3.4.11.18: methionyl aminopeptidase
This is an abbreviated version!
For detailed information about methionyl aminopeptidase, go to the full flat file.
Word Map on EC 3.4.11.18
-
3.4.11.18
-
microtubule-associated
-
microtubule
-
dendritic
-
hippocampus
-
tubulin
-
protein-2
-
tau
-
cerebral
-
aminopeptidases
-
fumagillin
-
nestin
-
neurite
-
cortical
-
cytoskeletal
-
neurofilament
-
neuroprotective
-
ischemia
-
fibrillary
-
synaptophysin
-
outgrowth
-
neurotrophic
-
neuron-specific
-
beta-tubulin
-
neurogenesis
-
map2
-
synapsin
-
antiangiogenic
-
deformylase
-
microtubule-binding
-
calbindin
-
synthesis
-
dinuclear
-
microsporidian
-
drug development
-
medicine
- 3.4.11.18
-
microtubule-associated
- microtubule
- dendritic
- hippocampus
- tubulin
- protein-2
- tau
- cerebral
- aminopeptidases
- fumagillin
- nestin
-
neurite
- cortical
- cytoskeletal
- neurofilament
-
neuroprotective
- ischemia
-
fibrillary
-
synaptophysin
-
outgrowth
-
neurotrophic
-
neuron-specific
- beta-tubulin
-
neurogenesis
- map2
- synapsin
-
antiangiogenic
-
deformylase
-
microtubule-binding
- calbindin
- synthesis
-
dinuclear
-
microsporidian
- drug development
- medicine
Reaction
release of N-terminal amino acids, preferentially methionine, from peptides and arylamides =
Synonyms
aminopeptidase, methionine, c1MetAP-Ia, c2MetAP-Ia, c3MetAP-Ib, CoCoEcMetAP, Ebp1, eMet-AP, ErbB-3 receptor binding protein, initiation factor 2 associated 67 kDa glycoprotein, L-methionine aminopeptidase, LdBPK_210960, MAP, MAP-2, MAP-Pfu, MAP11, MAP1D, mAPA, MapB, MetAP, MetAP-1, MetAP-2, MetAP-I, MetAP-II, MetAP1, MetAP1a, MetAP1b, MetAP1c, MetAP1D, MetAP2, methionine amino peptidase type 2, methionine aminopeptidase, methionine aminopeptidase 1, methionine aminopeptidase 1b, methionine aminopeptidase 2, methionine aminopeptidase AbMetAPx, methionine aminopeptidase AbMetAPy, methionine aminopeptidase II, methionine aminopeptidase type 1, methionine aminopeptidase type 1a, methionine aminopeptidase type 1c, methionine aminopeptidase type 2, methionine aminopeptidase type I, methionine aminopeptidase type II, methionine aminopeptidase type-2, methionine aminopeptidase-1, methionine aminopeptidase-2, methionine aminopetidase-2, More, p67, p67eIF2, peptidase M, PVX_094985, TM1478, type 1 methionine aminopeptidase, type 2 methionine aminopeptidase, type I MetAP, type I methionine aminopeptidase, YpdF
ECTree
3.4.11.18 methionyl aminopeptidaseAdvanced search results
results (
results (Substrates Products
Substrates Products on EC 3.4.11.18 - methionyl aminopeptidase
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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
-
-
?
L-alanine-4-methylcoumarin-7-amide + H2O
L-alanine + 7-amino-4-methylcoumarin
-
-
-
?
L-leucine-4-methylcoumarin-7-amide + H2O
L-leucine + 7-amino-4-methylcoumarin
-
-
-
?
L-Met-L-Ala-L-Ser
L-Met + L-Ala-L-Ser
-
isoform MAP, 77% of the activity with L-Met-Gly-L-Met-L-Met, isoform YflG, 18% of the activity with L-Met-Gly-L-Met-L-Met
-
-
?
L-Met-L-Gln-L-Asp-onconase + H2O
L-Met + L-Gln-L-Asp-onconase
-
wild-type, no substrate, mutant M206G/Q233G, 96% of Met removal, mutant M206T/Q233G, 91% of removal, mutant M206T/Q233T, 93% of removal
-
-
?
L-Met-L-Pro-4-nitroanilide + H2O
L-Met + L-Pro-4-nitroaniline
-
-
-
?
