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EC Tree
The taxonomic range for the selected organisms is: Pyrococcus furiosus The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
map-2, metap2, metap, methionine aminopeptidase, metap-2, metap1, methionine aminopeptidase 2, methionine aminopeptidase-2, metap-1, methionyl aminopeptidase,
more
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methionine aminopeptidase
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aminopeptidase, methionine
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initiation factor 2 associated 67 kDa glycoprotein
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L-methionine aminopeptidase
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methionine aminopeptidase
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methionine aminopeptidase type II
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hydrolysis of peptide bond
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L-Met-Gly-L-Met-L-Met + H2O
L-Met + Gly-L-Met-L-Met
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?
L-Met-p-nitroanilide + H2O
p-nitroaniline + L-Met
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?
Met-Ala-Ser + H2O
Met + Ala-Ser
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?
Met-Gly-Met-Met + H2O
Gly-Met-Met + Met
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?
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Mn2+
enzyme contains 2 Mn-ions residing in a distorted trigonal bipyramidal geometry. A bridging water molecule is displaced by L-methionine
Co2+
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activity requires divalent cations like Co2+
Mn2+
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activity requires divalent cations like Mn2+
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L-methionine
weak, competitive
((2RS,3R)-3-amino-2-hydroxy-5-ethylthio)pentanoyl-((S)-(-)-(1-naphthyl)ethyl)amide
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A-311263, the inhibitor has little or no preference for the type of divalent metal ion that occupies the active site of MetAP
3-((2-naphthylmethyl)sulfanyl)-4H-1,2,4-triazole
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A-310840
butaneboronic acid
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substrate analog
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0.59
L-Met-p-nitroanilide
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in 25 mM HEPES buffer at 30°C (pH 7.5) with 150 mM KCl
5.1
Met-Gly-Met-Met
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in 25 mM HEPES buffer at 30°C (pH 7.5) with 150 mM KCl
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0.057
L-Met-p-nitroanilide
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in 25 mM HEPES buffer at 30°C (pH 7.5) with 150 mM KCl
188
Met-Gly-Met-Met
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in 25 mM HEPES buffer at 30°C (pH 7.5) with 150 mM KCl
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0.002 - 0.02
((2RS,3R)-3-amino-2-hydroxy-5-ethylthio)pentanoyl-((S)-(-)-(1-naphthyl)ethyl)amide
0.003 - 0.44
3-((2-naphthylmethyl)sulfanyl)-4H-1,2,4-triazole
0.002
((2RS,3R)-3-amino-2-hydroxy-5-ethylthio)pentanoyl-((S)-(-)-(1-naphthyl)ethyl)amide
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Co2+-loaded wild type enzyme, in 25 mM HEPES buffer, pH 7.5, containing 150 mM KCl, at 30°C
0.02
((2RS,3R)-3-amino-2-hydroxy-5-ethylthio)pentanoyl-((S)-(-)-(1-naphthyl)ethyl)amide
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Mn2+-loaded wild type enzyme, in 25 mM HEPES buffer, pH 7.5, containing 150 mM KCl, at 30°C
0.003
3-((2-naphthylmethyl)sulfanyl)-4H-1,2,4-triazole
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Co2+-loaded wild type enzyme, in 25 mM HEPES buffer, pH 7.5, containing 150 mM KCl, at 30°C
0.44
3-((2-naphthylmethyl)sulfanyl)-4H-1,2,4-triazole
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Mn2+-loaded wild type enzyme, in 25 mM HEPES buffer, pH 7.5, containing 150 mM KCl, at 30°C
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0.02 - 0.027
((2RS,3R)-3-amino-2-hydroxy-5-ethylthio)pentanoyl-((S)-(-)-(1-naphthyl)ethyl)amide
0.015 - 1
3-((2-naphthylmethyl)sulfanyl)-4H-1,2,4-triazole
0.0017
L-MetStaCys
Pyrococcus furiosus
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in 25 mM HEPES buffer at 30°C (pH 7.5)
0.002
L-MetStaVal
Pyrococcus furiosus
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in 25 mM HEPES buffer at 30°C (pH 7.5)
