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Literature summary for 3.4.11.18 extracted from

  • D'Souza, V.M.; Holz, R.C.
    The Methionyl aminopeptidase from Escherichia coli can function as an iron(II) enzyme (1999), Biochemistry, 38, 11079-11085.
    View publication on PubMed

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.95
-
Met-Gly-Met-Met pH 7.5, 30°C, Fe(II)-substituted enzyme Escherichia coli
3.16
-
Met-Gly-Met-Met pH 7.5, 30°C, Co(II)-substituted enzyme Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ in vivo metal ions are likely Fe(II) ions Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
29633
-
x * 29633, apoenzyme, MALDI-TOF Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Escherichia coli

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
? x * 29633, apoenzyme, MALDI-TOF Escherichia coli