Methionine aminopeptidase 2, a member of the dimetallohydrolase family, is a cytosolic metalloenzyme that catalyzes the hydrolytic removal of N-terminal methionine residues from nascent proteins.
32.
The protein encoded by this gene is an aminopeptidase involved in trimming HLA class I-binding precursors so that they can be presented on MHC class I molecules.
33.
Leucine aminopeptidase, ( left ) a little like carboxypeptidase A, chops off certain amino acids one-by-one from one end of a protein or peptide.
34.
Several proteins within the pathway require either Ca 2 + ions, Mn 2 + ions, or divalent ions to function as aminopeptidase P, Proprotein convertases and sulfotransferases.
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Deficiency of X-prolyl aminopeptidase results in excretion of large amounts of imino-oligopeptides in urine ( Blau et al ., 1988 ) . [ supplied by OMIM]
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These proteins include methionine aminopeptidase 2, an enzyme that occurs in humans and other mammals that does not use the corrin ring of B 12, but binds cobalt directly.
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They are leucine aminopeptidase positive, pyrrolidonylarylamidase negative, and do not grow in 6.5 % NaCl, and almost all species are negative for growth on bile esculin agar.
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Angiotensin-converting enzyme ACE, aminopetidase A and aminopeptidase N have cascading actions in the renin-angiotensin-aldosterone system, which suggests a common phylogenetic origin between these molecules.
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The sequence of smARF, however, predicts that the initiating methionine would not be cleaved by methionine aminopeptidase and would probably be acetylated, and so is degraded by the proteasome without ubiquination.
40.
ERAP2 is an aminopeptidase that, together with the closely related ERAP1, trims peptides in the endoplasmic reticulum and loads these peptides on HLA molecules for presentation to T cells of the immune system.
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