Literature summary 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.

Crystallization (Commentary)

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

Inhibitors

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

Metals/Ions

EC Number	Metals/Ions	Comment	Organism	Structure
3.4.11.18	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]

EC Number	Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
3.4.11.18	33000	-	x * 33000, SDS-PAGE	Pyrococcus furiosus

Organism

EC Number	Organism	UniProt	Comment	Textmining
3.4.11.18	Pyrococcus furiosus	P56218	isoform MetAP-II	-

Subunits

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

Ki Value [mM]

EC Number	Ki Value [mM]	Ki Value maximum [mM]	Inhibitor	Comment	Organism	Structure
3.4.11.18	150	-	L-methionine	pH 7.5	Pyrococcus furiosus

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Release 2023.1 (January 2023)