L-Met-L-Ser-L-Ser-L-His-L-Arg-L-Trp-L-Asp-L-Trp + H2O
L-Met + L-Ser-L-Ser-L-His-L-Arg-L-Trp-L-Asp-L-Trp
-
-
-
-
?
L-methionyl-7-amido-4-methylcoumarin + H2O
L-methionine + 7-amino-4-methylcoumarin
-
-
-
-
?
Leu-Gly-Gly + H2O
?
-
34% of the activity with Met-Ala-Ser
-
-
?
Leu-Leu-Tyr + H2O
?
-
32% of the activity with Leu-Gly-Gly
-
-
?
Leu-Ser-Phe + H2O
?
-
30% of the activity with Met-Ala-Ser
-
-
?
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-Ala-His-Thr-Leu-Pro-Glu-Glu-Leu + H2O
Met + Ala-His-Thr-Leu-Pro-Glu-Glu-Leu
-
-
-
-
?
Met-Ala-Pro-Thr-Ser-Ser-Ser-Thr-Lys-Lys-Thr-Gln-Leu + H2O
Met + Ala-Pro-Thr-Ser-Ser-Ser-Thr-Lys-Lys-Thr-Gln-Leu
-
-
-
-
?
Met-Ala-Ser-His-Arg-Trp-Asp-Trp + H2O
Met + Ala-Ser-His-Arg-Trp-Asp-Trp
-
-
-
-
?
Met-Arg-Phe + H2O
Met + Arg-Phe
-
substrate of isozymes c1MetAP-Ia and c3MetAP-Ib, no activity with isozyme c2MetAP-Ia
-
-
?
Met-Asp-Gly + H2O
Met + Asp-Gly
-
substrate of isozyme c3MetAP-Ib, no activity with the other two isozymes
-
-
?
Met-Gly-Ala-Gln-Phe-Ser-Lys-Thr + H2O
Met + Gly-Ala-Gln-Phe-Ser-Lys-Thr
-
-
-
-
?
Met-Gly-Ser-His-Arg-Trp-Asp-Trp + H2O
Met + Gly-Ser-His-Arg-Trp-Asp-Trp
-
-
-
-
?
Met-Leu-Gly + H2O
Met + Leu-Gly
-
substrate of isozymes c1MetAP-Ia and c3MetAP-Ib, no activity with isozyme c2MetAP-Ia
-
-
?
Met-Met-Ala + H2O
Met + Met-Ala
-
substrate of isozymes c1MetAP-Ia and c3MetAP-Ib, no activity with isozyme c2MetAP-Ia
-
-
?
Met-Pro-Ser-His-Arg-Trp-Asp-Trp + H2O
Met + Pro-Ser-His-Arg-Trp-Asp-Trp
-
-
-
-
?
Met-Pro-Thr-Ser-Ser-Ser-Thr-Lys-Lys-Thr-Gln-Leu-Cys + H2O
Met + Pro-Thr-Ser-Ser-Ser-Thr-Lys-Lys-Thr-Gln-Leu-Cys
-
-
-
-
?
Met-Ser-Ser-His-Arg-Trp-Asp-Trp + H2O
Met + Ser-Ser-His-Arg-Trp-Asp-Trp
-
-
-
-
?
Met-Thr-Ser-His-Arg-Trp-Asp-Trp + H2O
Met + Thr-Ser-His-Arg-Trp-Asp-Trp
-
-
-
-
?
Met-Val-His-Thr-Leu-Pro-Glu-Glu-Leu + H2O
Met + Val-His-Thr-Leu-Pro-Glu-Glu-Leu
-
-
-
-
?
Met-Val-Ser-His-Arg-Trp-Asp-Trp + H2O
Met + Val-Ser-His-Arg-Trp-Asp-Trp
-
-
-
-
?
Met-[2-mercapto-ethanoyl]-Phe + H2O
[2-mercapto-ethanoyl]-Phe + Met
-
-
-
?
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
-
-
?
Nle-Gly-Met-Phe + H2O
Gly-Met-Phe + norleucine
KT943909
zinc-activated einzyme shows 159% of the activity with substrate Nle-Gly-Met-Phe
-
-
?
glutathione-S-transferase + H2O
?
-
removal of Met(init) from glutathione-S-transferase. Processing of glutathione-S-transferase in yeast relies almost entirely on MetAP1 function
-
-
?
glyceraldehye 3-phosphate dehydrogenase + H2O
?
