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Literature summary 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

Inhibitors

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

Metals/Ions

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

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.4.11.18 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
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?

Organism

EC Number Organism UniProt Comment Textmining
3.4.11.18 Escherichia coli
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.11.18 Met-Gly-Met-Met + H2O
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Escherichia coli Gly-Met-Met + Met
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?
3.4.11.18 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]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.4.11.18 100
-
2 min, complete loss of activity Escherichia coli