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
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microtubule-associated
- microtubule
- dendritic
- hippocampus
- tubulin
- protein-2
- tau
- cerebral
- aminopeptidases
- fumagillin
- nestin
-
neurite
- cortical
- cytoskeletal
- neurofilament
-
neuroprotective
- ischemia
-
fibrillary
-
synaptophysin
-
outgrowth
-
neurotrophic
-
neuron-specific
- beta-tubulin
-
neurogenesis
- map2
- synapsin
-
antiangiogenic
-
deformylase
-
microtubule-binding
- calbindin
- synthesis
-
dinuclear
-
microsporidian
- drug development
- medicine
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 (Engineering
Engineering on EC 3.4.11.18 - methionyl aminopeptidase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
C70A
hydrolysis of Met-Ala-Ser similar to wild-type, relaxed specificity
C70S
D108A
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2% of the activity compared to the wild-type enzyme, cobalt content is 6% of that of the wild-type enzyme
D97A
D97E
the mutation causes an about 9000fold decrease in kcat and a 2000fold decreased catalytic efficiency (kcat/Km) for the Co(II)-loaded enzyme towards L-Met-Gly-L-Met-L-Met as compared to the wild type enzyme
D97N
the mutation causes an about 9000fold decrease in kcat and a 3000fold decreased catalytic efficiency (kcat/Km) for the Co(II)-loaded enzyme towards L-Met-Gly-L-Met-L-Met as compared to the wild type enzyme
E204V
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5% of the activity compared to the wild-type enzyme, cobalt content is not detectable
E235V
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3% of the activity compared to the wild-type enzyme, cobalt content is 3% of that of the wild-type enzyme
H171L
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6% of the activity compared to the wild-type enzyme, cobalt content is 6% of that of the wild-type enzyme
H178A
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the mutant enzyme binds only one equivalent of Co(II) or Fe(II) tightly with affinities that are identical to the wild-type. The turnover-number for Co(II) loaded H178A decreases 70fold towards Met-Gly-Met-Met ans 290fold towards Met-Pro-p-nitroanilide. The KM-value for Met-Gly-Met-Met remains unaffected, while that for Met-Pro-p-nitroanilide increases approximately 2fold for Co(II) - and Fe(II)-loaded H178A. The ratio of turnover-number to Km-value for both Co(II)- and Fe(II)-loaded H178A towards both substrates ranges from 50fold to 580fold reduction
H63A
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the mutation does not affect the ability of the enzyme to bind divalent metal ions but affects the hydrolysis of small peptide substrates whereas large peptides can overcome the observed loss in binding energy by additional hydrophilic and hydrophobic interactions
H79A
Y168A
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increase in initiator methionine removal with valine in penultimate position of substrate
A362T
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type II enzyme, mutation results in resistance to ovalicin, TNP-470 and fumagillin when expressed in yeast
C202A
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hydrolysis of Met-PSI[C(O)S]Gly-Phe similar to wild-type, relaxed specificity
H382Y
T334A
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type I enzyme, mutation renders the resistant wild-type enzyme sensitive to ovalicin
Y444C
C105S
C105V
6fold decrease in kcat/Km value compared to wild-type
DELTA 2-10
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30% activity with 10fold amount of enzyme in the assay relative to wild type
DELTA 2-15
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30% activity with 10fold amount of enzyme in the assay relative to wild type
C105S
C105T
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4old decrease in kcat/Km value compared to wild-type
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C105V
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6fold decrease in kcat/Km value compared to wild-type
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B255L
no substantial growth defect in comparison to the growth of control strains
V18G
no substantial growth defect in comparison to the growth of control strains
V18G/W55L
mutant has traces of enzymatic activity, and has no substantial growth defect in comparison to the growth of control strains. When isof0orm MapA is present, the 8% activity of MapB mutant V18G/W255L is sufficient for viability and normal growth, whereas bacteria without MapA can retrieve no viable colonies
C22S
C27S
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the activity with Met-Gly-Met-Met is 107% of that of the wild-type enzyme
C37S
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the activity with Met-Gly-Met-Met is 94% of that of the wild-type enzyme
C40S
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the activity with Met-Gly-Met-Met is 85% of that of the wild-type enzyme
C50S
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the activity with Met-Gly-Met-Met is 99% of that of the wild-type enzyme
C54S
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the activity with Met-Gly-Met-Met is 97% of that of the wild-type enzyme
D219N
