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Information on EC 3.4.11.18 - methionyl aminopeptidase and Organism(s) Pyrococcus furiosus and UniProt Accession P56218
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EC Tree
3.4.11.18 methionyl aminopeptidaseSpecify your search results
Word Map
- 3.4.11.18
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microtubule-associated
- microtubule
- dendritic
- hippocampus
- tubulin
- protein-2
- tau
- cerebral
- aminopeptidases
- fumagillin
- nestin
-
neurite
- cortical
- cytoskeletal
- neurofilament
-
neuroprotective
- ischemia
-
fibrillary
-
synaptophysin
-
outgrowth
-
neurotrophic
-
neuron-specific
- beta-tubulin
-
neurogenesis
- map2
- synapsin
-
antiangiogenic
-
deformylase
-
microtubule-binding
- calbindin
- synthesis
-
dinuclear
-
microsporidian
- drug development
- medicine
The taxonomic range for the selected organisms is: Pyrococcus furiosus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
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
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
aminopeptidase, methionine
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initiation factor 2 associated 67 kDa glycoprotein
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-
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L-methionine aminopeptidase
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-
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MAP
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-
-
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MetAP
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-
-
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MetAP-1
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-
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MetAP-2
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-
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MetAP1
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-
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MetAP2
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-
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methionine aminopeptidase
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-
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p67
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p67eIF2
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peptidase M
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
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-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -
CAS REGISTRY NUMBER
COMMENTARY
61229-81-0
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mn2+
enzyme contains 2 Mn-ions residing in a distorted trigonal bipyramidal geometry. A bridging water molecule is displaced by L-methionine
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
((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
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.057
L-Met-p-nitroanilide
-
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
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.002 - 0.02
((2RS,3R)-3-amino-2-hydroxy-5-ethylthio)pentanoyl-((S)-(-)-(1-naphthyl)ethyl)amide
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
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.02 - 0.027
((2RS,3R)-3-amino-2-hydroxy-5-ethylthio)pentanoyl-((S)-(-)-(1-naphthyl)ethyl)amide
0.02
((2RS,3R)-3-amino-2-hydroxy-5-ethylthio)pentanoyl-((S)-(-)-(1-naphthyl)ethyl)amide
Pyrococcus furiosus
-
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
-
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
-
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
-
Mn2+-loaded wild type enzyme, in 25 mM HEPES buffer, pH 7.5, containing 150 mM KCl, at 30°C
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
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
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
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
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
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
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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