in Cyanobacterial Mycosporine‐Like Amino Acid (MAA) Biosynthesis

Von Wiley-VCH zur Verfügung gestellt

What's in a name? Cyanobacteria can introduce structural diversity into MAAs by using a mysD ligase with relaxed specify to modify mycosporine-glycine. The naming of mysD, based solely upon sequence similarity to the d-Ala-d-Ala ligase of bacterial peptidoglycan biosynthesis, has been confusing. Combining phylogeny and α-fold tertiary protein structure prediction unambiguously distinguished mysD from d-Ala-d-Ala ligase, and the generic name mycosporine-glycine-amine ligase (MG-amine ligase) is proposed.


Mycosporine-like amino acids (MAAs) are natural UV-absorbing sunscreens that evolved in cyanobacteria and algae to palliate harmful effects from obligatory exposure to solar radiation. Multiple lines of evidence prove that in cyanobacteria all MAAs are derived from mycosporine-glycine, which is typically modified by an ATP-dependent ligase encoded by the gene mysD. The function of the mysD ligase has been experimentally described but haphazardly named based solely upon sequence similarity to the d-alanine-d-alanine ligase of bacterial peptidoglycan biosynthesis. Combining phylogeny and alpha-fold tertiary protein structure prediction unambiguously distinguished mysD from d-alanine-d-alanine ligase. The renaming of mysD to mycosporine-glycine-amine ligase (MG-amine ligase) using recognised enzymology rules of nomenclature is, therefore, proposed, and considers relaxed specificity for several different amino acid substrates. The evolutionary and ecological context of MG-amine ligase catalysis merits wider appreciation especially when considering exploiting cyanobacteria for biotechnology, for example, producing mixtures of MAAs with enhanced optical or antioxidant properties.

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