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Literature summary for 3.4.11.18 extracted from

  • Addlagatta, A.; Hu, X.; Liu, J.O.; Matthews, B.W.
    Structural basis for the functional differences between type I and type II human methionine aminopeptidases (2005), Biochemistry, 44, 14741-14749.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
truncated MetAP1 lacking N-terminal 89 amino acids Homo sapiens

Protein Variants

Protein Variants Comment Organism
additional information truncated MetAP1 lacking N-terminal 89 amino acids, 2.5fold increase in KM-value Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
Co2+ in excess, a third Co2+ ion binds to the active site regions and results in inhibition Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.74
-
L-Met-L-Pro-4-nitroanilide wild-type, pH 7.5, 22°C Homo sapiens
1.8
-
L-Met-L-Pro-4-nitroanilide truncated mutant lacking N-terminal 89 amino acids, pH 7.5, 22°C Homo sapiens

Metals/Ions

Metals/Ions Comment Organism Structure
Co2+
-
Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
MetAP1 isoform
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-Met-L-Pro-4-nitroanilide + H2O
-
Homo sapiens L-Met + L-Pro-4-nitroanilide
-
?

Subunits

Subunits Comment Organism
More N-terminal region contains 3 distinct PxxP motifs that may participate in binding to the ribosome Homo sapiens

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.11
-
L-Met-L-Pro-4-nitroanilide wild-type, pH 7.5, 22°C Homo sapiens
0.425
-
L-Met-L-Pro-4-nitroanilide truncated mutant lacking N-terminal 89 amino acids, pH 7.5, 22°C Homo sapiens