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Meaghan Trimarchi Marks (@met77) • Instagram photos and videos

Unlike H 2 O 2 - or HOCl/OCI --induced CaM oxidation, which is capable of modifying each of the nine available methionine residues, MSR-A stereospecifically oxidizes only methionine (Met77) to MetO (Lim et al., 2013). The Met77 residues are located in the carboxyl part of the central linker.

The FASEB Journal

We verified that MaCaM1 interacts with MaMsrA7 in vitro and in vivo, and sulfoxidated MaCaM1 could be partly repaired by MaMsrA7 (MaMsrA7 reduces oxidized residues Met77 and Met110 in MaCaM1). Furthermore, we investigated two known CaM-binding proteins, catalase (MaCAT1) and MaHY5-1.

Drosophila Methionine sulfoxide reductase A is not a methionine oxidase ...

Thus, methionine sulfoxide reductase A can mediate the reversible covalent modification of Met77 in CaM. To assess whether this is a regulatory mechanism in vivo, we utilized CRISPR to mutate Met77 to Gln because Gln is a mimic of MetO.

Oxidation of Methionine 77 in Calmodulin Alters Mouse ... - Preprints

Oxidation and reduction of Met77 in calmodulin could function as an on-off switch by modulating interaction of the calmodulin with one or more specific targets. We used a human protein array to detect interactions of wild-type or M77Q calmodulin.

(PDF) Oxidation of Methionine 77 in Calmodulin Alters ... - ResearchGate

At that point, these authors concluded that the reversible covalent modification of Met76 (Met77 if we count the initiating methionine, which is absent in the mature form of the protein) may regulate the interaction of calmodulin with one or more of its many targets.