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Information on EC 3.4.11.18 - methionyl aminopeptidase and Organism(s) Homo sapiens and UniProt Accession Q6UB28
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EC Tree
3.4.11.18 methionyl aminopeptidaseSpecify your search results
Word Map
- 3.4.11.18
-
microtubule-associated
- microtubule
- dendritic
- hippocampus
- tubulin
- protein-2
- tau
- cerebral
- aminopeptidases
- fumagillin
- nestin
-
neurite
- cortical
- cytoskeletal
- neurofilament
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neuroprotective
- ischemia
-
fibrillary
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synaptophysin
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outgrowth
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neurotrophic
-
neuron-specific
- beta-tubulin
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neurogenesis
- map2
- synapsin
-
antiangiogenic
-
deformylase
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microtubule-binding
- calbindin
- synthesis
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dinuclear
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microsporidian
- drug development
- medicine
The taxonomic range for the selected organisms is: Homo sapiens
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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-
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initiation factor 2 associated 67 kDa glycoprotein
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L-methionine aminopeptidase
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MAP
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-
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MetAP
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-
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MetAP-1
MetAP-2
MetAP1
MetAP2
methionine aminopeptidase
methionine aminopeptidase 2
methionine aminopeptidase type 2
methionine aminopeptidase type II
methionine aminopeptidase-1
methionine aminopeptidase-2
p67
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-
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p67eIF2
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-
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peptidase M
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MetAP-1
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MetAP-2
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MetAP1
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MetAP2
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MetAP2
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methionine aminopeptidase
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-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
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PATHWAY SOURCE
PATHWAYS
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-, -
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
14-3-3gamma protein + H2O
?
14-3-3gamma is a shared substrate between isoform MetAP1 and MetAP2 in HUVEC cells
-
-
?
glyceraldehye 3-phosphate dehydrogenase + H2O
?
-
MetAP2-specific substrate
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-
?
L-methionine-7-amido-4-methylcoumarin + H2O
L-methionine + 7-amino-4-methylcoumarin
-
-
-
?
MAPLDLDRWGRPVGRRRRPVRVYP-OH + H2O
L-methionine + APLDLDRWGRPVGRRRRPVRVYP-OH
sequence corresponds to the N-terminus of the human serine/threonine-protein phosphatase 6 catalytic subunit protein
-
-
?
Met-Gly-Ala-Gln-Phe-Ser-Lys-Thr + H2O
Met + Gly-Ala-Gln-Phe-Ser-Lys-Thr
-
-
-
-
?
MGKVKVGV + H2O
L-Met + GKVKVGV
N-terminal peptide of glyceraldehyde 3-phosphate dehydrogenase
-
-
?
MGNLKSVA + H2O
L-Met + GNLKSVA
N-terminal peptide of endothelial nitric oxide synthase
-
-
?
MTNKSSLKNN-OH + H2O
L-methionine + TNKSSLKNN-OH
sequence corresponds to the N-terminus of the yeast VHS3 protein
-
-
?
SH3 binding glutamic acid rich-like protein + H2O
?
-
MetAP2-specific substrate
-
-
?
Met-peptide + H2O
Met + peptide
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the enzyme is directly involved in the regulation of growth factor-stimulated endothelial cell proliferation
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-
?
additional information
?
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while the nature of the P1' residue of peptide substrates dictates the substrate specificity in the active site of metAP2 the P2' residue appears to play a key role in the kinetics of peptidolysis. The catalytic efficiency of dipeptide substrates is at least 250fold lower than those of the tripeptides. When the P1' amino acid of the peptide substrate is sterically large such as with L-Leu, MetAP2 exhibits no detectable activity. L-Nle is the only amino acid residue other than L-Met that can be accomodated at the N-terminus of a substrate
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-
?
additional information
?
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together with N-myristoyltransferase, enzyme plays a major role in the process of myristoylation of oncoproteins including the c-src family
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-
?
additional information
?
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no activity when using Glu-Ala-Ser and Leu-Ala-Ser peptides as substrates
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-
?
additional information
?
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active site strutcure and substrate binding, overview
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-
?
additional information
?
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substrate specificity is systematically profiled by screening against a combinatorial peptide library and kinetic analysis of individually synthesized peptide substrates
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-
?
NATURAL SUBSTRATE
NATURAL 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
additional information
?
-
-
together with N-myristoyltransferase, enzyme plays a major role in the process of myristoylation of oncoproteins including the c-src family
-
-
?
Met-peptide + H2O
Met + peptide
-
the enzyme is directly involved in the regulation of growth factor-stimulated endothelial cell proliferation
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-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Co2+
significant activation at 0.01 mM, at least two Co2+ ions, which may act cooperatively, are needed to promote catalysis
Co2+
Mn2+
-
stimulates activity of MetAP2 with Met-Ala-Ser or Met-Gly-Ala-Gln-Phe-Ser-Lys-Thr 10-20fold, maximal stimulation at 0.001 mM. In presence of 5 mM glutathione 30-40fold stimulation
Zn2+
Co2+
-
stimulates activity of MetAP2 with Met-Ala-Ser or Met-Gly-Ala-Gln-Phe-Ser-Lys-Thr 10-20fold, maximal stimulation at 0.01 mM. In presence of 5 mM glutathione 30-40fold stimulation
Co2+
-
at low concentrations, 0.01 mM, Co2+ plays a key role in the stimulation of enzyme activity. It is still questionable that Co(II) is the physically relevant divalent cation
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(2E,4E,6E,8E)-10-((3R,4S,5S,6R)-5-methoxy-4-((2R,3R)-2-methyl-3-(3-methylbut-2-enyl)oxiran-2-yl)-1-oxaspiro[2.5]octan-6-yloxy)-10-oxodeca-2,4,6,8-tetraenoic acid
-
-
(3E)-3-(furan-2-ylmethylidene)-5-(hydroxymethyl)-1-methoxy-6-[2-methyl-3-(3-methylbut-2-en-1-yl)oxiran-2-yl]bicyclo[3.1.0]hexan-2-one
no activity at 0.1 mM
(3R,4S,5S,6R)-5-methoxy-4-((2R,3R)-2-methyl-3-(3-methylbut-2-enyl)oxiran-2-yl)-1-oxaspiro[2.5]octan-6-ol
-
-
(3R,4S,5S,6R)-5-methoxy-4-((2R,3R)-2-methyl-3-(3-methylbut-2-enyl)oxiran-2-yl)-1-oxaspiro[2.5]octan-6-yl (2R)-3-methyl-1-(2-(1-methylpyrrolidin-2-yl)ethylamino)-1-oxobutan-2-ylcarbamate
-
-
(3R,4S,5S,6R)-5-methoxy-4-((2R,3R)-2-methyl-3-(3-methylbut-2-enyl)oxiran-2-yl)-1-oxaspiro[2.5]octan-6-yl (R)-1-amino-3-methyl-1-oxobutan-2-yl carbamate
-
i.e. PPI-2458, advanced into phase I clinical studies in non-Hodgkin's lymphoma and solid cancers, overview
(3R,4S,5S,6R)-5-methoxy-4-((2R,3R)-2-methyl-3-(3-methylbut-2-enyl)oxiran-2-yl)-1-oxaspiro[2.5]octan-6-yl (R)-1-amino-3-methyl-1-oxobutan-2-ylcarbamate
-
-
(3R,4S,5S,6R)-5-methoxy-4-((2R,3R)-2-methyl-3-(3-methylbut-2-enyl)oxiran-2-yl)-1-oxaspiro[2.5]octan-6-yl (R)-1-hydroxy-3-methylbutan-2-ylcarbamate
-
-
(3R,4S,5S,6R)-5-methoxy-4-((2R,3R)-2-methyl-3-(3-methylbut-2-enyl)oxiran-2-yl)-1-oxaspiro[2.5]octan-6-yl (R)-3-methyl-1-(morpholinoamino)-1-oxobutan-2-ylcarbamate
-
-
(3R,4S,5S,6R)-5-methoxy-4-((2R,3R)-2-methyl-3-(3-methylbut-2-enyl)oxiran-2-yl)-1-oxaspiro[2.5]octan-6-yl (R)-3-methyl-1-oxo-1-(2-(pyrrolidin-1-yl)ethylamino)butan-2-ylcarbamate
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(3R,4S,5S,6R)-5-methoxy-4-((2R,3R)-2-methyl-3-(3-methylbut-2-enyl)oxiran-2-yl)-1-oxaspiro[2.5]octan-6-yl 1-amino-2-methyl-1-oxopropan-2-ylcarbamate
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-
(3R,4S,5S,6R)-5-methoxy-4-((2R,3R)-2-methyl-3-(3-methylbut-2-enyl)oxiran-2-yl)-1-oxaspiro[2.5]octan-6-yl 1-carbamoylcyclopentylcarbamate
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(3R,4S,5S,6R)-5-methoxy-4-((2R,3R)-2-methyl-3-(3-methylbut-2-enyl)oxiran-2-yl)-1-oxaspiro[2.5]octan-6-yl 2-(1-methylpyrrolidin-2-yl)ethylcarbamate
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(3R,4S,5S,6R)-5-methoxy-4-((2R,3R)-2-methyl-3-(3-methylbut-2-enyl)oxiran-2-yl)-1-oxaspiro[2.5]octan-6-yl 2-(pyrrolidin-1-yl)ethylcarbamate
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(3R,4S,5S,6R)-5-methoxy-4-((2R,3R)-2-methyl-3-(3-methylbut-2-enyl)oxiran-2-yl)-1-oxaspiro[2.5]octan-6-yl isopropylcarbamate
-
-
(3R,4S,5S,6R)-5-methoxy-4-((2R,3R)-2-methyl-3-(3-methylbut-2-enyl)oxiran-2-yl)-1-oxaspiro[2.5]octan-6-yl morpholinocarbamate
-
-
(3R,4S,5S,6R)-5-methoxy-4-((2R,3R)-2-methyl-3-(3-methylbut-2-enyl)oxiran-2-yl)-1-oxaspiro[2.5]octan-6-yl tert-butylcarbamate
-
-
(3R,5S,6R)-5-methoxy-4-[(3R)-2-methyl-3-(3-methylbut-2-en-1-yl)oxiran-2-yl]-1-oxaspiro[2.5]oct-6-yl (chloroacetyl)carbamate
-
-
(8S)-2-[[(4-fluorophenyl)sulfonyl]amino]-8-methyl-5,6,7,8-tetrahydronaphthalene-1-carboxylic acid
-
(R)-methyl 2-(((3R,4S,5S,6R)-5-methoxy-4-((2R,3R)-2-methyl-3-(3-methylbut-2-enyl)oxiran-2-yl)-1-oxaspiro[2.5]octan-6-yloxy)carbonylamino)-2-phenylacetate
-
-
(R)-methyl 2-(((3R,4S,5S,6R)-5-methoxy-4-((2R,3R)-2-methyl-3-(3-methylbut-2-enyl)oxiran-2-yl)-1-oxaspiro[2.5]octan-6-yloxy)carbonylamino)-3-methylbutanoate
-
-
(R)-methyl 2-(((3R,4S,5S,6R)-5-methoxy-4-((2R,3R)-2-methyl-3-(3-methylbut-2-enyl)oxiran-2-yl)-1-oxaspiro[2.5]octan-6-yloxy)carbonylamino)-4-methylpentanoate
-
-
(S)-methyl 2-(((3R,4S,5S,6R)-5-methoxy-4-((2R,3R)-2-methyl-3-(3-methylbut-2-enyl)oxiran-2-yl)-1-oxaspiro[2.5]octan-6-yloxy)-carbonylamino)-3-methylbutanoate
-
-
1-(((3R,4S,5S,6R)-5-methoxy-4-((2R,3R)-2-methyl-3-(3-methylbut-2-enyl)oxiran-2-yl)-1-oxaspiro[2.5]octan-6-yloxy)carbonyl)-piperidine-4-carboxylic acid
-
-
1-(5-chloro-6-methyl-2-pyridin-2-ylpyrimidin-4-yl)-4-(2,4-dichlorobenzyl)-1,4-diazepane
-
1-methoxy-5-(methoxymethyl)-6-[2-methyl-3-(3-methylbut-2-en-1-yl)oxiran-2-yl]bicyclo[3.1.0]hexan-2-one
no activity at 0.1 mM
2-(2-(((3R,4S,5S,6R)-5-methoxy-4-((2R,3R)-2-methyl-3-(3-methylbut-2-enyl)oxiran-2-yl)-1-oxaspiro[2.5]octan-6-yloxy)-carbonylamino)ethyl)-1,1-dimethylpyrrolidinium iodide
-
-
2-(5-methoxy-6-[2-methyl-3-((3-methylbut-2-en-1-yl)oxiran-2-yl]-4-oxobicyclo[3.1.0]hex-1-yl)methyl)-1H-isoindole-1,3(2H)-dione
