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Literature summary for 3.4.11.18 extracted from

  • Kendall, R.L.; Bradshaw, R.A.
    Isolation and characterization of the methionine aminopeptidase from porcine liver responsible for the co-translational processing of proteins (1992), J. Biol. Chem., 267, 20667-20673.
    View publication on PubMed
Search for more literature for 3.4.11.18

Inhibitors

Inhibitors Comment Organism Structure
2-mercaptoethanol
-
 Sus scrofa
EDTA
-
 Sus scrofa

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.222
-
 Met-Val-His-Thr-Leu-Pro-Glu-Glu-Leu
-
 Sus scrofa
0.28
-
 Met-Pro-His-Thr-Leu-Pro-Glu-Glu
-
 Sus scrofa
0.625
-
 Met-Ala-His-Thr-Leu-Pro-Glu-Glu-Leu
-
 Sus scrofa

Metals/Ions

Metals/Ions Comment Organism Structure
Co2+ stimulates Sus scrofa

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
66000
-
 gel filtration Sus scrofa
70000
-
 1 * 70000, SDS-PAGE Sus scrofa

Organism

Organism UniProt Comment Textmining
Sus scrofa
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Sus scrofa

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
 Sus scrofa
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
 Sus scrofa

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Met-Ala-His-Thr-Leu-Pro-Glu-Glu-Leu + H2O
-
 Sus scrofa Met + Ala-His-Thr-Leu-Pro-Glu-Glu-Leu
-
 ?
Met-Ala-Ser-(Gly)5-(Leu)3 + H2O
-
 Sus scrofa Met + Ala-Ser-(Gly)5-(Leu)3
-
 ?
Met-Pro-His-Thr-Leu-Pro-Glu-Glu + H2O
-
 Sus scrofa Met + Pro-His-Thr-Leu-Pro-Glu-Glu
-
 ?
Met-Val-His-Thr-Leu-Pro-Glu-Glu-Leu + H2O
-
 Sus scrofa Met + Val-His-Thr-Leu-Pro-Glu-Glu-Leu
-
 ?
additional information specificity: the enzyme does not cleave amino-terminal methionine when it precedes residues of lysine Sus scrofa ?
-
 ?
additional information specificity: the enzyme cleaves amino-terminal methionine when it precedes residues of valine Sus scrofa ?
-
 ?
additional information specificity: the enzyme cleaves amino-terminal methionine when it precedes residues of proline Sus scrofa ?
-
 ?
additional information specificity: the enzyme does not cleave amino-terminal methionine when it precedes residues of leucine Sus scrofa ?
-
 ?
additional information specificity: the enzyme cleaves amino-terminal methionine when it precedes residues of serine Sus scrofa ?
-
 ?
additional information specificity: the enzyme cleaves amino-terminal methionine when it precedes residues of glycine Sus scrofa ?
-
 ?
additional information specificity: the enzyme cleaves amino-terminal methionine when it precedes residues of alanine Sus scrofa ?
-
 ?

Subunits

Subunits Comment Organism
monomer 1 * 70000, SDS-PAGE Sus scrofa

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6
-
 octapeptide substrate related to the amino-terminal portion of the beta-chain of human hemoglobin with either valine or alanine in the penultimate position Sus scrofa
6 8 reaction with Met-Ala-Ser-(Gly)5-(Leu)3 Sus scrofa