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the mutant enzyme has 1000fold lower activity and a different substrate specificity when compared to wild-type enzyme. Expression of the mutant enzyme in yeast causes a slow-growth phenotype and interferes with wild-type metAP1 in a dominant manner. 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. 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'
DELTA2-69
H174A
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no enzymic activity, overexpression using a strong promoter in map1 null strain is lethal, overexpression using a weak promoter slightly inhibits growth
H62R
H66R
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the activity with Met-Gly-Met-Met is 84% of that of the wild-type enzyme
M329A
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mutation produces an avarage catalytic efficiency 1.5fold higher than the native enzyme on normal substrates and cleaves substrates containing penultimate Asn, Gln, Ile, Leu, Met and Phe
additional information
D97A
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4% of the activity compared to the wild-type enzyme, cobalt content is not detectable
D97A
the mutation causes an about 9000fold decrease in kcat and a 6100fold decreased catalytic efficiency (kcat/Km) for the Co(II)-loaded enzyme towards L-Met-Gly-L-Met-L-Met as compared to the wild type enzyme, the mutation effectively removes the ability of the enzyme to form a dinuclear site, providing a MetAP enzyme that retains catalytic activity, albeit at extremely low levels
H79A
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Co2+-loaded H79A exhibits an overall of more than 7000fold decrease in specific activity, the almost complete loss of activity is primarily due to a more than 6000fold decrease in kcat, the Km value obtained for Co2+-loaded H79A is approximately half the value observed for wild type MetAP-I, specific activity of Mn2+-loaded H79A decreases by about 2.6fold while kcat decreases by about 3.5fold, the observed Km value for Mn2+ loaded H79A is about 1.4fold larger than that observed for wild type enzyme
H382Y
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type II enzyme, mutation results in resistance to ovalicin, TNP-470 and fumagillin when expressed in yeast
H382Y
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the single site mutation in the S1 subsite of human MetAP2b results in inhibitor resistance
Y444C
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type II enzyme, mutation results in resistance to TNP-470, but not to fumagillin when expressed in yeast
Y444C
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the single site mutation in the S1 subsite of human MetAP2b results in inhibitor resistance
C105S
contratry to wild-type, no inhibition by cysteien-modifying compounds N-ethylmaleimide, 5,5'-dithiobis(2-nitrobenzoic acid) and 2-hydroxyethyl disulfide
C105S
10fold decrease in kcat/Km value compared to wild-type
C105S
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contratry to wild-type, no inhibition by cysteien-modifying compounds N-ethylmaleimide, 5,5'-dithiobis(2-nitrobenzoic acid) and 2-hydroxyethyl disulfide
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C105S
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10fold decrease in kcat/Km value compared to wild-type
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C22S
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zinc finger point mutant, processing efficiency of the mutant enzyme is less than that of the wild-type enzyme in vivo. Association of the mutant enzyme with the 60S ribosome subunit is disrupted
C22S
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the activity with Met-Gly-Met-Met is 116% of that of the wild-type enzyme
DELTA2-69
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zinc-finger deletion mutant, processing efficiency of the mutant enzyme is less than that of the wild-type enzyme in vivo
DELTA2-69
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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 mole of cobalt ion,the activity with Met-Gly-Met-Met is 84% of that of the wild-type enzyme
H62R
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zinc finger point mutant, processing efficiency of the mutant enzyme is less than that of the wild-type enzyme in vivo. Association of the mutant enzyme with the 60S ribosome subunit is disrupted
H62R
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the activity with Met-Gly-Met-Met is 95% of that of the wild-type enzyme
additional information
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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
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truncated MetAP1 lacking N-terminal 89 amino acids, 2.5fold increase in KM-value
additional information
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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
additional information
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enzyme deletion mutant, N-terminal region (residues 2-57) is essential but not sufficient for enzyme to fully interfere with map1 null growth
additional information
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the map-2 deficient mutant is severely impaired in surviving conditions of prolonged nitrogen starvation and high light exposure