no activity at 0.1 mM
2-({3-[3,5-bis[4-nitrobenzylidene]-4-oxopiperidin-1-yl]-3-oxopropylsulfanyl) ethanesulfonic acid
-
inhibitor of MetAP2
2-[[(4-fluorophenyl)sulfonyl]amino]-5,6,7,8-tetrahydronaphthalene-1-carboxylic acid
-
2-[[(4-fluorophenyl)sulfonyl]amino]-8-methyl-5,6-dihydronaphthalene-1-carboxylic acid
-
3-(((2-(((1'-methyl-1,4'-bipiperidin-4-yl)methyl)amino)phenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000055 mM, 50% inhibition of proliferation of HT-1080 cells at 0.00037 mM
3-(((2-(((1-(1-methylethyl)piperidin-4-yl)methyl)amino)phenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000046 mM, 50% inhibition of proliferation of HT-1080 cells at 0.00095 mM
3-(((2-(((1-methylpiperidin-4-yl)methyl)amino)phenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000015 mM, 50% inhibition of proliferation of HT-1080 cells at 0.00013 mM
3-(((2-(((2-(diethylamino)ethyl)carbamoyl)amino)phenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000017 mM, 50% inhibition of proliferation of HT-1080 cells at 0.00037 mM
3-(((2-((1E)-3-((2-hydroxyethyl)(methyl)amino)prop-1-en-1-yl)phenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000015 mM, 50% inhibition of proliferation of HT-1080 cells at 0.000024 mM
3-(((2-((1E)-3-(4-methylpiperazin-1-yl)prop-1-en-1-yl)phenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000018 mM, 50% inhibition of proliferation of HT-1080 cells at 0.000042 mM
3-(((2-((1E)-3-(diethylamino)but-1-en-1-yl)-4-fluorophenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000016 mM, 50% inhibition of proliferation of HT-1080 cells at 0.00007 mM
3-(((2-((1E)-3-(diethylamino)but-1-en-1-yl)phenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000019 mM, 50% inhibition of proliferation of HT-1080 cells at 0.00026 mM
3-(((2-((1E)-3-(diethylamino)prop-1-en-1-yl)-4-fluorophenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000011 mM, 50% inhibition of proliferation of HT-1080 cells at 0.000006 mM
3-(((2-((1E)-3-(diethylamino)prop-1-en-1-yl)phenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
3-(((2-((1E)-3-(dimethylamino)prop-1-en-1-yl)-4-fluorophenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000019 mM, 50% inhibition of proliferation of HT-1080 cells at 0.000036 mM
3-(((2-((1E)-3-(dimethylamino)prop-1-en-1-yl)phenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000017 mM, 50% inhibition of proliferation of HT-1080 cells at 0.000081 mM
3-(((2-((1E)-3-(ethyl(2-hydroxyethyl)amino)but-1-en-1-yl)phenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000015 mM, 50% inhibition of proliferation of HT-1080 cells at 0.000038 mM
3-(((2-((1E)-3-(ethyl(methyl)amino)prop-1-en-1-yl)phenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000009 mM, 50% inhibition of proliferation of HT-1080 cells at 0.000023 mM
3-(((2-((1E)-3-(methyl(1-methylethyl)amino)prop-1-en-1-yl)phenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000012 mM, 50% inhibition of proliferation of HT-1080 cells at 0.000027 mM
3-(((2-((1E)-4-(diethylamino)but-1-en-1-yl)phenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
3-(((2-((1E)-5-(diethylamino)pent-1-en-1-yl)phenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
3-(((2-((2-(1-(1-methylethyl)pyrrolidin-2-yl)ethyl)amino)phenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000062 mM, 50% inhibition of proliferation of HT-1080 cells at 0.00035 mM
3-(((2-((2-(1-(1-methylpiperidin-4-yl)pyrrolidin-2-yl)ethyl)amino)phenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000070 mM, 50% inhibition of proliferation of HT-1080 cells at 0.0005 mM
3-(((2-((2-(1-(cyclohexylmethyl)pyrrolidin-2-yl)ethyl)amino)phenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.00015 mM, 50% inhibition of proliferation of HT-1080 cells at 0.0015 mM
3-(((2-((2-(1-piperidin-4-ylpyrrolidin-2-yl)ethyl)amino)phenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000069 mM, 50% inhibition of proliferation of HT-1080 cells at 0.0013 mM
3-(((2-((2-(1H-imidazol-1-yl)ethyl)amino)phenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000010 mM, 50% inhibition of proliferation of HT-1080 cells at 0.0029 mM
3-(((2-((2-(2-oxopyrrolidin-1-yl)ethyl)amino)phenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000040 mM, 50% inhibition of proliferation of HT-1080 cells at 0.0014 mM
3-(((2-((2-(bis(1-methylethyl)amino)ethyl)amino)phenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000031 mM, 50% inhibition of proliferation of HT-1080 cells at 0.00064 mM
3-(((2-((2-(diethylamino)ethyl)amino)phenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000031 mM, 50% inhibition of proliferation of HT-1080 cells at 0.00054 mM
3-(((2-((2-(diethylamino)ethyl)carbamoyl)phenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000031 mM, 50% inhibition of proliferation of HT-1080 cells at 0.00052 mM
3-(((2-((2-(dimethylamino)ethyl)amino)phenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000048 mM, 50% inhibition of proliferation of HT-1080 cells at 0.0013 mM
3-(((2-((2-(dimethylamino)ethyl)sulfanyl)-4-fluorophenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000030 mM, 50% inhibition of proliferation of HT-1080 cells at 0.0007 mM
3-(((2-((2-pyridin-2-ylethyl)amino)phenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000053 mM, 50% inhibition of proliferation of HT-1080 cells at 0.0020 mM
3-(((2-((2-pyridin-4-ylethyl)amino)phenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000016 mM, 50% inhibition of proliferation of HT-1080 cells at 0.0085 mM
3-(((2-((2-pyrrolidin-1-ylethyl)amino)phenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000069 mM, 50% inhibition of proliferation of HT-1080 cells at 0.0022 mM
3-(((2-((2-pyrrolidin-2-ylethyl)amino)phenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000022 mM, 50% inhibition of proliferation of HT-1080 cells at 0.00014 mM
3-(((2-((3-((2-hydroxyethyl)amino)propyl)amino)phenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000015 mM, 50% inhibition of proliferation of HT-1080 cells at 0.00028 mM
3-(((2-((3-((2-tert-butoxy-2-oxoethyl)amino)propyl)amino)phenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.00011 mM, 50% inhibition of proliferation of HT-1080 cells at 0.0043 mM
3-(((2-((3-((tert-butoxycarbonyl)amino)propyl)amino)phenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000077 mM, 50% inhibition of proliferation of HT-1080 cells at 0.0049 mM
3-(((2-((3-(1,4'-bipiperidin-1'-yl)propyl)amino)phenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000058 mM, 50% inhibition of proliferation of HT-1080 cells at 0.0011 mM
3-(((2-((3-(1-methylpyrrolidin-2-yl)propyl)amino)phenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000017 mM, 50% inhibition of proliferation of HT-1080 cells at 0.000096 mM
3-(((2-((3-(4-methylpiperazin-1-yl)propyl)amino)phenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000026 mM, 50% inhibition of proliferation of HT-1080 cells at 0.00041 mM
3-(((2-((3-(bis(1-methylethyl)amino)propyl)amino)phenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000052 mM, 50% inhibition of proliferation of HT-1080 cells at 0.00029 mM
3-(((2-((3-(bis(2-hydroxyethyl)amino)propyl)amino)phenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000026 mM, 50% inhibition of proliferation of HT-1080 cells at 0.001 mM
3-(((2-((3-(diethylamino)-1-methylpropyl)carbamoyl)-4-fluorophenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000067 mM, 50% inhibition of proliferation of HT-1080 cells at 0.00012 mM
3-(((2-((3-(diethylamino)-1-methylpropyl)carbamoyl)phenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000017 mM, 50% inhibition of proliferation of HT-1080 cells at 0.0026 mM
3-(((2-((3-(diethylamino)propyl)amino)-4-methylphenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.00015 mM, 50% inhibition of proliferation of HT-1080 cells at 0.0021 mM
3-(((2-((3-(diethylamino)propyl)amino)-5-(trifluoromethyl)phenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.00069 mM, 50% inhibition of proliferation of HT-1080 cells at 0.100 mM
3-(((2-((3-(diethylamino)propyl)amino)-5-methylphenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000066 mM, 50% inhibition of proliferation of HT-1080 cells at 0.00066 mM
3-(((2-((3-(diethylamino)propyl)amino)-6-fluorophenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
3-(((2-((3-(diethylamino)propyl)amino)phenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000025 mM, 50% inhibition of proliferation of HT-1080 cells at 0.0014 mM
3-(((2-((3-(diethylamino)propyl)carbamoyl)phenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000025 mM, 50% inhibition of proliferation of HT-1080 cells at 0.00055 mM
3-(((2-((3-(dimethylamino)-2,2-dimethylpropyl)amino)phenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000018 mM, 50% inhibition of proliferation of HT-1080 cells at 0.00061 mM
3-(((2-((3-(dimethylamino)propyl)amino)phenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000014 mM, 50% inhibition of proliferation of HT-1080 cells at 0.00019 mM
3-(((2-((3-(ethylamino)propyl)amino)phenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000012 mM, 50% inhibition of proliferation of HT-1080 cells at 0.00011 mM
3-(((2-((3-aminopropyl)amino)phenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000013 mM, 50% inhibition of proliferation of HT-1080 cells at 0.00016 mM
3-(((2-((3-morpholin-4-ylpropyl)amino)phenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000022 mM, 50% inhibition of proliferation of HT-1080 cells at 0.00032 mM
3-(((2-((3-piperazin-1-ylpropyl)amino)phenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000020 mM, 50% inhibition of proliferation of HT-1080 cells at 0.00051 mM
3-(((2-((3-pyrrolidin-1-ylpropyl)amino)phenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000017 mM, 50% inhibition of proliferation of HT-1080 cells at 0.000085 mM
3-(((2-((4-(diethylamino)-1-methylbutyl)amino)phenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.00013 mM, 50% inhibition of proliferation of HT-1080 cells at 0.00021 mM
3-(((2-((4-(dimethylamino)butyl)amino)phenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000012 mM, 50% inhibition of proliferation of HT-1080 cells at 0.00046 mM
3-(((2-((piperidin-3-ylmethyl)amino)phenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000035 mM, 50% inhibition of proliferation of HT-1080 cells at 0.00029 mM
3-(((2-((piperidin-4-ylmethyl)amino)phenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000017 mM, 50% inhibition of proliferation of HT-1080 cells at 0.00046 mM
3-(((2-((pyridin-4-ylmethyl)amino)phenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000035 mM, 50% inhibition of proliferation of HT-1080 cells at 0.017 mM
3-(((2-((pyrrolidin-3-ylmethyl)amino)phenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000034 mM, 50% inhibition of proliferation of HT-1080 cells at 0.00038 mM
3-(((2-(3,3,4,5,5-pentamethylpiperazin-1-yl)phenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000091 mM, 50% inhibition of proliferation of HT-1080 cells at 0.015 mM
3-(((2-(3-(diethylamino)propoxy)phenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000018 mM, 50% inhibition of proliferation of HT-1080 cells at 0.0062 mM
3-(((2-(3-(diethylamino)propyl)-4-fluorophenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000017 mM, 50% inhibition of proliferation of HT-1080 cells at 0.000024 mM
