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Literature summary for 3.4.11.18 extracted from

  • Larrabee, J.A.; Thamrong-Nawasawat, T.; Yee Mon, S.
    High-pressure liquid chromatographic method for the assay of methionine aminopeptidase activity: application to the study of enzymic inactivation (1999), Anal. Biochem., 269, 194-198.
    View publication on PubMed
Search for more literature for 3.4.11.18

Inhibitors

Inhibitors Comment Organism Structure
DTNB the enzyme is fully reactivated when incubated with tris(2-carboxyethyl)-phosphine hydrochloride Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Co2+ optimal concentration is 1 mM Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
Met-peptide + H2O Escherichia coli the enzyme removes the N-terminal Met from polypeptides, and thus plays a key role in protein synthesis, modification and transport Met + peptide
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Met-Gly-Met-Met + H2O
-
 Escherichia coli Gly-Met-Met + Met
-
 ?
Met-peptide + H2O the enzyme removes the N-terminal Met from polypeptides, and thus plays a key role in protein synthesis, modification and transport Escherichia coli Met + peptide
-
 ?

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
100
-
 2 min, complete loss of activity Escherichia coli