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methionyl aminopeptidase
methionyl aminopeptidase catalyzes the hydrolytic removal of N-terminal methionine residues
type I methionyl aminopeptidase
Methionine aminopeptidase is a cobalt-binding enzyme. Bacterial and organellar examples (type I) differ from eukaroytic and archaeal (type II) examples in lacking a region of approximately 60 amino acids between the 4th and 5th cobalt-binding ligands. This model describes type I. The role of this protein in general is to produce the mature form of cytosolic proteins by removing the N-terminal methionine.
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