3-(((2-(3-(diethylamino)propyl)phenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000009 mM, 50% inhibition of proliferation of HT-1080 cells at 0.000073 mM
3-(((2-(3-(dimethylamino)propyl)phenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000010 mM, 50% inhibition of proliferation of HT-1080 cells at 0.000035 mM
3-(((2-(4-(diethylamino)butyl)phenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000019 mM, 50% inhibition of proliferation of HT-1080 cells at 0.000068 mM
3-(((2-(4-benzylpiperazin-1-yl)phenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000020 mM, 50% inhibition of proliferation of HT-1080 cells at 0.0016 mM
3-(((2-(5-(diethylamino)pentyl)phenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000045 mM, 50% inhibition of proliferation of HT-1080 cells at 0.00035mM
3-(((2-aminophenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000013 mM, 50% inhibition of proliferation of HT-1080 cells at 0.0062 mM
3-(((3-chloro-2-((3-(diethylamino)propyl)amino)phenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000015 mM, 50% inhibition of proliferation of HT-1080 cells at 0.00037 mM
3-(((3R,4S,5S,6R)-5-methoxy-4-((2R,3R)-2-methyl-3-(3-methylbut-2-enyl)oxiran-2-yl)-1-oxaspiro[2.5]octan-6-yloxy)carbonylamino)-N,N,N-trimethylpropan-1-aminium iodide
-
-
3-(((4-chloro-2-((3-(diethylamino)propyl)amino)-5-fluorophenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.00079 mM, 50% inhibition of proliferation of HT-1080 cells at 0.013 mM
3-(((4-chloro-2-((3-(diethylamino)propyl)amino)phenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.00011 mM, 50% inhibition of proliferation of HT-1080 cells at 0.0031 mM
3-(((5-chloro-2-((3-(diethylamino)propyl)amino)phenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000056 mM, 50% inhibition of proliferation of HT-1080 cells at 0.010 mM
3-((4-methylpent-3-enoyl)amino)-N-1,3-thiazol-2-ylpyridine-2-carboxamide
-
wild-type, 50% inhibition at 0.0149 mM, mutant lacking N-terminal 66 amino acids, 50% inhibition at 0.00068 mM
3-((5-methylhex-4-enoyl)amino)-N-1,3-thiazol-2-ylpyridine-2-carboxamide
-
wild-type, 50% inhibition at 0.0074 mM, mutant lacking N-terminal 66 amino acids, 50% inhibition at 0.0010 mM
3-((cyclopent-1-en-1-ylcarbonyl)amino)-N-1,3-thiazol-2-ylpyridine-2-carboxamide
-
wild-type, 50% inhibition above 100 mM, mutant lacking N-terminal 66 amino acids, 50% inhibition above 100 mM
3-((phenylsulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000010 mM, 50% inhibition of proliferation of HT-1080 cells at 0.0024 mM
3-((R)-2-(((3R,4S,5S,6R)-5-methoxy-4-((2R,3R)-2-methyl-3-(3-methylbut-2-enyl)oxiran-2-yl)-1-oxaspiro[2.5]octan-6-yloxy)-carbonylamino)-3-methylbutanamido)benzoic acid
-
-
3-(2,3-dihydro-1,4-benzodioxin-6-yl)-5-{[(2-nitrophenyl)methyl]sulfanyl}-4-phenyl-4H-1,2,4-triazole
-
-
3-(2,3-dihydrobenzo[b][1,4]dioxin-6-yl)-5-(2-fluorobenzylthio)-4-phenyl-4H-1,2,4-triazole
-
-
3-(2,3-dihydrobenzo[b][1,4]dioxin-6-yl)-5-(2-methylbenzylthio)-4-phenyl-4H-1,2,4-triazole
-
-
3-(2,3-dihydrobenzo[b][1,4]dioxin-6-yl)-5-(2-nitrobenzylthio)-4-phenyl-4H-1,2,4-triazole
-
-
3-(2,3-dihydrobenzo[b][1,4]dioxin-6-yl)-5-(3-methoxybenzylthio)-4-phenyl-4H-1,2,4-triazole
-
-
3-(2,3-dihydrobenzo[b][1,4]dioxin-6-yl)-5-(4-fluorobenzylthio)-4-phenyl-4H-1,2,4-triazole
-
-
3-(2,3-dihydrobenzo[b][1,4]dioxin-6-yl)-5-(4-nitrobenzylthio)-4-phenyl-4H-1,2,4-triazole
-
-
3-(2,4-difluorobenzylthio)-5-(2,3-dihydrobenzo[b][1,4]dioxin-6-yl)-4-phenyl-4H-1,2,4-triazole
-
-
3-(2,6-difluorobenzylthio)-5-(2,3-dihydrobenzo[b][1,4]dioxin-6-yl)-4-phenyl-4H-1,2,4-triazole
-
-
3-(2-bromobenzylthio)-5-(2,3-dihydrobenzo[b][1,4]dioxin-6-yl)-4-phenyl-4H-1,2,4-triazole
-
-
3-(2-chlorobenzylthio)-5-(2,3-dihydrobenzo[b][1,4]dioxin-6-yl)-4-phenyl-4H-1,2,4-triazole
-
-
3-(3-bromobenzylthio)-5-(2,3-dihydrobenzo[b][1,4]dioxin-6-yl)-4-phenyl-4H-1,2,4-triazole
-
-
3-(3-chlorobenzylthio)-5-(2,3-dihydrobenzo[b][1,4]dioxin-6-yl)-4-phenyl-4H-1,2,4-triazole
-
-
3-(4-bromobenzylthio)-5-(2,3-dihydrobenzo[b][1,4]dioxin-6-yl)-4-phenyl-4H-1,2,4-triazole
-
-
3-(4-chlorobenzylthio)-5-(2,3-dihydrobenzo[b][1,4]dioxin-6-yl)-4-phenyl-4H-1,2,4-triazole
-
-
3-(benzoylamino)-N-1,3-thiazol-2-ylpyridine-2-carboxamide
-
wild-type, 50% inhibition above 100 mM, mutant lacking N-terminal 66 amino acids, 50% inhibition at 0.0074 mM
3-(benzylthio)-5-(2,3-dihydrobenzo[b][1,4]dioxin-6-yl)-4-phenyl-4H-1,2,4-triazole
-
-
3-(hexanoylamino)-N-1,3-thiazol-2-ylpyridine-2-carboxamide
-
wild-type, 50% inhibition at 0.0867 mM, mutant lacking N-terminal 66 amino acids, 50% inhibition at 0.0020 mM
3-(pent-4-enoylamino)-N-1,3-thiazol-2-ylpyridine-2-carboxamide
-
wild-type, 50% inhibition above 0.1 mM, mutant lacking N-terminal 66 amino acids, 50% inhibition at 0.00079 mM
3-hydroxy-N-1,3-thiazol-2-ylpyridine-2-carboxamide
-
wild-type, 50% inhibition at 0.0081 mM, mutant lacking N-terminal 66 amino acids, 50% inhibition at 0.0035 mM
3-[(phenylsulfonyl)amino]-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
-
4-((((3R,4S,5S,6R)-5-methoxy-4-((2R,3R)-2-methyl-3-(3-methylbut-2-enyl)oxiran-2-yl)-1-oxaspiro[2.5]octan-6-yloxy)carbonylamino)methyl)benzoic acid
-
-
4-methyl-2-(1H-1,2,3-triazol-5-yl)pyridine
-
Co(II)-form, Ki,app-value 8 nM, Mn(II)-form, 0.014 mM, 50% reduction of viability of human umbilical vein endothelial cell above 0.03 mM
4-[4-(4-methoxyphenyl)piperazin-1-yl]-2-(pyridin-2-yl)quinazoline
EC50 value in presence of Co(II) is 0.0001 mM, superior inhibitory potency and selectivity for isoform MetAP1
5-((R)-1-[1,2,4]triazolo[1,5-a]pyrimidin-7-yl-pyrrolidin-2-ylmethoxy)-isoquinoline
-
5-(1-benzofuran-2-yl)-1H-1,2,3-triazole
-
Co(II)-form, Ki,app-value 15 nM, Mn(II)-form, 26% inhibition at 0.02 mM, 50% reduction of viability of human umbilical vein endothelial cell at 0.006 mM
5-(3,4-dibromophenyl)-1H-1,2,3-triazole
-
Co(II)-form, Ki,app-value 1 nM, Mn(II)-form, 0.016 mM, 50% reduction of viability of human umbilical vein endothelial cell at 0.002 mM
5-(4-bromophenyl)-1H-1,2,3-triazole
-
Co(II)-form, Ki,app-value 3 nM, Mn(II)-form, 0.011 mM, 50% reduction of viability of human umbilical vein endothelial cell at 0.006 mM
5-(4-chlorophenyl)-1H-1,2,3-triazole
-
Co(II)-form, Ki,app-value 6 nM, Mn(II)-form, 0.011 mM, 50% reduction of viability of human umbilical vein endothelial cell at 0.005 mM
5-(4-iodophenyl)-1H-1,2,3-triazole
-
Co(II)-form, Ki,app-value 1 nM, Mn(II)-form, not inhibitory at 0.02 mM, 50% reduction of viability of human umbilical vein endothelial cell at 0.02 mM
5-(4-methylphenyl)-1H-1,2,3-triazole
-
Co(II)-form, Ki,app-value 15 nM, Mn(II)-form, 4400 nM, 50% reduction of viability of human umbilical vein endothelial cell at 0.03 mM
5-(hydroxymethyl)-1-methoxy-6-[2-methyl-3-(3-methylbut-2-en-1-yl)oxiran-2-yl]bicyclo[3.1.0]hexan-2-ol
no activity at 0.1 mM
5-chloro-2-(5-chloropyridin-2-yl)-6-methyl-N-((R)-2-phenyl-2-(4-phenylbutylamino)ethyl)pyrimidin-4-amine
compound shows 500fold specificity for isoform AP1 over isoform AP2
5-chloro-2-(5-chloropyridin-2-yl)-N-(2,4-diphenylbutyl)-6-methylpyrimidin-4-amine
compound shows 3175fold specificity for isoform AP1 over isoform AP2
5-chloro-6-methyl-N-(2-phenylethyl)-2-pyridin-2-ylpyrimidin-4-amine
-
5-chloro-N,6-dimethyl-N-(2-phenylethyl)-2-pyridin-2-ylpyrimidin-4-amine
-
5-methoxy-6-[2-methyl-3-(3-methylbut-2-en-1-yl)oxiran-2-yl]-4-oxobicyclo[3.1.0]hexane-1-carbaldehyde
-
5-methyl-2-((phenylsulfonyl)amino)benzoic acid
50% inhibition of enzyme at 0.0014 mM, 50% inhibition of proliferation of HT-1080 cells at 0.0072 mM
5-methyl-2-(1H-1,2,3-triazol-5-yl)pyridine
-
Co(II)-form, Ki,app-value 3 nM, Mn(II)-form, 0.015 mM, 50% reduction of viability of human umbilical vein endothelial cell at 0.002 mM
5-[(2E)-hepta-2,6-dien-4-yn-1-ylidene]pyrimidine-2,4,6(1H,3H,5H)-trione
-
5-[(3-methylbut-2-en-1-yl)sulfanyl]-N-(2-methylphenyl)-4H-1,2,4-triazol-3-amine
-
5-[(cyclohexylmethyl)sulfanyl]-N-(2-methylphenyl)-4H-1,2,4-triazol-3-amine
-
5-[(cyclohexylmethyl)sulfanyl]-N-(3,4-dimethoxyphenyl)-4H-1,2,4-triazol-3-amine
-
5-[(cyclohexylmethyl)sulfanyl]-N-(4-methoxyphenyl)-4H-1,2,4-triazol-3-amine
-
5-[(cyclohexylmethyl)sulfanyl]-N-(4-methylphenyl)-4H-1,2,4-triazol-3-amine
-
5-[[(2-methyl-2,5-dihydro-1,3-thiazol-4-yl)methyl]sulfanyl]-N-(4-methylphenyl)-4H-1,2,4-triazol-3-amine
-
5-[[(5-methylisoxazol-3-yl)methyl]sulfanyl]-N-(2-methylphenyl)-4H-1,2,4-triazol-3-amine
-
5-[[(5-methylisoxazol-3-yl)methyl]sulfanyl]-N-(4-methylphenyl)-4H-1,2,4-triazol-3-amine
-
5-[[2-(2-fluorophenyl)ethyl]sulfanyl]-N-(2-methylphenyl)-4H-1,2,4-triazol-3-amine
-
5-[[2-(2-fluorophenyl)ethyl]sulfanyl]-N-(4-methoxyphenyl)-4H-1,2,4-triazol-3-amine
-
5-[[2-(2-fluorophenyl)ethyl]sulfanyl]-N-(4-methylphenyl)-4H-1,2,4-triazol-3-amine
-
5-[[2-(2-methoxyphenyl)ethyl]sulfanyl]-N-(2-methylphenyl)-4H-1,2,4-triazol-3-amine
-
5-[[2-(2-methoxyphenyl)ethyl]sulfanyl]-N-(4-methylphenyl)-4H-1,2,4-triazol-3-amine
-
5-[[2-(3,4-difluorophenyl)ethyl]sulfanyl]-N-(2-methylphenyl)-4H-1,2,4-triazol-3-amine
-
5-[[2-(3,4-difluorophenyl)ethyl]sulfanyl]-N-(3,4-dimethoxyphenyl)-4H-1,2,4-triazol-3-amine
-
5-[[2-(3,4-difluorophenyl)ethyl]sulfanyl]-N-(4-methoxyphenyl)-4H-1,2,4-triazol-3-amine
-
5-[[2-(3,4-difluorophenyl)ethyl]sulfanyl]-N-(4-methylphenyl)-4H-1,2,4-triazol-3-amine
-
6-(1,5-dimethylhex-4-en-1-yl)-5-(hydroxymethyl)-1-methoxybicyclo[3.1.0]hexan-2-one
-
6-[(1E)-1,5-dimethylhexa-1,4-dien-1-yl]-5-(hydroxymethyl)-1-methoxybicyclo[3.1.0]hexan-2-one
-
A-310840
-
IC50: 0.000031 mM for enzyme with Zn2+, 0.000043 mM for enzyme with Ni2+, 0.000069 mM for enzyme with Co2+, 0.000026 for enzyme with Fe2+, 0.0578 mM for enzyme with Mn2+
A-311263
-
IC50: 0.000121 mM for enzyme with Zn2+, 0.000107 mM for enzyme with Ni2+, 0.000149 mM for enzyme with Co2+, 0.00011 mM for enzyme with Fe2+, 0.000055 mM for enzyme with Mn2+
ethyl (6E)-8-[(2R,3R)-3-[(1S,5S)-5-(hydroxymethyl)-1-methoxy-2-oxobicyclo[3.1.0]hex-6-yl]-3-methyloxiran-2-yl]oct-6-enoate
no activity at 0.1 mM
fumagillol
-
i.e. (3R,4S,5S,6R)-5-methoxy-4-((2R,3R)-2-methyl-3-(3-methylbut-2-enyl)oxiran-2-yl)-1-oxaspiro[2.5]octan-6-ol
isobutyl (2-((1,3-thiazol-2-ylamino)carbonyl)pyridin-3-yl)carbamate
-
wild-type, 50% inhibition above 100 mM, mutant lacking N-terminal 66 amino acids, 50% inhibition above 100 mM
methyl 4-([5-[(3-methylbut-2-en-1-yl)sulfanyl]-4H-1,2,4-triazol-3-yl]amino)benzoate
-
methyl 4-([5-[(cyclohexylmethyl)sulfanyl]-4H-1,2,4-triazol-3-yl]amino)benzoate
-
methyl 4-([5-[(pyridin-2-ylmethyl)sulfanyl]-4H-1,2,4-triazol-3-yl]amino)benzoate
-
methyl 4-([5-[(pyridin-4-ylmethyl)sulfanyl]-4H-1,2,4-triazol-3-yl]amino)benzoate
-
methyl 4-[(5-[[(2-methyl-1,3-thiazolidin-4-yl)methyl]sulfanyl]-4H-1,2,4-triazol-3-yl)amino]benzoate
-
methyl 4-[(5-[[(5-methylisoxazol-3-yl)methyl]sulfanyl]-4H-1,2,4-triazol-3-yl)amino]benzoate
-
methyl 4-[(5-[[2-(2-fluorophenyl)ethyl]sulfanyl]-4H-1,2,4-triazol-3-yl)amino]benzoate
-
methyl 4-[(5-[[2-(2-methoxyphenyl)ethyl]sulfanyl]-4H-1,2,4-triazol-3-yl)amino]benzoate
-
methyl 4-[(5-[[2-(2-methylphenyl)ethyl]sulfanyl]-4H-1,2,4-triazol-3-yl)amino]benzoate
-
methyl 4-[(5-[[2-(3,4-difluorophenyl)ethyl]sulfanyl]-4H-1,2,4-triazol-3-yl)amino]benzoate
-
N-((R)-2-(5-chloro-2-(5-chloropyridin-2-yl)-6-methylpyrimidin-4-ylamino)-1-phenylethyl)-3-phenylpropanamide
compound shows 323fold specificity for isoform AP1 over isoform AP2
N-(2-methylphenyl)-5-[(pyridin-4-ylmethyl)sulfanyl]-4H-1,2,4-triazol-3-amine
-
N-(2-methylphenyl)-5-[[(2-methyl-1,3-thiazolidin-4-yl)methyl]sulfanyl]-4H-1,2,4-triazol-3-amine
