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Literature summary 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

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.11.18 2-mercaptoethanol
-
Sus scrofa
3.4.11.18 EDTA
-
Sus scrofa

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.4.11.18 0.222
-
Met-Val-His-Thr-Leu-Pro-Glu-Glu-Leu
-
Sus scrofa
3.4.11.18 0.28
-
Met-Pro-His-Thr-Leu-Pro-Glu-Glu
-
Sus scrofa
3.4.11.18 0.625
-
Met-Ala-His-Thr-Leu-Pro-Glu-Glu-Leu
-
Sus scrofa

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.4.11.18 Co2+ stimulates Sus scrofa

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.4.11.18 66000
-
gel filtration Sus scrofa
3.4.11.18 70000
-
1 * 70000, SDS-PAGE Sus scrofa

Organism

EC Number Organism UniProt Comment Textmining
3.4.11.18 Sus scrofa
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.4.11.18
-
Sus scrofa

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.4.11.18 liver
-
Sus scrofa
-

Specific Activity [micromol/min/mg]

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

Substrates and Products (Substrate)

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

Subunits

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

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.4.11.18 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
3.4.11.18 6 8 reaction with Met-Ala-Ser-(Gly)5-(Leu)3 Sus scrofa