-
MetAP2-specific substrate
-
-
?
glyceraldehye 3-phosphate dehydrogenase + H2O
?
-
MetAP2-specific substrate
-
-
?
L-Met 4-nitroanilide + H2O
L-Met + 4-nitroaniline
-
-
-
?
L-Met 4-nitroanilide + H2O
L-Met + 4-nitroaniline
-
-
-
?
L-Met 4-nitroanilide + H2O
L-Met + 4-nitroaniline
-
-
-
?
L-Met 4-nitroanilide + H2O
L-Met + 4-nitroaniline
-
-
-
?
L-Met-7-amido-4-methylcoumarin + H2O
L-Met + 7-amino-4-methylcoumarin
-
-
-
-
?
L-Met-7-amido-4-methylcoumarin + H2O
L-Met + 7-amino-4-methylcoumarin
-
-
-
?
L-Met-Gly-L-Met-L-Met + H2O
L-Met + Gly-L-Met-L-Met
-
-
-
-
?
L-Met-L-Pro-p-nitroanilide + H2O
L-Met + L-Pro-p-nitroanilide
-
-
-
-
?
L-Met-p-nitroanilide + H2O
L-Met + p-nitroaniline
Mycolicibacterium smegmatis mc(2)155 / ATCC 700084
-
-
-
-
?
L-methionine 4-methylcoumaryl-7-amide + H2O
L-methionine + 7-amino-4-methylcoumarin
-
-
-
?
L-methionine 4-methylcoumaryl-7-amide + H2O
L-methionine + 7-amino-4-methylcoumarin
-
-
-
?
L-methionine 4-methylcoumaryl-7-amide + H2O
L-methionine + 7-amino-4-methylcoumarin
-
-
-
?
L-methionine 4-methylcoumaryl-7-amide + H2O
L-methionine + 7-amino-4-methylcoumarin
-
-
-
?
L-methionine 4-methylcoumaryl-7-amide + H2O
L-methionine + 7-amino-4-methylcoumarin
-
-
-
?
L-methionine 4-nitroanilide + H2O
L-methionine + 4-nitroaniline
-
-
-
?
L-methionine 4-nitroanilide + H2O
L-methionine + 4-nitroaniline
-
-
-
?
L-methionine-4-methylcoumarin-7-amide + H2O
L-methionine + 7-amino-4-methylcoumarin
-
-
-
?
L-methionine-4-methylcoumarin-7-amide + H2O
L-methionine + 7-amino-4-methylcoumarin
-
fluorogenic substrate
-
-
?
L-methionine-7-amido-4-methylcoumarin + H2O
L-methionine + 7-amino-4-methylcoumarin
-
-
-
?
L-methionine-7-amido-4-methylcoumarin + H2O
L-methionine + 7-amino-4-methylcoumarin
-
-
-
?
L-methionine-7-amido-4-methylcoumarin + H2O
L-methionine + 7-amino-4-methylcoumarin
-
-
-
-
?
L-methionyl 4-methylcoumarin-7-amide + H2O
L-methionine + 7-amino-4-methylcoumarin
-
fluorogenic substrate
-
-
?
L-methionyl 4-methylcoumarin-7-amide + H2O
L-methionine + 7-amino-4-methylcoumarin
fluorogenic substrate
-
-
?
L-methionyl 4-methylcoumarin-7-amide + H2O
L-methionine + 7-amino-4-methylcoumarin
fluorogenic substrate
-
-
?
Met-4-methylcoumaryl-7-amide + H2O
Met + 7-amino-4-methylcoumarin
-
-
-
?
Met-4-methylcoumaryl-7-amide + H2O
Met + 7-amino-4-methylcoumarin
-
-
-
?
Met-7-amido-4-methylcoumarin + H2O
Met + 7-amino-4-methylcoumarin
-
-
-
?
Met-7-amido-4-methylcoumarin + H2O
Met + 7-amino-4-methylcoumarin
-
-
-
?
Met-7-amido-4-methylcoumarin + H2O
Met + 7-amino-4-methylcoumarin
-
-
-
?
Met-7-amido-4-methylcoumarin + H2O
Met + 7-amino-4-methylcoumarin
-
-
-
?
Met-Ala-Ser + H2O
Met + Ala-Ser
-
also cleaves methionine from other tripeptides with a relatively small and/or uncharged penultimate amino acid residue (Pro, Gly, Val, Thr, or Ser) but not if bulky and/or charged (Arg, His, Leu, Met, or Tyr)
-
-
?