-
N-(2-methylphenyl)-5-[[2-(2-methylphenyl)ethyl]sulfanyl]-4H-1,2,4-triazol-3-amine
-
N-(3,4-dimethoxyphenyl)-5-[(3-methylbut-2-en-1-yl)sulfanyl]-4H-1,2,4-triazol-3-amine
-
N-(3,4-dimethoxyphenyl)-5-[(pyridin-2-ylmethyl)sulfanyl]-4H-1,2,4-triazol-3-amine
-
N-(3,4-dimethoxyphenyl)-5-[(pyridin-4-ylmethyl)sulfanyl]-4H-1,2,4-triazol-3-amine
-
N-(3,4-dimethoxyphenyl)-5-[[(2-methyl-1,3-thiazolidin-4-yl)methyl]sulfanyl]-4H-1,2,4-triazol-3-amine
-
N-(3,4-dimethoxyphenyl)-5-[[(5-methylisoxazol-3-yl)methyl]sulfanyl]-4H-1,2,4-triazol-3-amine
-
N-(3,4-dimethoxyphenyl)-5-[[2-(2-fluorophenyl)ethyl]sulfanyl]-4H-1,2,4-triazol-3-amine
-
N-(3,4-dimethoxyphenyl)-5-[[2-(2-methoxyphenyl)ethyl]sulfanyl]-4H-1,2,4-triazol-3-amine
-
N-(3,4-dimethoxyphenyl)-5-[[2-(2-methylphenyl)ethyl]sulfanyl]-4H-1,2,4-triazol-3-amine
-
N-(4,5-dihydro-1,3-thiazol-2-yl)-3-[(2,2-dimethylpropanoyl)amino]pyridine-2-carboxamide
-
N-(4,5-dihydro-1,3-thiazol-2-yl)-3-[(3-phenylpropanoyl)amino]pyridine-2-carboxamide
-
N-(4,5-dihydro-1,3-thiazol-2-yl)-3-[[(1E)-2-methylpropylidene]amino]pyridine-2-carboxamide
-
N-(4-chlorophenyl)-5-[(3-methylbut-2-en-1-yl)sulfanyl]-4H-1,2,4-triazol-3-amine
-
N-(4-chlorophenyl)-5-[(cyclohexylmethyl)sulfanyl]-4H-1,2,4-triazol-3-amine
-
N-(4-chlorophenyl)-5-[(pyridin-2-ylmethyl)sulfanyl]-4H-1,2,4-triazol-3-amine
-
N-(4-chlorophenyl)-5-[(pyridin-4-ylmethyl)sulfanyl]-4H-1,2,4-triazol-3-amine
-
N-(4-chlorophenyl)-5-[[(2-methyl-1,3-thiazolidin-4-yl)methyl]sulfanyl]-4H-1,2,4-triazol-3-amine
-
N-(4-chlorophenyl)-5-[[(5-methylisoxazol-3-yl)methyl]sulfany]-4H-1,2,4-triazol-3-amine
-
N-(4-chlorophenyl)-5-[[2-(2-fluorophenyl)ethyl]sulfanyl]-4H-1,2,4-triazol-3-amine
-
N-(4-chlorophenyl)-5-[[2-(2-methoxyphenyl)ethyl]sulfanyl]-4H-1,2,4-triazol-3-amine
-
N-(4-chlorophenyl)-5-[[2-(2-methylphenyl)ethyl]sulfanyl]-4H-1,2,4-triazol-3-amine
-
N-(4-methoxyphenyl)-5-[(3-methylbut-2-en-1-yl)sulfanyl]-4H-1,2,4-triazol-3-amine
-
N-(4-methoxyphenyl)-5-[(pyridin-2-ylmethyl)sulfanyl]-4H-1,2,4-triazol-3-amine
-
N-(4-methoxyphenyl)-5-[(pyridin-4-ylmethyl)sulfanyl]-4H-1,2,4-triazol-3-amine
-
N-(4-methoxyphenyl)-5-[[(5-methylisoxazol-3-yl)methyl]sulfanyl]-4H-1,2,4-triazol-3-amine
-
N-(4-methoxyphenyl)-5-[[2-(2-methoxyphenyl)ethyl]sulfanyl]-4H-1,2,4-triazol-3-amine
-
N-(4-methylphenyl)-5-[(pyridin-2-ylmethyl)sulfanyl]-4H-1,2,4-triazol-3-amine
-
N-(4-methylphenyl)-5-[(pyridin-4-ylmethyl)sulfanyl]-4H-1,2,4-triazol-3-amine
-
N-(4-methylphenyl)-5-[(thiophen-2-ylmethyl)sulfanyl]-4H-1,2,4-triazol-3-amine
-
N-(4-methylphenyl)-5-[[(2-methyl-1,3-thiazolidin-4-yl)methyl]sulfanyl]-4H-1,2,4-triazol-3-amine
-
N-(4-methylphenyl)-5-[[2-(2-methylphenyl)ethyl]sulfanyl]-4H-1,2,4-triazol-3-amine
-
N-(5-[[(2-methyl-1,3-thiazolidin-4-yl)methyl]sulfanyl]-4H-1,2,4-triazol-3-yl)pyridin-3-amine
-
N-(5-[[(5-methylisoxazol-3-yl)methyl]sulfanyl]-4H-1,2,4-triazol-3-yl)pyridin-3-amine
-
N-1,3-thiazol-2-ylpyridine-2-carboxamide
-
wild-type, 50% inhibition at 0.0104 mM, mutant lacking N-terminal 66 amino acids, 50% inhibition at 0.0049 mM
N-biphenyl-2-yl-5-[(3,4-difluorobenzyl)sulfanyl]-4H-1,2,4-triazol-3-amine
-
N-biphenyl-2-yl-5-[(3-methylbut-2-en-1-yl)sulfanyl]-4H-1,2,4-triazol-3-amine
-
N-biphenyl-2-yl-5-[(cyclohexylmethyl)sulfanyl]-4H-1,2,4-triazol-3-amine
-
N-biphenyl-2-yl-5-[(pyridin-4-ylmethyl)sulfanyl]-4H-1,2,4-triazol-3-amine
-
N-biphenyl-2-yl-5-[[(5-methylisoxazol-3-yl)methyl]sulfanyl]-4H-1,2,4-triazol-3-amine
-
N-[4-(chloromethyl)phenyl]-5-[[2-(3,4-difluorophenyl)ethyl]sulfanyl]-4H-1,2,4-triazol-3-amine
-
N-[5-[(3,4-difluorobenzyl)sulfanyl]-4H-1,2,4-triazol-3-yl]pyridin-3-amine
-
N-[5-[(cyclohexylmethyl)sulfanyl]-4H-1,2,4-triazol-3-yl]pyridin-3-amine
-
N-[5-[(pyridin-2-ylmethyl)sulfanyl]-4H-1,2,4-triazol-3-yl]pyridin-3-amine
-
N-[5-[(pyridin-4-ylmethyl)sulfanyl]-4H-1,2,4-triazol-3-yl]pyridin-3-amine
-
tert-butyl [2-(4,5-dihydro-1,3-thiazol-2-ylcarbamoyl)pyridin-3-yl]carbamate
-
[(1R)-1-carbamoyl-2-methyl-propyl]-carbamic acid-(3R,4S,5S,6R)-5-methoxy-4-[(2R,3R)-2-methyl-3-(3-methyl-but-2-enyl)-oxiranyl]-1-oxa-spiro[2.5]oct-6-yl ester
PPI-2458
[(1R)-1-carbamoyl-2-methyl-propyl]-carbamic acid-(3R,4S,5S,6R)-5-methoxy-4-[(2R,3R)-2-methyl-3-(3-methylbut-2-enyl)oxiranyl]-1-oxaspiro(2,5)oct-6-yl ester
-
PPI-2458, potent inhibitor
[amino(cyclohexyl)methyl]phosphonic acid
compound selectively inhibits the Streptococcus pneumoniae MetAP in low micromolar range but not the human enzyme. Residue F309 in the human enzyme and M205 in the Streptococcus pneumoniae MetAP at the analogous position render them with different susceptibilities against the inhibitor
3-(((2-((1E)-3-(diethylamino)prop-1-en-1-yl)phenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000012 mM, 50% inhibition of proliferation of HT-1080 cells at 0.000019 mM
3-(((2-((1E)-3-(diethylamino)prop-1-en-1-yl)phenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000027 mM, 50% inhibition of proliferation of HT-1080 cells at 0.00029 mM
3-(((2-((1E)-4-(diethylamino)but-1-en-1-yl)phenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000016 mM, 50% inhibition of proliferation of HT-1080 cells at 0.000049 mM
3-(((2-((1E)-4-(diethylamino)but-1-en-1-yl)phenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000025 mM, 50% inhibition of proliferation of HT-1080 cells at 0.00017 mM
3-(((2-((1E)-5-(diethylamino)pent-1-en-1-yl)phenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000020 mM, 50% inhibition of proliferation of HT-1080 cells at 0.00012 mM
3-(((2-((1E)-5-(diethylamino)pent-1-en-1-yl)phenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000028 mM, 50% inhibition of proliferation of HT-1080 cells at 0.000033 mM
3-(((2-((3-(diethylamino)propyl)amino)-6-fluorophenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000019 mM, 50% inhibition of proliferation of HT-1080 cells at 0.014 mM
3-(((2-((3-(diethylamino)propyl)amino)-6-fluorophenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.00018 mM, 50% inhibition of proliferation of HT-1080 cells at 0.0083 mM
bengamide A
nonspecific, reversible inhibitor of MetAP-1 and MetAP-2
Co2+
-
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
fumagillin
a covalent bond is formed between a reactive epoxide of fumagillin and histidine-231 in the active site of Met-AP2. Fumagillin-based drugs inhibit MetAP-2 but not MetAP-1
fumagillin
-
binding structure, specificity determinants lie in the S1 hydrophobic methionine binding subsite, overview
TNP-470
is likely to inhibit the enzyme by occupying the active site in the same fashion as fumagillin
TNP-470
-
binding structure, specificity determinants lie in the S1 hydrophobic methionine binding subsite, overview
additional information
-
inhibitor synthesis, pharmacokinetics, and molecular modelling
-
additional information
identification of inhibitors for human methionine aminopeptidases MetAP1 and MetAP2. 5-chloro-6-methyl-2-pyridin-2-ylpyrimidine is the minimum element for the inhibition of MetAP1, 5'-chloro is the favored substituent on the pyridine ring for the enhanced potency against MetAP1, and long C4 side chains are the essentials for higher Met AP1-selectivity
-
additional information
-
identification of inhibitors for human methionine aminopeptidases MetAP1 and MetAP2. 5-chloro-6-methyl-2-pyridin-2-ylpyrimidine is the minimum element for the inhibition of MetAP1, 5'-chloro is the favored substituent on the pyridine ring for the enhanced potency against MetAP1, and long C4 side chains are the essentials for higher Met AP1-selectivity
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.576
Met-Pro-p-nitroanilide
in 40 mM HEPES, pH 8.0, and 100 mM NaCl, at 23°C
1.8
L-Met-L-Pro-4-nitroanilide
-
truncated mutant lacking N-terminal 89 amino acids, pH 7.5, 22°C
1.28
L-Met-PSI[C(O)S]Gly-L-Phe
-
N-terminally truncated mutant, lacking 66 amino acids, pH 7.0, 22°C
8.81
L-Met-PSI[C(O)S]Gly-L-Phe
-
N-terminally truncated mutant lacking 135 amino acids, pH 7.0, 22°C
0.386
L-methionine 4-nitroanilide
wild-type, pH not specified in the publication, temperature not specified in the publication
0.4019
L-methionine 4-nitroanilide
mutant F309M, pH not specified in the publication, temperature not specified in the publication
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0065
Met-Pro-p-nitroanilide
in 40 mM HEPES, pH 8.0, and 100 mM NaCl, at 23°C
0.0633
Met-7-amido-4-methylcoumarin
-
pH 7.5, 30°C, in presence of 0.01 mM CoCl2
0.425
L-Met-L-Pro-4-nitroanilide
-
truncated mutant lacking N-terminal 89 amino acids, pH 7.5, 22°C
0.97
L-Met-PSI[C(O)S]Gly-L-Phe
-
N-terminally truncated mutant, lacking 66 amino acids, pH 7.0, 22°C
7.31
L-Met-PSI[C(O)S]Gly-L-Phe
-
N-terminally truncated mutant lacking 135 amino acids, pH 7.0, 22°C
16.61
L-Met-PSI[C(O)S]Gly-L-Phe
-
N-terminally truncated mutant, lacking 66 amino acids, pH 7.0, 22°C
0.0033
L-methionine 4-nitroanilide
mutant F309M, pH not specified in the publication, temperature not specified in the publication
0.0483
L-methionine 4-nitroanilide
wild-type, pH not specified in the publication, temperature not specified in the publication
additional information
additional information
-
turnover-numbers of truncated enzyme
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
10
L-methionine 4-nitroanilide
mutant F309M, pH not specified in the publication, temperature not specified in the publication
128
L-methionine 4-nitroanilide
wild-type, pH not specified in the publication, temperature not specified in the publication
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000001
3-(anilino)-5-(3-methyl-2-butenylthio)-1,2,4-triazole
in 50 mM HEPES (pH 7.5), with 100 mM NaCl
0.000015
3-(N-methyl-anilino)-5-benzylthio-1,2,4-triazole
in 50 mM HEPES (pH 7.5), with 100 mM NaCl
0.000066
3-anilino-5-(3-methyl-butylthio)-methylthio-1,2,4-triazole
in 50 mM HEPES (pH 7.5), with 100 mM NaCl
0.0000005
3-anilino-5-benzylthio-1,2,4-triazole
in 50 mM HEPES (pH 7.5), with 100 mM NaCl
0.01
3-anilino-5-benzylthio-1-methyl-1,2,4-triazole
IC50 above 0.01 mM, in 50 mM HEPES-Na+ (pH 7.5), with 100 mM NaCl
0.0013
3-anilino-5-benzylthio-2-methyl-1,2,4-triazole
in 50 mM HEPES (pH 7.5), with 100 mM NaCl
0.001
3-anilino-5-methylthio-1,2,4-triazole
in 50 mM HEPES (pH 7.5), with 100 mM NaCl
0.000003
3-[2-(isopropyl)-anilino]-5-(furan-2-ylmethylthio)-1,2,4-triazole
in 50 mM HEPES (pH 7.5), with 100 mM NaCl
0.000024
3-[2-(isopropyl)-anilino]-5-(furan-3-ylmethylthio)-1,2,4-triazole
in 50 mM HEPES (pH 7.5), with 100 mM NaCl
0.00000004
5-(benzylsulfanyl)-N-(2-methylphenyl)-4H-1,2,4-triazol-3-amine
apparent value
0.0000017
5-(benzylsulfanyl)-N-(3,4-dimethoxyphenyl)-4H-1,2,4-triazol-3-amine
apparent value
0.00000043
5-(benzylsulfanyl)-N-(4-chlorophenyl)-4H-1,2,4-triazol-3-amine
apparent value
0.00000005
5-(benzylsulfanyl)-N-(4-methoxyphenyl)-4H-1,2,4-triazol-3-amine
apparent value
0.00000007
5-(benzylsulfanyl)-N-(4-methylphenyl)-4H-1,2,4-triazol-3-amine
apparent value
0.00074
5-(benzylsulfanyl)-N-biphenyl-2-yl-4H-1,2,4-triazol-3-amine
apparent value
0.162
5-[(2E)-hepta-2,6-dien-4-yn-1-ylidene]pyrimidine-2,4,6(1H,3H,5H)-trione
-
0.00000015
5-[(3-methylbut-2-en-1-yl)sulfanyl]-N-(2-methylphenyl)-4H-1,2,4-triazol-3-amine
apparent value
0.0000033
5-[(cyclohexylmethyl)sulfanyl]-N-(2-methylphenyl)-4H-1,2,4-triazol-3-amine
apparent value
0.0000083
5-[(cyclohexylmethyl)sulfanyl]-N-(3,4-dimethoxyphenyl)-4H-1,2,4-triazol-3-amine
apparent value
0.0000031
