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
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3.4.11.18
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microtubule-associated
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microtubule
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dendritic
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hippocampus
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tubulin
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protein-2
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tau
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cerebral
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aminopeptidases
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fumagillin
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nestin
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neurite
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cortical
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cytoskeletal
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neurofilament
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neuroprotective
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ischemia
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fibrillary
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synaptophysin
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outgrowth
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neurotrophic
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neuron-specific
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beta-tubulin
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neurogenesis
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map2
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synapsin
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antiangiogenic
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deformylase
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microtubule-binding
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calbindin
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synthesis
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dinuclear
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microsporidian
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drug development
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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
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3.4.11.18 methionyl aminopeptidaseAdvanced search results
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results (Metals Ions
Metals Ions on EC 3.4.11.18 - methionyl aminopeptidase
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METALS and IONS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Ca2+
Co2+
Fe2+
Mg2+
Mn2+
Ni2+
Zinc
Zn2+
additional information
Co2+
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required, both isoform MAP and YflG. YflG shows strong preference for Co2+
Co2+
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absolutely required, maximal enzyme activity is observed at 3.0 molar equivalents
Co2+
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in mutant enzymes D97A and E204V cobalt content is not detectable, in mutant enzyme H171L and 235V the cobalt content is 3% of that of the wild-type enzyme, in mutant enzyme D108A the cobalt content is 6% of that of the wild-type enzyme
Co2+
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maximal activity is observed after addition of only 1 equivalent of divalent metal ion, the metal binding constant for the first binding event is 0.0003 mM for Co(II)-substituted enzyme. The metal ion resides in a pentacoordinate geometry
Co2+
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the active site contains two Co2+, ligated by the side chains of Asp97, Asp108, Glu204, Glu235, and His171 with approximate octahedral coordination
Co2+
enzyme binds up to 1.1 equivalents of Co2+ in the metal concentration range found in vivo. Dissociation constant is about 0.0025-0.004 mM
Co2+
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the dicobalt form of the methionine aminopeptidase has an active site with one 5-coordinate Co2+ and a more weakly bound 6-coordinate Co2+
Co2+
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the kcat value increases as a function of Co2+ ion concentration and exhibits a maximum after the addition of one equivalent of Co2+
Co2+
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activates, two metal ions are coordinated by five conserved amino acid residues D97, D108, H171, E204 and E235, activation kinetics, overview
Co2+
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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+
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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
Co2+
significant activation at 0.01 mM, at least two Co2+ ions, which may act cooperatively, are needed to promote catalysis
Co2+
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determination of metal affinity to the active site of the metalloenzyme by onlinear curve fitting of metal titration curves using the multiple independent binding sites, MIBS, model, overview
Co2+
and Ni2+, best activators. Highest activity at 0.1 mM
Co2+
may substitute for Ni2+. Highest activity at 0.04 mM
Co2+
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the mutant enzyme contains 0.43 mol of Co2+ per mol. The wild-type enzyme contains 0.75 mol of Co2+ per mol of enzyme
Co2+
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1 mol of wild-type enzyme contains 2 mol of zinc ions and at least 1 mol of cobalt ion, whereas 1 mol of the truncated methionine aminopeptidase DELTA2-69 lacking the putative zinc fingers cotains only a trace amount of zinc ions but still contains one mol of cobalt ion
Co2+
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loosely associated with the enzyme protein
Fe2+
activator after removal of divalent metal ions with Chelex-100
Fe2+
activator after removal of divalent metal ions with EDTA
Fe2+
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maximal activity is observed after addition of only 1 equivalent of divalent metal ion, the metal binding constant for the first binding event is 0.0002 mM for Fe(II)-substituted enzyme. The metal ion resides in a pentacoordinate geometry
Fe2+
Fe2+ is the likely metal cofactor used by MetAP in the cellular environment
Mn2+
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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
Mn2+
may substitute for Co2+ or Ni2+, highest activity at 0.4 mM
Mn2+
enzyme contains 2 Mn-ions residing in a distorted trigonal bipyramidal geometry. A bridging water molecule is displaced by L-methionine
Ni2+
activator after removal of divalent metal ions with Chelex-100
Ni2+
activator after removal of divalent metal ions with EDTA, less efficient than Fe2+
Ni2+
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may substitute for Co2+, maximal enzyme activity is observed at 10.0 molar equivalents
Ni2+
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activates apoenzyme with Met-7-amido-4-methylcoumarin as substrate, very poor activity in presence of Met-S-Gly-Phe as substrate
Ni2+
and Co2+, best activators. Highest activity at 0.1 mM
Ni2+
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enzyme is active at concentrations below 0.002 mM, inhibition at higher concentrations
Zinc
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methionine aminopeptidase type 1 requires its N-terminal zinc finger domain for normal function in vivo
Zinc
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1 mol of wild-type enzyme contains 2 mol of Zn2+, zinc fingers are essential for normal MAP function
Zn2+
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may substitute for Co2+, maximal enzyme activity is observed at 10.0 molar equivalents. Activity with Zn2+ is not dependent on pH
Zn2+
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1 mol of wild-type enzyme contains 2 mol of zinc ions and at least 1 mol of cobalt ion, whereas 1 mol of the truncated methionine aminopeptidase DELTA2-69 lacking the putative zinc fingers cotains only a trace amount of zinc ions but still contains one mol of cobalt ion
additional information
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MetAP belongs to the dinuclear metallohydrolases, mathematical model and detailed analysis of the stoichiometric activation of MetAP by metal cofactors, overview
additional information
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MetAP can be activated in vitro by a number of divalent metals
additional information
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MetAp requires divalent metal ions for catalytic activity
additional information
Zn(II)-activated MAP2 shows negligible amidolytic activity
additional information
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Zn(II)-activated MAP2 shows negligible amidolytic activity
additional information
MetAP is one of the dinuclear metallohydrolases. MetAP1c requires divalent cations for activity. Co2+ and Fe2+ show the tightest binding, while Ni2+ is the most efficient cofactor for the catalysis. Metal binding kinetics, overview
additional information
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MetAP is one of the dinuclear metallohydrolases. MetAP1c requires divalent cations for activity. Co2+ and Fe2+ show the tightest binding, while Ni2+ is the most efficient cofactor for the catalysis. Metal binding kinetics, overview
additional information
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not activating: Ni2+, Mg2+, Ca2+, Cd2+, Cu2+
additional information
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the purified preparations do not contain significant amounts of any metal. Enzymatically important metal is loosely associated and lost during enzyme purification
additional information
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activating potencies of divalent metal ions with the three isozymes, overview