0.02
((2RS,3R)-3-amino-2-hydroxy-5-ethylthio)pentanoyl-((S)-(-)-(1-naphthyl)ethyl)amide
Pyrococcus furiosus
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Co2+-loaded wild type enzyme, in 25 mM HEPES buffer, pH 7.5, containing 150 mM KCl, at 30°C
0.027
((2RS,3R)-3-amino-2-hydroxy-5-ethylthio)pentanoyl-((S)-(-)-(1-naphthyl)ethyl)amide
Pyrococcus furiosus
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Mn2+-loaded wild type enzyme, in 25 mM HEPES buffer, pH 7.5, containing 150 mM KCl, at 30°C
0.015
3-((2-naphthylmethyl)sulfanyl)-4H-1,2,4-triazole
Pyrococcus furiosus
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Co2+-loaded wild type enzyme, in 25 mM HEPES buffer, pH 7.5, containing 150 mM KCl, at 30°C
1
3-((2-naphthylmethyl)sulfanyl)-4H-1,2,4-triazole
Pyrococcus furiosus
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Mn2+-loaded wild type enzyme, in 25 mM HEPES buffer, pH 7.5, containing 150 mM KCl, at 30°C
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Uniprot
brenda
isoform MetAP-II
Uniprot
brenda
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33000
x * 33000, SDS-PAGE
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in presence of L-methionine
sitting-drop variant of the vapor-diffusion method at room temperature, crystallization of monoclinic crystals and the transformation of original crystals to low-humidity form which is accompanied by a significant extension of resolution, in particular, from 3.2 to 1.75 A
electronic absorption spectrum in the absence and presence of both nitric oxide and the substrate-analog butaneboronic acid. Both bind to the catalytic Fe(II)-center of enzyme forming a complex that mimics an intermediate step between the Michaelis complex and the tetrahedral transition-state
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structure is determined by the multiple isomorphous replacement method and refined in three different crystal forms, one monoclinic and two hexagonal, at resolutions of 2.8, 2.9 and 3.5 A. Crystals are grown by the sitting-drop variant of the vapor-diffusion method
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synthesis
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recombinant human interferon alpha-2b is produced in Escherichia coli in two types of molecules, one type, in majority, having N-terminal methionine intact, whereas the other type, in minority, having the N-terminal methionine cleaved by methionine aminopeptidase of the host. The N-terminal methionine of the remaining molecules can be removed by utilizing methionine aminopeptidase from Pyrococcus furiosus
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Tahirov, T.H.; Oki, H.; Tsukihara, T.; Ogasahara, K.; Yutani, K.; Ogata, K.; Izu, Y.; Tsunasawa, S.; Kato, I.
Crystal structure of methionine aminopeptidase from hyperthermophile, Pyrococcus furiosus
J. Mol. Biol.
284
101-124
1998
Pyrococcus furiosus
brenda
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
Biochemistry
44
121-129
2005
Pyrococcus furiosus (P56218), Pyrococcus furiosus
brenda
Copik, A.J.; Waterson, S.; Swierczek, S.I.; Bennett, B.; Holz, R.C.
Both nucleophile and substrate bind to the catalytic Fe(II)-center in the type-II methionyl aminopeptidase from Pyrococcus furiosus
Inorg. Chem.
44
1160-1162
2005
Pyrococcus furiosus
brenda
Mitra, S.; Dygas-Holz, A.M.; Jiracek, J.; Zertova, M.; Zakova, L.; Holz, R.C.
A new colorimetric assay for methionyl aminopeptidases: examination of the binding of a new class of pseudopeptide analog inhibitors
Anal. Biochem.
357
43-49
2006
Escherichia coli, Pyrococcus furiosus
brenda
Mitra, S.; Sheppard, G.; Wang, J.; Bennett, B.; Holz, R.C.
Analyzing the binding of Co(II)-specific inhibitors to the methionyl aminopeptidases from Escherichia coli and Pyrococcus furiosus
J. Biol. Inorg. Chem.
14
573-585
2009
Escherichia coli, Pyrococcus furiosus
brenda
Tahirov, T.H.; Oki, H.; Tsukihara, T.; Ogasahara, K.; Yutani, K.; Libeu, C.P.; Izu, Y.; Tsunasawa, S.; Kato, I.
High-resolution crystals of methionine aminopeptidase from Pyrococcus furiosus obtained by water-mediated transformation
J. Struct. Biol.
121
68-72
1998
Pyrococcus furiosus (P56218), Pyrococcus furiosus
brenda
Arif, A.; Gardner, Q.; Rashid, N.; Akhtar, M.
Production of human interferon alpha-2b in Escherichia coli and removal of N-terminal methionine utilizing archaeal methionine aminopeptidase
Biologia (Poland)
70
982-987
2015
Pyrococcus furiosus
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brenda