5-[(cyclohexylmethyl)sulfanyl]-N-(4-methoxyphenyl)-4H-1,2,4-triazol-3-amine
apparent value
0.0001
5-[(cyclohexylmethyl)sulfanyl]-N-(4-methylphenyl)-4H-1,2,4-triazol-3-amine
apparent value
0.0000012
5-[[(2-methyl-2,5-dihydro-1,3-thiazol-4-yl)methyl]sulfanyl]-N-(4-methylphenyl)-4H-1,2,4-triazol-3-amine
apparent value
0.0000036
5-[[(5-methylisoxazol-3-yl)methyl]sulfanyl]-N-(2-methylphenyl)-4H-1,2,4-triazol-3-amine
apparent value
0.0000035 - 0.0000078
5-[[(5-methylisoxazol-3-yl)methyl]sulfanyl]-N-(4-methylphenyl)-4H-1,2,4-triazol-3-amine
0.00000023
5-[[2-(2-fluorophenyl)ethyl]sulfanyl]-N-(2-methylphenyl)-4H-1,2,4-triazol-3-amine
apparent value
0.00000013
5-[[2-(2-fluorophenyl)ethyl]sulfanyl]-N-(4-methoxyphenyl)-4H-1,2,4-triazol-3-amine
apparent value
0.00000065
5-[[2-(2-fluorophenyl)ethyl]sulfanyl]-N-(4-methylphenyl)-4H-1,2,4-triazol-3-amine
apparent value
0.000061
5-[[2-(2-methoxyphenyl)ethyl]sulfanyl]-N-(2-methylphenyl)-4H-1,2,4-triazol-3-amine
apparent value
0.01
5-[[2-(2-methoxyphenyl)ethyl]sulfanyl]-N-(4-methylphenyl)-4H-1,2,4-triazol-3-amine
Ki above 0.01 mM, apparent value
0.0000024
5-[[2-(3,4-difluorophenyl)ethyl]sulfanyl]-N-(2-methylphenyl)-4H-1,2,4-triazol-3-amine
apparent value
0.000004
5-[[2-(3,4-difluorophenyl)ethyl]sulfanyl]-N-(3,4-dimethoxyphenyl)-4H-1,2,4-triazol-3-amine
apparent value
0.0000021
5-[[2-(3,4-difluorophenyl)ethyl]sulfanyl]-N-(4-methoxyphenyl)-4H-1,2,4-triazol-3-amine
apparent value
0.0000033
5-[[2-(3,4-difluorophenyl)ethyl]sulfanyl]-N-(4-methylphenyl)-4H-1,2,4-triazol-3-amine
apparent value
0.0000005
methyl 4-([5-[(3-methylbut-2-en-1-yl)sulfanyl]-4H-1,2,4-triazol-3-yl]amino)benzoate
apparent value
0.0000027
methyl 4-([5-[(cyclohexylmethyl)sulfanyl]-4H-1,2,4-triazol-3-yl]amino)benzoate
apparent value
0.0000009
methyl 4-([5-[(pyridin-2-ylmethyl)sulfanyl]-4H-1,2,4-triazol-3-yl]amino)benzoate
apparent value
0.0000009
methyl 4-([5-[(pyridin-4-ylmethyl)sulfanyl]-4H-1,2,4-triazol-3-yl]amino)benzoate
apparent value
0.0000038
methyl 4-[(5-[[(2-methyl-1,3-thiazolidin-4-yl)methyl]sulfanyl]-4H-1,2,4-triazol-3-yl)amino]benzoate
apparent value
0.0000008
methyl 4-[(5-[[(5-methylisoxazol-3-yl)methyl]sulfanyl]-4H-1,2,4-triazol-3-yl)amino]benzoate
apparent value
0.00000041
methyl 4-[(5-[[2-(2-fluorophenyl)ethyl]sulfanyl]-4H-1,2,4-triazol-3-yl)amino]benzoate
apparent value
0.00001
methyl 4-[(5-[[2-(2-methoxyphenyl)ethyl]sulfanyl]-4H-1,2,4-triazol-3-yl)amino]benzoate
apparent value
0.000135
methyl 4-[(5-[[2-(2-methylphenyl)ethyl]sulfanyl]-4H-1,2,4-triazol-3-yl)amino]benzoate
apparent value
0.0000013
methyl 4-[(5-[[2-(3,4-difluorophenyl)ethyl]sulfanyl]-4H-1,2,4-triazol-3-yl)amino]benzoate
apparent value
0.0000007
methyl 4-[[5-(benzylsulfanyl)-4H-1,2,4-triazol-3-yl]amino]benzoate
apparent value
0.0000037
N-(2-methylphenyl)-5-[(pyridin-4-ylmethyl)sulfanyl]-4H-1,2,4-triazol-3-amine
apparent value
0.0000038
N-(2-methylphenyl)-5-[[(2-methyl-1,3-thiazolidin-4-yl)methyl]sulfanyl]-4H-1,2,4-triazol-3-amine
apparent value
0.0000025
N-(2-methylphenyl)-5-[[2-(2-methylphenyl)ethyl]sulfanyl]-4H-1,2,4-triazol-3-amine
apparent value
0.0000009
N-(3,4-dimethoxyphenyl)-5-[(3-methylbut-2-en-1-yl)sulfanyl]-4H-1,2,4-triazol-3-amine
apparent value
0.000024
N-(3,4-dimethoxyphenyl)-5-[(pyridin-2-ylmethyl)sulfanyl]-4H-1,2,4-triazol-3-amine
apparent value
0.0000096
N-(3,4-dimethoxyphenyl)-5-[(pyridin-4-ylmethyl)sulfanyl]-4H-1,2,4-triazol-3-amine
apparent value
0.000021
N-(3,4-dimethoxyphenyl)-5-[[(2-methyl-1,3-thiazolidin-4-yl)methyl]sulfanyl]-4H-1,2,4-triazol-3-amine
apparent value
0.000007
N-(3,4-dimethoxyphenyl)-5-[[(5-methylisoxazol-3-yl)methyl]sulfanyl]-4H-1,2,4-triazol-3-amine
apparent value
0.0000013
N-(3,4-dimethoxyphenyl)-5-[[2-(2-fluorophenyl)ethyl]sulfanyl]-4H-1,2,4-triazol-3-amine
apparent value
0.001
N-(3,4-dimethoxyphenyl)-5-[[2-(2-methoxyphenyl)ethyl]sulfanyl]-4H-1,2,4-triazol-3-amine
Ki above 0.001 mM, apparent value
0.000018
N-(3,4-dimethoxyphenyl)-5-[[2-(2-methylphenyl)ethyl]sulfanyl]-4H-1,2,4-triazol-3-amine
apparent value
0.00000052
N-(4-chlorophenyl)-5-[(3-methylbut-2-en-1-yl)sulfanyl]-4H-1,2,4-triazol-3-amine
apparent value
0.0000052
N-(4-chlorophenyl)-5-[(cyclohexylmethyl)sulfanyl]-4H-1,2,4-triazol-3-amine
apparent value
0.000004
N-(4-chlorophenyl)-5-[(pyridin-2-ylmethyl)sulfanyl]-4H-1,2,4-triazol-3-amine
apparent value
0.0000025
N-(4-chlorophenyl)-5-[(pyridin-4-ylmethyl)sulfanyl]-4H-1,2,4-triazol-3-amine
apparent value
0.0000048
N-(4-chlorophenyl)-5-[[(2-methyl-1,3-thiazolidin-4-yl)methyl]sulfanyl]-4H-1,2,4-triazol-3-amine
apparent value
0.0000018
N-(4-chlorophenyl)-5-[[(5-methylisoxazol-3-yl)methyl]sulfany]-4H-1,2,4-triazol-3-amine
apparent value
0.00000061
N-(4-chlorophenyl)-5-[[2-(2-fluorophenyl)ethyl]sulfanyl]-4H-1,2,4-triazol-3-amine
apparent value
0.01
N-(4-chlorophenyl)-5-[[2-(2-methoxyphenyl)ethyl]sulfanyl]-4H-1,2,4-triazol-3-amine
apparent value
0.000023
N-(4-chlorophenyl)-5-[[2-(2-methylphenyl)ethyl]sulfanyl]-4H-1,2,4-triazol-3-amine
apparent value
0.00000016
N-(4-methoxyphenyl)-5-[(3-methylbut-2-en-1-yl)sulfanyl]-4H-1,2,4-triazol-3-amine
apparent value
0.000018
N-(4-methoxyphenyl)-5-[(pyridin-2-ylmethyl)sulfanyl]-4H-1,2,4-triazol-3-amine
apparent value
0.0000061
N-(4-methoxyphenyl)-5-[(pyridin-4-ylmethyl)sulfanyl]-4H-1,2,4-triazol-3-amine
apparent value
0.0000016
N-(4-methoxyphenyl)-5-[[(5-methylisoxazol-3-yl)methyl]sulfanyl]-4H-1,2,4-triazol-3-amine
apparent value
0.000034
N-(4-methoxyphenyl)-5-[[2-(2-methoxyphenyl)ethyl]sulfanyl]-4H-1,2,4-triazol-3-amine
apparent value
0.0000078
N-(4-methylphenyl)-5-[(pyridin-2-ylmethyl)sulfanyl]-4H-1,2,4-triazol-3-amine
apparent value
0.0000057
N-(4-methylphenyl)-5-[(pyridin-4-ylmethyl)sulfanyl]-4H-1,2,4-triazol-3-amine
apparent value
0.0000052
N-(4-methylphenyl)-5-[(thiophen-2-ylmethyl)sulfanyl]-4H-1,2,4-triazol-3-amine
apparent value
0.0000078
N-(4-methylphenyl)-5-[[(2-methyl-1,3-thiazolidin-4-yl)methyl]sulfanyl]-4H-1,2,4-triazol-3-amine
apparent value
0.0000065
N-(4-methylphenyl)-5-[[2-(2-methylphenyl)ethyl]sulfanyl]-4H-1,2,4-triazol-3-amine
apparent value
0.0000091
N-(5-[[(2-methyl-1,3-thiazolidin-4-yl)methyl]sulfanyl]-4H-1,2,4-triazol-3-yl)pyridin-3-amine
apparent value
0.0000015
N-(5-[[(5-methylisoxazol-3-yl)methyl]sulfanyl]-4H-1,2,4-triazol-3-yl)pyridin-3-amine
apparent value
0.00035
N-biphenyl-2-yl-5-[(2-fluorobenzyl)sulfanyl]-4H-1,2,4-triazol-3-amine
apparent value
0.002
N-biphenyl-2-yl-5-[(2-methoxybenzyl)sulfanyl]-4H-1,2,4-triazol-3-amine
Ki above 0.002 mM, apparent value
0.002
N-biphenyl-2-yl-5-[(2-methylbenzyl)sulfanyl]-4H-1,2,4-triazol-3-amine
Ki above 0.002 mM, apparent value
0.002
N-biphenyl-2-yl-5-[(3,4-difluorobenzyl)sulfanyl]-4H-1,2,4-triazol-3-amine
Ki above 0.002 mM, apparent value
0.00048
N-biphenyl-2-yl-5-[(3-methylbut-2-en-1-yl)sulfanyl]-4H-1,2,4-triazol-3-amine
apparent value
0.00065
N-biphenyl-2-yl-5-[(cyclohexylmethyl)sulfanyl]-4H-1,2,4-triazol-3-amine
apparent value
0.002
N-biphenyl-2-yl-5-[(pyridin-4-ylmethyl)sulfanyl]-4H-1,2,4-triazol-3-amine
Ki above 0.002 mM, apparent value
0.0017
N-biphenyl-2-yl-5-[[(5-methylisoxazol-3-yl)methyl]sulfanyl]-4H-1,2,4-triazol-3-amine
apparent value
0.00000075
N-phenyl-5-[(thiophen-2-ylmethyl)sulfanyl]-4H-1,2,4-triazol-3-amine
apparent value
0.0000015
N-[4-(chloromethyl)phenyl]-5-[[2-(3,4-difluorophenyl)ethyl]sulfanyl]-4H-1,2,4-triazol-3-amine
apparent value
0.00000004
N-[5-(benzylsulfanyl)-4H-1,2,4-triazol-3-yl]pyridin-3-amine
apparent value
0.0000003
N-[5-[(2-fluorobenzyl)sulfanyl]-4H-1,2,4-triazol-3-yl]pyridin-3-amine
apparent value
0.0000017
N-[5-[(2-methylbenzyl)sulfanyl]-4H-1,2,4-triazol-3-yl]pyridin-3-amine
apparent value
0.0000005
N-[5-[(3,4-difluorobenzyl)sulfanyl]-4H-1,2,4-triazol-3-yl]pyridin-3-amine
apparent value
0.000003
N-[5-[(cyclohexylmethyl)sulfanyl]-4H-1,2,4-triazol-3-yl]pyridin-3-amine
apparent value
0.0000057
N-[5-[(pyridin-2-ylmethyl)sulfanyl]-4H-1,2,4-triazol-3-yl]pyridin-3-amine
apparent value
0.000000245
[(1R)-1-carbamoyl-2-methyl-propyl]-carbamic acid-(3R,4S,5S,6R)-5-methoxy-4-[(2R,3R)-2-methyl-3-(3-methylbut-2-enyl)oxiranyl]-1-oxaspiro(2,5)oct-6-yl ester
-
recombinant MetAP-2, in 50 mM Hepes, 100 mM MnCl2, 100 mM NaCl, 0.005% (w/v) bovine serum albumin, 0.006% (w/v) 3-[(3-cholamidopropyl)dimethylammonio]propanesulphonic acid, at pH 7.5
0.5
[amino(cyclohexyl)methyl]phosphonic acid
IC50 value above 0.5 mM, pH not specified in the publication, temperature not specified in the publication
0.0000035
5-[[(5-methylisoxazol-3-yl)methyl]sulfanyl]-N-(4-methylphenyl)-4H-1,2,4-triazol-3-amine
apparent value
0.0000078
5-[[(5-methylisoxazol-3-yl)methyl]sulfanyl]-N-(4-methylphenyl)-4H-1,2,4-triazol-3-amine
apparent value
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0000006
(3R,4S,5S,6R)-5-methoxy-4-((2R,3R)-2-methyl-3-(3-methylbut-2-enyl)oxiran-2-yl)-1-oxaspiro[2.5]octan-6-yl (2R)-3-methyl-1-(2-(1-methylpyrrolidin-2-yl)ethylamino)-1-oxobutan-2-ylcarbamate
Homo sapiens
-
above, in HUVEC
0.000000095
(3R,4S,5S,6R)-5-methoxy-4-((2R,3R)-2-methyl-3-(3-methylbut-2-enyl)oxiran-2-yl)-1-oxaspiro[2.5]octan-6-yl (R)-1-amino-3-methyl-1-oxobutan-2-ylcarbamate
Homo sapiens
-
in HUVEC
0.0000017
(3R,4S,5S,6R)-5-methoxy-4-((2R,3R)-2-methyl-3-(3-methylbut-2-enyl)oxiran-2-yl)-1-oxaspiro[2.5]octan-6-yl (R)-3-methyl-1-(morpholinoamino)-1-oxobutan-2-ylcarbamate
Homo sapiens
-
in HUVEC
0.0000006
(3R,4S,5S,6R)-5-methoxy-4-((2R,3R)-2-methyl-3-(3-methylbut-2-enyl)oxiran-2-yl)-1-oxaspiro[2.5]octan-6-yl (R)-3-methyl-1-oxo-1-(2-(pyrrolidin-1-yl)ethylamino)butan-2-ylcarbamate
Homo sapiens
-
in HUVEC
0.0000017
(3R,4S,5S,6R)-5-methoxy-4-((2R,3R)-2-methyl-3-(3-methylbut-2-enyl)oxiran-2-yl)-1-oxaspiro[2.5]octan-6-yl 1-amino-2-methyl-1-oxopropan-2-ylcarbamate
Homo sapiens
-
in HUVEC
0.0000007
(3R,4S,5S,6R)-5-methoxy-4-((2R,3R)-2-methyl-3-(3-methylbut-2-enyl)oxiran-2-yl)-1-oxaspiro[2.5]octan-6-yl 1-carbamoylcyclopentylcarbamate
Homo sapiens
-
in HUVEC
0.0000002
(3R,4S,5S,6R)-5-methoxy-4-((2R,3R)-2-methyl-3-(3-methylbut-2-enyl)oxiran-2-yl)-1-oxaspiro[2.5]octan-6-yl 2-(1-methylpyrrolidin-2-yl)ethylcarbamate
Homo sapiens
-
above, in HUVEC
0.0000001
(3R,4S,5S,6R)-5-methoxy-4-((2R,3R)-2-methyl-3-(3-methylbut-2-enyl)oxiran-2-yl)-1-oxaspiro[2.5]octan-6-yl 2-(pyrrolidin-1-yl)ethylcarbamate
Homo sapiens
-
in HUVEC
0.00000006
(3R,4S,5S,6R)-5-methoxy-4-((2R,3R)-2-methyl-3-(3-methylbut-2-enyl)oxiran-2-yl)-1-oxaspiro[2.5]octan-6-yl isopropylcarbamate
Homo sapiens
-
in HUVEC
0.0000007
(3R,4S,5S,6R)-5-methoxy-4-((2R,3R)-2-methyl-3-(3-methylbut-2-enyl)oxiran-2-yl)-1-oxaspiro[2.5]octan-6-yl morpholinocarbamate
Homo sapiens
-
in HUVEC
0.0000011
(3R,4S,5S,6R)-5-methoxy-4-((2R,3R)-2-methyl-3-(3-methylbut-2-enyl)oxiran-2-yl)-1-oxaspiro[2.5]octan-6-yl tert-butylcarbamate
Homo sapiens
-
in HUVEC
0.00000025
(3R,5S,6R)-5-methoxy-4-[(3R)-2-methyl-3-(3-methylbut-2-en-1-yl)oxiran-2-yl]-1-oxaspiro[2.5]oct-6-yl (chloroacetyl)carbamate
Homo sapiens
-
in HUVEC
0.000027
(8S)-2-[[(4-fluorophenyl)sulfonyl]amino]-8-methyl-5,6,7,8-tetrahydronaphthalene-1-carboxylic acid
Homo sapiens
-
0.000000036
(R)-methyl 2-(((3R,4S,5S,6R)-5-methoxy-4-((2R,3R)-2-methyl-3-(3-methylbut-2-enyl)oxiran-2-yl)-1-oxaspiro[2.5]octan-6-yloxy)carbonylamino)-2-phenylacetate
Homo sapiens
-
in HUVEC
0.00000004
(R)-methyl 2-(((3R,4S,5S,6R)-5-methoxy-4-((2R,3R)-2-methyl-3-(3-methylbut-2-enyl)oxiran-2-yl)-1-oxaspiro[2.5]octan-6-yloxy)carbonylamino)-3-methylbutanoate
Homo sapiens
-
in HUVEC
0.000000038