Met-Lys-bradykinin + H2O
Met + Lys-bradykinin
-
i.e. Met-Lys-Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg
-
-
?
Met-peptide + H2O
Met + peptide
-
the enzyme removes the N-terminal Met from polypeptides, and thus plays a key role in protein synthesis, modification and transport
-
-
?
Met-peptide + H2O
Met + peptide
-
the enzyme catalyzes the removal of an amino-terminal methionine from a newly synthesized polypeptide
-
-
?
Met-peptide + H2O
Met + peptide
-
the enzyme is directly involved in the regulation of growth factor-stimulated endothelial cell proliferation
-
-
?
Met-peptide + H2O
Met + peptide
-
the biological function is removing the terminal methionine from nascent peptides
-
-
?
Met-peptide + H2O
Met + peptide
-
the biological function is removing the terminal methionine from nascent peptides during protein synthesis
-
-
?
Met-peptide + H2O
Met + peptide
-
the enzyme is responsible for hydrolysis of the initiator methionine residue from the majority of newly synthesized proteins. Potentially important role in the production of recombinant proteins, since failure to correctly remove initiator methionine residues can result in a product that is inactive or immunogenic
-
-
?
SH3 binding glutamic acid rich-like protein + H2O
?
-
MetAP2-specific substrate
-
-
?
SH3 binding glutamic acid rich-like protein + H2O
?
-
MetAP2-specific substrate
-
-
?
additional information
?
-
-
active site structure and substrate binding, overview
-
-
?
additional information
?
-
-
no substrates: Gly 4-nitroanilide , Ala 4-nitroanilide, Ser 7-amido-4-methyl-coumarin, Leu 4-nitroanilide, Glu 4-nitroanilide, Lys 4-nitroanilide and Arg 4-nitroanilide
-
-
?
additional information
?
-
active site structure and substrate binding, overview
-
-
?
additional information
?
-
-
active site structure and substrate binding, overview
-
-
?
additional information
?
-
active site structure and substrate binding, overview
-
-
?
additional information
?
-
-
residues adjacent to the initiation methionine can significantly influence the methionine cleavage process
-
-
?
additional information
?
-
-
detailed analysis of mutants specificity on oligo- and protein substrates
-
-
?
additional information
?
-
-
enzyme hydrolyzes N-terminal L-methionine when the next amino acid is L-alanine, L-proline, or L-serine with substrate preference in decreasing order: proloine, alanine, serine. enzyme hydrolyzes the Xaa-Po peptide bond when the first amino acid is L-alanine, L-asparagine, or L-methionine
-
-
?
additional information
?
-
-
peptides with Val or Thr at P1' are much less efficiently cleaved than those with Ala, Cys, Gly, Pro, or Ser in this position
-
-
?
additional information
?
-
-
substrate specificity is systematically profiled by screening against a combinatorial peptide library and kinetic analysis of individually synthesized peptide substrates
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
together with N-myristoyltransferase, enzyme plays a major role in the process of myristoylation of oncoproteins including the c-src family
-
-
?
additional information
?
-
-
no activity when using Glu-Ala-Ser and Leu-Ala-Ser peptides as substrates
-
-
?
additional information
?
-
-
active site strutcure and substrate binding, overview
-
-
?
additional information
?
-
-
substrate specificity is systematically profiled by screening against a combinatorial peptide library and kinetic analysis of individually synthesized peptide substrates
-
-
?
additional information
?
-
among the 4-methylcoumarin-7-amides tested, activity is highest with L-alanine 4-methylcoumarin-7-amide
-
-
?
additional information
?
-
-
among the 4-methylcoumarin-7-amides tested, activity is highest with L-alanine 4-methylcoumarin-7-amide
-
-
?
additional information
?
-
-
isozyme substrate specificity, overview
-
-
?
additional information
?
-
-
MetAP carries out the cotranslational N-terminal methionine excision
-
-
?
additional information
?
-
-
the enzyme hydrolyzes NH2-terminal methionine from methionyl peptides longer than tetrapeptides and from shorter methionyl peptides with blocked carboxy ends
-
-
?
additional information
?
