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Literature summary for 3.4.11.18 extracted from

  • Copik, A.J.; Nocek, B.P.; Swierczek, S.I.; Ruebush, S.; Jang, S.B.; Meng, L.; D'Souza V.M.; Peters, J.W.; Bennett, B.; Holz, R.C.
    EPR and X-ray crystallographic characterization of the product-bound form of the MnII-loaded methionyl aminopeptidase from Pyrococcus furiosus (2005), Biochemistry, 44, 121-129.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
in presence of L-methionine Pyrococcus furiosus

Inhibitors

Inhibitors Comment Organism Structure
L-methionine weak, competitive Pyrococcus furiosus

Metals/Ions

Metals/Ions Comment Organism Structure
Mn2+ enzyme contains 2 Mn-ions residing in a distorted trigonal bipyramidal geometry. A bridging water molecule is displaced by L-methionine Pyrococcus furiosus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
33000
-
x * 33000, SDS-PAGE Pyrococcus furiosus

Organism

Organism UniProt Comment Textmining
Pyrococcus furiosus P56218 isoform MetAP-II
-

Subunits

Subunits Comment Organism
? x * 33000, SDS-PAGE Pyrococcus furiosus

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
150
-
L-methionine pH 7.5 Pyrococcus furiosus