(R)-methyl 2-(((3R,4S,5S,6R)-5-methoxy-4-((2R,3R)-2-methyl-3-(3-methylbut-2-enyl)oxiran-2-yl)-1-oxaspiro[2.5]octan-6-yloxy)carbonylamino)-4-methylpentanoate
Homo sapiens
-
in HUVEC
0.000000018
(S)-methyl 2-(((3R,4S,5S,6R)-5-methoxy-4-((2R,3R)-2-methyl-3-(3-methylbut-2-enyl)oxiran-2-yl)-1-oxaspiro[2.5]octan-6-yloxy)-carbonylamino)-3-methylbutanoate
Homo sapiens
-
in HUVEC
0.0000013
1-(((3R,4S,5S,6R)-5-methoxy-4-((2R,3R)-2-methyl-3-(3-methylbut-2-enyl)oxiran-2-yl)-1-oxaspiro[2.5]octan-6-yloxy)carbonyl)-piperidine-4-carboxylic acid
Homo sapiens
-
in HUVEC
0.0011 - 0.0081
1-(5-chloro-6-methyl-2-pyridin-2-ylpyrimidin-4-yl)-4-(2,4-dichlorobenzyl)-1,4-diazepane
0.0398
2-(1,3-thiazol-2-yl)-1H-imidazo[4,5-b]pyridine
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0101
2-(1,3-thiazol-4-yl)-1H-benzimidazol-5-amine
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.019
2-(1,3-thiazol-4-yl)-1H-imidazo[4,5-c]pyridine
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0001
2-(2-(((3R,4S,5S,6R)-5-methoxy-4-((2R,3R)-2-methyl-3-(3-methylbut-2-enyl)oxiran-2-yl)-1-oxaspiro[2.5]octan-6-yloxy)-carbonylamino)ethyl)-1,1-dimethylpyrrolidinium iodide
Homo sapiens
-
in HUVEC
0.0329
2-(pyrazin-2-yl)-1H-benzimidazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0093
2-(pyridin-2-yl)-1H-benzimidazol-5-amine
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0039
2-[(2,1,3-benzothiadiazol-4-ylsulfonyl)amino]-5-bromobenzoic acid
Homo sapiens
-
0.00001
2-[[(4-fluorophenyl)sulfonyl]amino]-5,6,7,8-tetrahydronaphthalene-1-carboxylic acid
Homo sapiens
-
0.00002
2-[[(4-fluorophenyl)sulfonyl]amino]-8-methyl-5,6-dihydronaphthalene-1-carboxylic acid
Homo sapiens
-
0.0001
3-(((3R,4S,5S,6R)-5-methoxy-4-((2R,3R)-2-methyl-3-(3-methylbut-2-enyl)oxiran-2-yl)-1-oxaspiro[2.5]octan-6-yloxy)carbonylamino)-N,N,N-trimethylpropan-1-aminium iodide
Homo sapiens
-
in HUVEC
0.000015
3-((R)-2-(((3R,4S,5S,6R)-5-methoxy-4-((2R,3R)-2-methyl-3-(3-methylbut-2-enyl)oxiran-2-yl)-1-oxaspiro[2.5]octan-6-yloxy)-carbonylamino)-3-methylbutanamido)benzoic acid
Homo sapiens
-
in HUVEC
0.01178
3-(2,3-dihydro-1,4-benzodioxin-6-yl)-5-{[(2-nitrophenyl)methyl]sulfanyl}-4-phenyl-4H-1,2,4-triazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00093
3-(2,3-dihydrobenzo[b][1,4]dioxin-6-yl)-5-(2-fluorobenzylthio)-4-phenyl-4H-1,2,4-triazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.01766
3-(2,3-dihydrobenzo[b][1,4]dioxin-6-yl)-5-(2-methylbenzylthio)-4-phenyl-4H-1,2,4-triazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.03071
3-(2,3-dihydrobenzo[b][1,4]dioxin-6-yl)-5-(3-methoxybenzylthio)-4-phenyl-4H-1,2,4-triazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00224
3-(2,3-dihydrobenzo[b][1,4]dioxin-6-yl)-5-(4-fluorobenzylthio)-4-phenyl-4H-1,2,4-triazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.01239
3-(2,3-dihydrobenzo[b][1,4]dioxin-6-yl)-5-(4-nitrobenzylthio)-4-phenyl-4H-1,2,4-triazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00395
3-(2,4-difluorobenzylthio)-5-(2,3-dihydrobenzo[b][1,4]dioxin-6-yl)-4-phenyl-4H-1,2,4-triazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0048
3-(2,6-difluorobenzylthio)-5-(2,3-dihydrobenzo[b][1,4]dioxin-6-yl)-4-phenyl-4H-1,2,4-triazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00537
3-(2-bromobenzylthio)-5-(2,3-dihydrobenzo[b][1,4]dioxin-6-yl)-4-phenyl-4H-1,2,4-triazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00184
3-(2-chlorobenzylthio)-5-(2,3-dihydrobenzo[b][1,4]dioxin-6-yl)-4-phenyl-4H-1,2,4-triazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00591
3-(3-bromobenzylthio)-5-(2,3-dihydrobenzo[b][1,4]dioxin-6-yl)-4-phenyl-4H-1,2,4-triazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00192
3-(3-chlorobenzylthio)-5-(2,3-dihydrobenzo[b][1,4]dioxin-6-yl)-4-phenyl-4H-1,2,4-triazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00729
3-(4-bromobenzylthio)-5-(2,3-dihydrobenzo[b][1,4]dioxin-6-yl)-4-phenyl-4H-1,2,4-triazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00345
3-(4-chlorobenzylthio)-5-(2,3-dihydrobenzo[b][1,4]dioxin-6-yl)-4-phenyl-4H-1,2,4-triazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00601
3-(benzylthio)-5-(2,3-dihydrobenzo[b][1,4]dioxin-6-yl)-4-phenyl-4H-1,2,4-triazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000009
3-[(phenylsulfonyl)amino]-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
Homo sapiens
-
0.000015
3-[[(4-fluorophenyl)sulfonyl]amino]naphthalene-2-carboxylic acid
Homo sapiens
-
0.0000007
4-((((3R,4S,5S,6R)-5-methoxy-4-((2R,3R)-2-methyl-3-(3-methylbut-2-enyl)oxiran-2-yl)-1-oxaspiro[2.5]octan-6-yloxy)carbonylamino)methyl)benzoic acid
Homo sapiens
-
in HUVEC
0.0388
5,6-dimethyl-2-(1,3-thiazol-4-yl)-1H-benzimidazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000038
5-((R)-1-[1,2,4]triazolo[1,5-a]pyrimidin-7-yl-pyrrolidin-2-ylmethoxy)-isoquinoline
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
0.0002
5-chloro-2-(5-chloropyridin-2-yl)-6-methyl-N-((R)-2-phenyl-2-(4-phenylbutylamino)ethyl)pyrimidin-4-amine
Homo sapiens
22°C, pH not specified in the publication
0.000063
5-chloro-2-(5-chloropyridin-2-yl)-N-(2,4-diphenylbutyl)-6-methylpyrimidin-4-amine
Homo sapiens
22°C, pH not specified in the publication
0.0132
5-methoxy-6-[2-methyl-3-(3-methylbut-2-en-1-yl)oxiran-2-yl]-4-oxobicyclo[3.1.0]hexane-1-carbaldehyde
Homo sapiens
-
0.0485
5-nitro-2-(1,3-thiazol-4-yl)-1H-benzimidazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0288
5-nitro-2-(pyridin-2-yl)-1H-benzimidazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0441
5-tert-butyl-2-(pyridin-2-yl)-1H-benzimidazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0575
6-(1,5-dimethylhex-4-en-1-yl)-5-(hydroxymethyl)-1-methoxybicyclo[3.1.0]hexan-2-one
Homo sapiens
-
0.0338
6-[(1E)-1,5-dimethylhexa-1,4-dien-1-yl]-5-(hydroxymethyl)-1-methoxybicyclo[3.1.0]hexan-2-one
Homo sapiens
-
0.000031
A-310840
Homo sapiens
-
IC50: 0.000031 mM for enzyme with Zn2+, 0.000043 mM for enzyme with Ni2+, 0.000069 mM for enzyme with Co2+, 0.000026 for enzyme with Fe2+, 0.0578 mM for enzyme with Mn2+
0.000121
A-311263
Homo sapiens
-
IC50: 0.000121 mM for enzyme with Zn2+, 0.000107 mM for enzyme with Ni2+, 0.000149 mM for enzyme with Co2+, 0.00011 mM for enzyme with Fe2+, 0.000055 mM for enzyme with Mn2+
0.000093
N-((R)-2-(5-chloro-2-(5-chloropyridin-2-yl)-6-methylpyrimidin-4-ylamino)-1-phenylethyl)-3-phenylpropanamide
Homo sapiens
22°C, pH not specified in the publication
0.0029
N-(4,5-dihydro-1,3-thiazol-2-yl)-3-[(2,2-dimethylpropanoyl)amino]pyridine-2-carboxamide
Homo sapiens
MetAP1
0.0035
N-(4,5-dihydro-1,3-thiazol-2-yl)-3-[(3-phenylpropanoyl)amino]pyridine-2-carboxamide
Homo sapiens
MetAP1
0.0064
N-(4,5-dihydro-1,3-thiazol-2-yl)-3-[[(1E)-2-methylpropylidene]amino]pyridine-2-carboxamide
Homo sapiens
MetAP1
0.041
phenyl[2-(1,3-thiazol-4-yl)-1H-benzimidazol-5-yl]methanone
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0015
tert-butyl [2-(4,5-dihydro-1,3-thiazol-2-ylcarbamoyl)pyridin-3-yl]carbamate
Homo sapiens
MetAP1
0.0011
1-(5-chloro-6-methyl-2-pyridin-2-ylpyrimidin-4-yl)-4-(2,4-dichlorobenzyl)-1,4-diazepane
Homo sapiens
MetAP1
0.0081
1-(5-chloro-6-methyl-2-pyridin-2-ylpyrimidin-4-yl)-4-(2,4-dichlorobenzyl)-1,4-diazepane
Homo sapiens
MetAP2
0.0243
1-methyl-2-(1,3-thiazol-4-yl)-1H-benzimidazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0324
1-methyl-2-(1,3-thiazol-4-yl)-1H-benzimidazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0133
2-(pyridin-2-yl)-1H-benzimidazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0284
2-(pyridin-2-yl)-1H-benzimidazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0329
2-(pyridin-2-yl)-1H-benzimidazole-5-carbonitrile
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0373
2-(pyridin-2-yl)-1H-benzimidazole-5-carbonitrile
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0401
2-(pyridin-2-yl)-1H-imidazo[4,5-b]pyrazine
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0484
2-(pyridin-2-yl)-1H-imidazo[4,5-b]pyrazine
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0267
2-(pyridin-2-yl)-1H-imidazo[4,5-b]pyridine
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0276
2-(pyridin-2-yl)-1H-imidazo[4,5-b]pyridine
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.008
2-(pyridin-2-yl)-1H-imidazo[4,5-c]pyridine
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0103
2-(pyridin-2-yl)-1H-imidazo[4,5-c]pyridine
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0284
5,6-dimethyl-2-(pyridin-2-yl)-1H-benzimidazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0326
5,6-dimethyl-2-(pyridin-2-yl)-1H-benzimidazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.028
5-chloro-2-(1,3-thiazol-4-yl)-1H-benzimidazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.047
5-chloro-2-(1,3-thiazol-4-yl)-1H-benzimidazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0181
5-chloro-2-(pyridin-2-yl)-1H-benzimidazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0488
5-chloro-2-(pyridin-2-yl)-1H-benzimidazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0004
5-chloro-4-methyl-2-pyridin-2-yl-6-pyrrolidin-1-ylpyrimidine
Homo sapiens
MetAP1
0.0008
5-chloro-4-methyl-2-pyridin-2-yl-6-pyrrolidin-1-ylpyrimidine
Homo sapiens
MetAP2
0.0006
5-chloro-6-methyl-N-(2-phenylethyl)-2-pyridin-2-ylpyrimidin-4-amine
Homo sapiens
MetAP1
0.0076
5-chloro-6-methyl-N-(2-phenylethyl)-2-pyridin-2-ylpyrimidin-4-amine
Homo sapiens
MetAP2
0.0033
5-chloro-N,6-dimethyl-N-(2-phenylethyl)-2-pyridin-2-ylpyrimidin-4-amine
Homo sapiens
MetAP1
0.0033
5-chloro-N,6-dimethyl-N-(2-phenylethyl)-2-pyridin-2-ylpyrimidin-4-amine
Homo sapiens
MetAP2
0.0384
5-fluoro-2-(1,3-thiazol-4-yl)-1H-benzimidazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0458
5-fluoro-2-(1,3-thiazol-4-yl)-1H-benzimidazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0149
5-fluoro-2-(pyridin-2-yl)-1H-benzimidazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0347
5-fluoro-2-(pyridin-2-yl)-1H-benzimidazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0355
5-methyl-2-(1,3-thiazol-4-yl)-1H-benzimidazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0406
5-methyl-2-(1,3-thiazol-4-yl)-1H-benzimidazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0077
5-methyl-2-(pyridin-2-yl)-1H-benzimidazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0326
5-methyl-2-(pyridin-2-yl)-1H-benzimidazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0339
8-(pyridin-2-yl)-7H-purine
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0364
8-(pyridin-2-yl)-7H-purine
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0056
8-hydroxy quinoline
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0215
8-hydroxy quinoline
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0081
N-(1,3-thiazol-2-yl)pyridine-2-carboxamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0258
N-(1,3-thiazol-2-yl)pyridine-2-carboxamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0398
N-(quinolin-8-yl)benzenesulfonamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0449
N-(quinolin-8-yl)benzenesulfonamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0412
quinolin-8-yl benzenesulfonate
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0417
quinolin-8-yl benzenesulfonate
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0348
quinolin-8-yl benzoate
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0428
quinolin-8-yl benzoate
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0447
thiabendazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0478
thiabendazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00105
TNP-470
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
1.3
-
substrate L-Nle-L-Ala-L-Ser, N-terminally truncated mutant lacking 135 amino acids, pH 7.0, 22°C
100
-
substrate L-Met-L-Ala-L-Ser, N-terminally truncated mutant, lacking 66 amino acids, pH 7.0, 22°C
12.1
-
substrate L-Thr-PSI[C(O)S]Gly-L-Phe, N-terminally truncated mutant, lacking 66 amino acids, pH 7.0, 22°C
141
-
substrate L-Nle-L-Ala-L-Ser, N-terminally truncated mutant, lacking 66 amino acids, pH 7.0, 22°C
146
-
substrate L-Met-PSI[C(O)S]Gly-L-Phe, N-terminally truncated mutant, lacking 66 amino acids, pH 7.0, 22°C
18.4
-
substrate L-Met-PSI[C(O)S]Gly-L-Phe, N-terminally truncated mutant lacking 135 amino acids, pH 7.0, 22°C
201
-
substrate L-Met-L-Ala-L-Ser-L-Trp, N-terminally truncated mutant, lacking 66 amino acids, pH 7.0, 22°C
22
-
substrate L-Phe-L-Ala-L-Ser-L-Trp, N-terminally truncated mutant, lacking 66 amino acids, pH 7.0, 22°C
23
-
substrate L-Leu-L-Ala-L-Ser-L-Trp, N-terminally truncated mutant, lacking 66 amino acids, pH 7.0, 22°C
30
8.8
-
substrate L-Thr-PSI[C(O)S]Gly-L-Phe, N-terminally truncated mutant lacking 135 amino acids, pH 7.0, 22°C
9.4
-
substrate L-Ala-PSI[C(O)S]Gly-L-Phe, N-terminally truncated mutant lacking 135 amino acids, pH 7.0, 22°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
colon cancer cell line, expression of enzyme is inversely correlated to cell density
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
-
MetAP2 is a bifunctional protein that plays a critical role in the regulation of post-translational processing and protein synthesis
physiological function
inhibition of the enzymatic activity of isoform MetAP2 inhibitor fumagillin or siRNA mediated down-regulation of the protein level of MetAP2 both lead to strong signals of unprocessed 14-3-3gamma protein with intact initiator methionine in the immunoblot
physiological function
N-terminally acetylated terminal Met residues followed by a small residue cannot be removed by MetAPs. Yeast Naa50-mediated N-terminal acetylation may act to retain the N-terminal Met residue of proteins otherwise susceptible to MetAP
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). MAP12_HUMAN
335
0
37088
Swiss-Prot
Mitochondrion (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
two-cobalt-dependent MetAP families, presently composed of the prokaryote and yeast sequence (and represented by the Escherichia coli structure) (type I), and by human MetAP, the yeast open reading frame, and the partial prokaryotic sequence (type II)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
N-terminal region contains 3 distinct PxxP motifs that may participate in binding to the ribosome
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
isoform MetAP2 is post-translationally regulated by an allosteric disulfide bond, which controls substrate specificity and catalytic efficiency. Isoform MetAP2 contains a single Cys228-Cys448 disulfide bond that has an -RH-staple configuration and links two beta-loop structures, which are hallmarks of allosteric disulfide bonds. The disulfide bond exists in oxidized and reduced states in the recombinant enzyme. The disulfide has a standard redox potential of -261 mV and is efficiently reduced by the protein reductant, thioredoxin, with a rate constant of 16180 per M and s. The MetAP2 disulfide bond also exists in oxidized and reduced states in glioblastoma tumor cells, and stressing the cells by oxygen or glucose deprivation results in more oxidized enzyme. Oxidized and reduced isoforms have different catalytic efficiencies for hydrolysis of MetAP2 peptide substrates
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
1.8 resolution crystal structure of free enzyme and enzyme complexed with fumagillin. Crystals are grown in 1 to 2 weeks at 4°C from sitting drops, with a protein concentration of 12 mg/ml
complexed with inhibitor, sitting drop vapour diffusion method with 15-20% tert-butyl alcohol containing 0.4-0.1 M aqueous sodium citrate at pH 5.5
crystal structure of N-terminally truncated MetAP1 in complex with inhibitor 4-[4-(4-methoxyphenyl)piperazin-1-yl]-2-(pyridin-2-yl)quinazoline and Co(II)
in complex with inhibitor 5-((R)-1-[1,2,4]triazolo[1,5-a]pyrimidin-7-yl-pyrrolidin-2-ylmethoxy)-isoquinoline. The His339 side-chain imidazole ring is coplanar sandwiched between the imidazole of His331 and the aryl-ether moiety of the inhibitor
MetAP1 in complex with ovalicin, hanging drop vapour diffusion method, with 4%-6% PEG 10000 or 12%-16% PEG monomethyl ether 2000, in 100 mM HEPES at pH 5.4-6.2
N-terminally truncated isoform AP1 in complex with inhibitor 5-chloro-2-(5-chloropyridin-2-yl)-6-methyl-N-((R)-2-phenyl-2-(4-phenylbutylamino)ethyl)pyrimidin-4-amine. Both pyridine nitrogen N1 and pyrimidine nitrogen N1 are bound to Co3, displaying a near-perfect octahedral coordination which is completed by the nitrogen atom from the side chain of His212 and three water molecules
sitting drop vapour diffusion method, in complex with L-methionine and D-methionine at 1.9 and 2.0 A resolution, respectively
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A362T
-
type II enzyme, mutation results in resistance to ovalicin, TNP-470 and fumagillin when expressed in yeast
C202A
-
hydrolysis of Met-PSI[C(O)S]Gly-Phe similar to wild-type, relaxed specificity
H382Y
T334A
-
type I enzyme, mutation renders the resistant wild-type enzyme sensitive to ovalicin
Y444C
additional information
H382Y
-
type II enzyme, mutation results in resistance to ovalicin, TNP-470 and fumagillin when expressed in yeast
H382Y
-
the single site mutation in the S1 subsite of human MetAP2b results in inhibitor resistance
Y444C
-
type II enzyme, mutation results in resistance to TNP-470, but not to fumagillin when expressed in yeast
Y444C
-
the single site mutation in the S1 subsite of human MetAP2b results in inhibitor resistance
additional information
-
the 107 N-terminal residues of MetAP2 are not required for either the peptidolytic activity of the enzyme or its stability. The N-terminally truncated enzyme and the full-length enzyme yield essentially identical kinetic behavior and physical properties
additional information
-
truncated MetAP1 lacking N-terminal 89 amino acids, 2.5fold increase in KM-value
additional information
-
truncated mutant lacking N-terminal 66 amino acids, 2.5fold increase in kcat value. Truncated mutant lacking N-terminal 135 amino acids, 4fold increase in KM-value
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
recombinant full-lenth enzyme is not stable during purification and storage at 4°C, and a smaller but active protein appears that corresponds to N-terminally truncated protein lacking amino acids 1-66
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
adenoviral transfer of c-Myc increaseds the expression of MetAP2 in human umbilical vein endothelial cells and reveals that cellular proliferation may involve a cross-talk between c-Myc and MetAP2
-
expressed in Escherichia coli
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the 3,5-bis(benzylidene)-4-piperidone derivative 2-(3-[3,5-bis[4-nitrobenzylidene]-4-oxopiperidin-1-yl]-3-oxopropylsulfanyl) ethanesulfonic acid, or NC2213, downregulates the enzyme in HT-29 cells
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
medicine
-
MetAP2 is a molecular target for antiangiogenesis and anticancer therapy
medicine
-
enzyme expression is increased in 8 out of 12 tumor samples. Reduction of enzyme level by MAP1D shRNa does not result in any difference of proliferation, cell survival, or cell numbers, but cells exhibit a dramatically reduced potential to form colonies in soft agar
medicine
-
enzyme inhibitor PPI-2458 inhibits proliferation of human fibroblast-like synviocytes derived from patients with rheumatoid arthritis with a growth inhibitory concentration of 0.04 nM. Growth inhibition is linked to enzyme inhibition
medicine
-
enzyme MetAP2 activity is elevated in all human colorectal adenocarcinomas examined compared with normal tissue. Immunohistochemistry shows moderate to strong cytoplasmic positivity for enzyme with increased intensity in the invasive tumor component
medicine
-
in colon cancer cell line HT-29, expression of enzyme is inversely correlated to cell density
medicine
-
inhibitor A357300 in combination with cyclophosphamide sustains tumor regression and inhibits establishment and growth rate of hematogenous metastatic deposits following tail vein inocculation in CHP-134 neuroblastoma cells
medicine
inhibitor PPI-2458 potently inhibits growth of several non-Hodgkin's lymphoma cell lines in a manner correlating with enzyme inhibition
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Arfin, S.M.; Kendall, R.L.; Hall, L.; Weaver, L.H.; Stewart, A.E.; Matthews, B.W.; Bradshaw, R.A.
Eukaryotic methionyl aminopeptidases: two classes of cobalt-dependent enzymes
Proc. Natl. Acad. Sci. USA
92
7714-7718
1995
Escherichia coli, Homo sapiens, Sus scrofa
Yang, G.; Kirkpatrick, R.B.; Ho, T.; Zhang, G.F.; Liang, P.H.; Johanson, K.O.; Casper, D.J.; Doyle, M.L.; Marino, J.P., Jr.; Thompson, S.K.; Chen, W.; Tew, D.G.; Meek, T.D.
Steady-State Kinetic Characterization of Substrates and Metal-Ion Specificities of the Full-Length and N-Terminally Truncated Recombinant Human Methionine Aminopeptidases (Type 2)
Biochemistry
40
10645-10654
2001
Homo sapiens
Son, K.H.; Kwon, J.Y.; Jeong, H.W.; Kim, H.K.; Kim, C.J.; Chang, Y.H.; Choi, J.D.; Kwon, B.M.
5-demethylovalicin, as a methionine aminopeptidase-2 inhibitor produced by Chrysosporium
Bioorg. Med. Chem.
10
185-188
2002
Homo sapiens
Liu, S.; Widom, J.; Kemp, C.W.; Crews, C.M.; Clardy, J.
Structure of human methionine aminopeptidase-2 complexed with fumagillin
Science
282
1324-1327
1998
Homo sapiens (P50579), Homo sapiens
Wang, J.; Sheppard, G.S.; Lou, P.; Kawai, M.; Park, C.; Egan, D.A.; Schneider, A.; Bouska, J.; Lesniewski, R.; Henkin, J.
Physiologically relevant metal cofactor for methionine aminopeptidase-2 is manganese
Biochemistry
42
5035-5042
2003
Homo sapiens
Selvakumar, P.; Lakshmikuttyamma, A.; Lawman, Z.; Bonham, K.; Dimmock, J.R.; Sharma, R.K.
Expression of methionine aminopeptidase 2,N-myristoyltransferase, and N-myristoyltransferase inhibitor protein 71 in HT29
Biochem. Biophys. Res. Commun.
322
1012-1017
2004
Homo sapiens
Li, J.Y.; Chen, L.L.; Cui, Y.M.; Luo, Q.L.; Gu, M.; Nan, F.J.; Ye, Q.Z.
Characterization of full length and truncated type I human methionine aminopeptidases expressed from Escherichia coli
Biochemistry
43
7892-7898
2004
Homo sapiens
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
Biochemistry
44
14741-14749
2005
Homo sapiens
Selvakumar, P.; Lakshmikuttyamma, A.; Kanthan, R.; Kanthan, S.C.; Dimmock, J.R.; Sharma, R.K.
High expression of methionine aminopeptidase 2 in human colorectal adenocarcinomas
Clin. Cancer Res.
10
2771-2775
2004
Homo sapiens
Morowitz, M.J.; Barr, R.; Wang, Q.; King, R.; Rhodin, N.; Pawel, B.; Zhao, H.; Erickson, S.A.; Sheppard, G.S.; Wang, J.; Maris, J.M.; Shusterman, S.
Methionine aminopeptidase 2 inhibition is an effective treatment strategy for neuroblastoma in preclinical models
Clin. Cancer Res.
11
2680-2685
2005
Homo sapiens
Cooper, A.C.; Karp, R.M.; Clark, E.J.; Taghizadeh, N.R.; Hoyt, J.G.; Labenski, M.T.; Murray, M.J.; Hannig, G.; Westlin, W.F.; Thompson, C.D.