-
-
the isozymes act on peptides in the cytosol, that are N-terminal fragments from digestion of hemoglobin in the digestive vacuole. The hemoglobin-derived peptides show leucine and alanine as most abundant amino acids
-
-
?
additional information
?
-
-
the enzyme shows preference for synthetic peptides containing leucine and alanine
-
-
?
additional information
?
-
-
removes methionine from hemoglobin nascent peptides
-
-
?
additional information
?
-
-
specificity: the enzyme does not cleave amino-terminal methionine when it precedes residues of glutamic acid
-
-
?
additional information
?
-
-
specificity: the enzyme cleaves amino-terminal methionine when it precedes residues of threonine
-
-
?
additional information
?
-
-
specificity: the enzyme does not cleave amino-terminal methionine when it precedes residues of lysine
-
-
?
additional information
?
-
-
specificity: the enzyme cleaves amino-terminal methionine when it precedes residues of valine
-
-
?
additional information
?
-
-
specificity: the enzyme does not cleave amino-terminal methionine when it precedes residues of asparagine
-
-
?
additional information
?
-
-
no activity with methionine 4-nitroanilide
-
-
?
additional information
?
-
-
specificity: the enzyme does not cleave amino-terminal methionine when it precedes residues of aspartic acid
-
-
?
additional information
?
-
-
specificity: the enzyme cleaves amino-terminal methionine when it precedes residues of proline
-
-
?
additional information
?
-
-
the mutant enzyme prefers substrates, having Ser or Pro at P1', over substrates that contain glycine and alanine at that position. The wild-type enzyme prefers substrates that have Ala, Gly, Ser or Pro at P1'. Amino-terminal Met cannot be removed by either the mutant or wild-type enzyme from substrates having large and charged amino acids at P1' position
-
-
?
additional information
?
-
-
specificity: the enzyme does not cleave amino-terminal methionine when it precedes residues of leucine
-
-
?
additional information
?
-
-
specificity: the enzyme does not cleave amino-terminal methionine when it precedes residues of isoleucine
-
-
?
additional information
?
-
-
removal of the initiator methionine if the penultimate residue has a small radius of gyration (Gly, Ala, Ser, Thr, Pro, Val and Cys)
-
-
?
additional information
?
-
-
specificity: the enzyme does not cleave amino-terminal methionine when it precedes residues of arginine
-
-
?
additional information
?
-
-
specificity: the enzyme cleaves amino-terminal methionine when it precedes residues of serine
-
-
?
additional information
?
-
-
specificity: the enzyme cleaves amino-terminal methionine when it precedes residues of glycine
-
-
?
additional information
?
-
-
specificity: the enzyme cleaves amino-terminal methionine when it precedes residues of alanine
-
-
?
additional information
?
-
-
specificity: the enzyme does not cleave amino-terminal methionine when it precedes residues of glutamine
-
-
?
additional information
?
-
no substrates: 4-nitroanilides of Val, Arg, Leu, Glu, Gly, Lys, Phe, Pro,Tyr, Ile
-
-
?
additional information
?
-
-
no substrates: 4-nitroanilides of Val, Arg, Leu, Glu, Gly, Lys, Phe, Pro,Tyr, Ile
-
-
?
additional information
?
-
no substrates: 4-nitroanilides of Val, Arg, Leu, Glu, Gly, Lys, Phe, Pro,Tyr, Ile
-
-
?
additional information
?
-
-
specificity: the enzyme does not cleave amino-terminal methionine when it precedes residues of lysine
-
-
?
additional information
?
-
-
specificity: the enzyme cleaves amino-terminal methionine when it precedes residues of valine
-
-
?
additional information
?
-
-
specificity: the enzyme cleaves amino-terminal methionine when it precedes residues of proline
-
-
?
additional information
?
-
-
specificity: the enzyme does not cleave amino-terminal methionine when it precedes residues of leucine
-
-
?
additional information
?
-
-
specificity: the enzyme cleaves amino-terminal methionine when it precedes residues of serine
-
-
?
additional information
?
-
-
specificity: the enzyme cleaves amino-terminal methionine when it precedes residues of glycine
-
-
?
additional information
?
-
-
specificity: the enzyme cleaves amino-terminal methionine when it precedes residues of alanine
-
-
?
additional information
?
-
-
substrate specificities of recombinant isozymes, overview, no activity towards tripeptides in which the N-terminal amino acid is not Met, no activity with Pro-Met and X-Gly-Gly peptides
-
-
?
