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Characterization and solution structure of mouse myristoylated methionine sulfoxide reductase A.


ABSTRACT: Methionine sulfoxide reductase A is an essential enzyme in the antioxidant system which scavenges reactive oxygen species through cyclic oxidation and reduction of methionine and methionine sulfoxide. The cytosolic form of the enzyme is myristoylated, but it is not known to translocate to membranes, and the function of myristoylation is not established. We compared the biochemical and biophysical properties of myristoylated and nonmyristoylated mouse methionine sulfoxide reductase A. These were almost identical for both forms of the enzyme, except that the myristoylated form reduced methionine sulfoxide in protein much faster than the nonmyristoylated form. We determined the solution structure of the myristoylated protein and found that the myristoyl group lies in a relatively surface exposed "myristoyl nest." We propose that this structure functions to enhance protein-protein interaction.

SUBMITTER: Lim JC 

PROVIDER: S-EPMC3408158 | biostudies-literature | 2012 Jul

REPOSITORIES: biostudies-literature

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Characterization and solution structure of mouse myristoylated methionine sulfoxide reductase A.

Lim Jung Chae JC   Gruschus James M JM   Ghesquière Bart B   Kim Geumsoo G   Piszczek Grzegorz G   Tjandra Nico N   Levine Rodney L RL  

The Journal of biological chemistry 20120601 30


Methionine sulfoxide reductase A is an essential enzyme in the antioxidant system which scavenges reactive oxygen species through cyclic oxidation and reduction of methionine and methionine sulfoxide. The cytosolic form of the enzyme is myristoylated, but it is not known to translocate to membranes, and the function of myristoylation is not established. We compared the biochemical and biophysical properties of myristoylated and nonmyristoylated mouse methionine sulfoxide reductase A. These were  ...[more]

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