A novel methionine aminopeptidase-2 inhibitor, PPI-2458, inhibits non-Hodgkin's lymphoma cell proliferation in vitro and in vivo
Clin. Cancer Res.
12
2583-2590
2006
Homo sapiens, Homo sapiens (P50579)
Li, J.Y.; Cui, Y.M.; Chen, L.L.; Gu, M.; Li, J.; Nan, F.J.; Ye, Q.Z.
Mutations at the S1 sites of methionine aminopeptidases from Escherichia coli and Homo sapiens reveal the residues critical for substrate specificity
J. Biol. Chem.
279
21128-21134
2004
Homo sapiens, Escherichia coli (P0AE18), Escherichia coli
Brdlik, C.M.; Crews, C.M.
A single amino acid residue defines the difference in ovalicin sensitivity between type I and II methionine aminopeptidases
J. Biol. Chem.
279
9475-9480
2004
Homo sapiens
Kallander, L.S.; Lu, Q.; Chen, W.; Tomaszek, T.; Yang, G.; Tew, D.; Meek, T.D.; Hofmann, G.A.; Schulz-Pritchard, C.K.; Smith, W.W.; Janson, C.A.; Ryan, M.D.; Zhang, G.F.; Johanson, K.O.; Kirkpatrick, R.B.; Ho, T.F.; Fisher, P.W.; Mattern, M.R.; Johnson, R.K.; Hansbury, M.J.; Winkler, J.D.; Ward, K.W.; Veber, D.F.; Thompson, S.K.
4-Aryl-1,2,3-triazole: a novel template for a reversible methionine aminopeptidase 2 inhibitor, optimized to inhibit angiogenesis in vivo
J. Med. Chem.
48
5644-5647
2005
Homo sapiens
Sheppard, G.S.; Wang, J.; Kawai, M.; Fidanze, S.D.; Bamaung, N.Y.; Erickson, S.A.; Barnes, D.M.; Tedrow, J.S.; Kolaczkowski, L.; Vasudevan, A.; Park, D.C.; Wang, G.T.; Sanders, W.J.; Mantei, R.A.; Palazzo, F.; Tucker-Garcia, L.; Lou, P.; Zhang, Q.; Park, C.H.; Kim, K.H.; Petros, A.; Olejniczak, E.; Nettesheim, D.; Hajduk, P.; Henkin, J.; Lesniewski, R.; Davidsen, S.K.; Bell, R.L.
Discovery and optimization of anthranilic acid sulfonamides as inhibitors of methionine aminopeptidase-2: a structural basis for the reduction of albumin binding
J. Med. Chem.
49
3832-3849
2006
Homo sapiens (P50579), Homo sapiens
Leszczyniecka, M.; Bhatia, U.; Cueto, M.; Nirmala, N.R.; Towbin, H.; Vattay, A.; Wang, B.; Zabludoff, S.; Phillips, P.E.
MAP1D, a novel methionine aminopeptidase family member is overexpressed in colon cancer
Oncogene
25
3471-3478
2006
Homo sapiens
Bernier, S.G.; Lazarus, D.D.; Clark, E.; Doyle, B.; Labenski, M.T.; Thompson, C.D.; Westlin, W.F.; Hannig, G.
A methionine aminopeptidase-2 inhibitor, PPI-2458, for the treatment of rheumatoid arthritis
Proc. Natl. Acad. Sci. USA
101
10768-10773
2004
Homo sapiens
Hu, X.; Dang, Y.; Tenney, K.; Crews, P.; Tsai, C.W.; Sixt, K.M.; Cole, P.A.; Liu, J.O.
Regulation of c-Src nonreceptor tyrosine kinase activity by bengamide A through inhibition of methionine aminopeptidases
Chem. Biol.
14
764-774
2007
Homo sapiens (P50579), Homo sapiens (P53582)
Sawanyawisuth, K.; Wongkham, C.; Pairojkul, C.; Saeseow, O.T.; Riggins, G.J.; Araki, N.; Wongkham, S.
Methionine aminopeptidase 2 over-expressed in cholangiocarcinoma: potential for drug target
Acta Oncol.
46
378-385
2007
Homo sapiens (P50579), Homo sapiens
Kass, D.; Bridges, R.S.; Borczuk, A.; Greenberg, S.
Methionine aminopeptidase-2 as a selective target of myofibroblasts in pulmonary fibrosis
Am. J. Respir. Cell Mol. Biol.
37
193-201
2007
Mus musculus (O08663), Rattus norvegicus (P38062), Homo sapiens (P50579)
Hu, X.; Addlagatta, A.; Matthews, B.W.; Liu, J.O.
Identification of pyridinylpyrimidines as inhibitors of human methionine aminopeptidases
Angew. Chem.
45
3772-3775
2006
Homo sapiens (P50579), Homo sapiens (P53582)
Upadhya, R.; Zhang, H.S.; Weiss, L.M.
System for expression of microsporidian methionine amino peptidase type 2 (MetAP2) in the yeast Saccharomyces cerevisiae
Antimicrob. Agents Chemother.
50
3389-3395
2006
Escherichia coli, Homo sapiens (P50579), Homo sapiens, Encephalitozoon cuniculi (Q8SR45), Encephalitozoon cuniculi
Hu, X.V.; Chen, X.; Han, K.C.; Mildvan, A.S.; Liu, J.O.
Kinetic and mutational studies of the number of interacting divalent cations required by bacterial and human methionine aminopeptidases
Biochemistry
46
12833-12843
2007
Escherichia coli, Homo sapiens (Q6UB28), Homo sapiens
Nonato, M.C.; Widom, J.; Clardy, J.
Human methionine aminopeptidase type 2 in complex with L- and D-methionine
Bioorg. Med. Chem. Lett.
16
2580-2583
2006
Homo sapiens (P50579), Homo sapiens
Kawai, M.; BaMaung, N.Y.; Fidanze, S.D.; Erickson, S.A.; Tedrow, J.S.; Sanders, W.J.; Vasudevan, A.; Park, C.; Hutchins, C.; Comess, K.M.; Kalvin, D.; Wang, J.; Zhang, Q.; Lou, P.; Tucker-Garcia, L.; Bouska, J.; Bell, R.L.; Lesniewski, R.; Henkin, J.; Sheppard, G.S.
Development of sulfonamide compounds as potent methionine aminopeptidase type II inhibitors with antiproliferative properties
Bioorg. Med. Chem. Lett.
16
3574-3577
2006
Homo sapiens (P50579)
Haldar, M.K.; Scott, M.D.; Sule, N.; Srivastava, D.K.; Mallik, S.
Synthesis of barbiturate-based methionine aminopeptidase-1 inhibitors
Bioorg. Med. Chem. Lett.
18
2373-2376
2008
Homo sapiens (P53582), Homo sapiens
Hannig, G.
Team work in protein processing
Chem. Biol.
14
732-734
2007
Homo sapiens (P50579), Homo sapiens (P53582)
Kowalinski, E.; Bange, G.; Bradatsch, B.; Hurt, E.; Wild, K.; Sinning, I.
The crystal structure of Ebp1 reveals a methionine aminopeptidase fold as binding platform for multiple interactions
FEBS Lett.
581
4450-4454
2007
Homo sapiens (P50579), Homo sapiens
Lu, J.; Chong, C.R.; Hu, X.; Liu, J.O.
Fumarranol, a rearranged fumagillin analogue that inhibits angiogenesis in vivo
J. Med. Chem.
49
5645-5648
2006
Homo sapiens (P50579)
Marino, J.P.; Fisher, P.W.; Hofmann, G.A.; Kirkpatrick, R.B.; Janson, C.A.; Johnson, R.K.; Ma, C.; Mattern, M.; Meek, T.D.; Ryan, M.D.; Schulz, C.; Smith, W.W.; Tew, D.G.; Tomazek, T.A.; Veber, D.F.; Xiong, W.C.; Yamamoto, Y.; Yamashita, K.; Yang, G.; Thompson, S.K.
Highly potent inhibitors of methionine aminopeptidase-2 based on a 1,2,4-triazole pharmacophore
J. Med. Chem.
50
3777-3785
2007
Homo sapiens (P50579), Homo sapiens
Tucker, L.A.; Zhang, Q.; Sheppard, G.S.; Lou, P.; Jiang, F.; McKeegan, E.; Lesniewski, R.; Davidsen, S.K.; Bell, R.L.; Wang, J.
Ectopic expression of methionine aminopeptidase-2 causes cell transformation and stimulates proliferation
Oncogene
2008
1-10
2008
Homo sapiens (P50579), Homo sapiens
Hu, X.; Addlagatta, A.; Lu, J.; Matthews, B.W.; Liu, J.O.
Elucidation of the function of type 1 human methionine aminopeptidase during cell cycle progression
Proc. Natl. Acad. Sci. USA
103
18148-18153
2006
Homo sapiens (P53582), Homo sapiens
Addlagatta, A.; Matthews, B.W.
Structure of the angiogenesis inhibitor ovalicin bound to its noncognate target, human type 1 methionine aminopeptidase
Protein Sci.
15
1842-1848
2006
Homo sapiens (P50579), Homo sapiens (P53582), Homo sapiens
Priest, R.C.; Spaull, J.; Buckton, J.; Grimley, R.L.; Sims, M.; Binks, M.; Malhotra, R.
Immunomodulatory activity of a methionine aminopeptidase-2 inhibitor on B cell differentiation
Clin. Exp. Immunol.
155
514-522
2009
Callithrix jacchus, Homo sapiens, Mus musculus
Warder, S.E.; Tucker, L.A.; McLoughlin, S.M.; Strelitzer, T.J.; Meuth, J.L.; Zhang, Q.; Sheppard, G.S.; Richardson, P.L.; Lesniewski, R.; Davidsen, S.K.; Bell, R.L.; Rogers, J.C.; Wang, J.
Discovery, identification, and characterization of candidate pharmacodynamic markers of methionine aminopeptidase-2 inhibition
J. Proteome Res.
7
4807-4820
2008
Homo sapiens, Mus musculus
Arico-Muendel, C.C.; Benjamin, D.R.; Caiazzo, T.M.; Centrella, P.A.; Contonio, B.D.; Cook, C.M.; Doyle, E.G.; Hannig, G.; Labenski, M.T.; Searle, L.L.; Lind, K.; Morgan, B.A.; Olson, G.; Paradise, C.L.; Self, C.; Skinner, S.R.; Sluboski, B.; Svendsen, J.L.; Thompson, C.D.; Westlin, W.; White, K.F.
Carbamate analogues of fumagillin as potent, targeted inhibitors of methionine aminopeptidase-2
J. Med. Chem.
52
8047-8056
2009
Homo sapiens
Alvarado, J.J.; Nemkal, A.; Sauder, J.M.; Russell, M.; Akiyoshi, D.E.; Shi, W.; Almo, S.C.; Weiss, L.M.
Structure of a microsporidian methionine aminopeptidase type 2 complexed with fumagillin and TNP-470
Mol. Biochem. Parasitol.
168
158-167
2009
Homo sapiens, Encephalitozoon cuniculi, Enterocytozoon bieneusi (B7XJ30), Enterocytozoon bieneusi, Enterocytozoon bieneusi H348 (B7XJ30)
Selvakumar, P.; Lakshmikuttyamma, A.; Das, U.; Pati, H.N.; Dimmock, J.R.; Sharma, R.K.
NC2213: a novel methionine aminopeptidase 2 inhibitor in human colon cancer HT29 cells
Mol. Cancer
8
65
2009
Homo sapiens
Xiao, Q.; Zhang, F.; Nacev, B.A.; Liu, J.O.; Pei, D.
Protein N-terminal processing: substrate specificity of Escherichia coli and human methionine aminopeptidases
Biochemistry
49
5588-5599
2010
Escherichia coli, Homo sapiens
Altmeyer, M.A.; Marschner, A.; Schiffmann, R.; Klein, C.D.
Subtype-selectivity of metal-dependent methionine aminopeptidase inhibitors
Bioorg. Med. Chem. Lett.
20
4038-4044
2010
Escherichia coli, Homo sapiens, Staphylococcus aureus
Hou, Y.P.; Sun, J.; Pang, Z.H.; Lv, P.C.; Li, D.D.; Yan, L.; Zhang, H.J.; Zheng, E.X.; Zhao, J.; Zhu, H.L.
Synthesis and antitumor activity of 1,2,4-triazoles having 1,4-benzodioxan fragment as a novel class of potent methionine aminopeptidase type II inhibitors
Bioorg. Med. Chem.
19
5948-5954
2011
Homo sapiens
Ma, A.C.; Fung, T.K.; Lin, R.H.; Chung, M.I.; Yang, D.; Ekker, S.C.; Leung, A.Y.
Methionine aminopeptidase 2 is required for hematopoietic stem cell initiation and proliferation
Blood
118
5448-5457
2011
Danio rerio, Homo sapiens
Chiu, J.; Wong, J.W.; Hogg, P.J.
Redox regulation of methionine aminopeptidase 2 activity
J. Biol. Chem.
289
15035-15043
2014
Homo sapiens (P50579)
Zhang, F.; Bhat, S.; Gabelli, S.B.; Chen, X.; Miller, M.S.; Nacev, B.A.; Cheng, Y.L.; Meyers, D.J.; Tenney, K.; Shim, J.S.; Crews, P.; Amzel, L.M.; Ma, D.; Liu, J.O.
Pyridinylquinazolines selectively inhibit human methionine aminopeptidase-1 in cells
J. Med. Chem.
56
3996-4016
2013
Homo sapiens (P53582), Homo sapiens
Heinrich, T.; Buchstaller, H.P.; Cezanne, B.; Rohdich, F.; Bomke, J.; Friese-Hamim, M.; Krier, M.; Knoechel, T.; Musil, D.; Leuthner, B.; Zenke, F.
Novel reversible methionine aminopeptidase-2 (MetAP-2) inhibitors based on purine and related bicyclic templates
Bioorg. Med. Chem. Lett.
27
551-556
2017
Homo sapiens (P50579)
Arya, T.; Reddi, R.; Kishor, C.; Ganji, R.J.; Bhukya, S.; Gumpena, R.; McGowan, S.; Drag, M.; Addlagatta, A.
Identification of the molecular basis of inhibitor selectivity between the human and streptococcal type I methionine aminopeptidases
J. Med. Chem.
58
2350-2357
2015
Streptococcus pneumoniae (B2IQ22), Homo sapiens (P53582), Homo sapiens, Streptococcus pneumoniae CGSP14 (B2IQ22)
Van Damme, P.; Hole, K.; Gevaert, K.; Arnesen, T.
N-terminal acetylome analysis reveals the specificity of Naa50 (Nat5) and suggests a kinetic competition between N-terminal acetyltransferases and methionine aminopeptidases
Proteomics
15
2436-2446
2015
Homo sapiens (P50579), Homo sapiens
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