Information on EC 3.4.11.15 - aminopeptidase Y

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The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota

EC NUMBER
COMMENTARY hide
3.4.11.15
-
RECOMMENDED NAME
GeneOntology No.
aminopeptidase Y
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
preferentially, release of N-terminal lysine
show the reaction diagram
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
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-
-
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CAS REGISTRY NUMBER
COMMENTARY hide
114796-97-3
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain JCM 1004
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-
Manually annotated by BRENDA team
strain JCM 1004
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-
Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(Arg)3 + H2O
Arg + Arg-Arg
show the reaction diagram
-
-
-
ir
(Leu)3 + H2O
Leu + Leu-Leu
show the reaction diagram
-
-
-
ir
(Lys)3 + H2O
Lys + Lys-Lys
show the reaction diagram
-
-
-
ir
Ala-7-amido-4-methylcoumarin + H2O
Ala + 7-amino-4-methylcoumarin
show the reaction diagram
Arg-2-naphthylamide + H2O
Arg + 2-naphthylamine
show the reaction diagram
-
-
-
-
?
Arg-4-nitroanilide + H2O
Arg + 4-nitroaniline
show the reaction diagram
-
-
-
ir
Arg-7-amido-4-methylcoumarin + H2O
Arg + 7-amino-4-methylcoumarin
show the reaction diagram
Arg-Arg-4-methylcoumaryl-7-amide + H2O
Arg + Arg-4-methylcoumaryl-7-amide
show the reaction diagram
-
-
-
ir
Arg-Arg-Lys-Ala-Leu-Ser-Pro + H2O
Arg + Arg-Lys-Ala-Leu-Ser-Pro
show the reaction diagram
-
-
-
ir
Arg-Gly-Tyr-Ser-Leu-Gly + H2O
Arg + Gly-Tyr-Ser-Leu-Gly
show the reaction diagram
-
-
-
ir
Arg-Val + H2O
Arg + Val
show the reaction diagram
-
-
-
ir
Arg-Val-OMe + H2O
Arg + Val-OMe
show the reaction diagram
-
-
-
ir
Arg-Val-Tyr-Ile-His-Pro-Phe + H2O
Arg + Val-Tyr-Ile-His-Pro-Phe
show the reaction diagram
-
-
-
ir
L-alanyl-L-alanine 4-nitroanilide + H2O
L-alanine + L-alanine 4-nitroanilide
show the reaction diagram
-
L-alanine 4-nitroanilide accumulates very fast in the reaction mixture, and the L-alanine 4-nitroanilide/4-nitroaniline ratio diminishes from 123 at 5 min to 69 at 25 min, therefore indicating that the enzyme is mostly cleaving the substrate to L-alanine 4-nitroanilide, and then also this last product to give 4-nitroaniline
-
-
?
L-alanyl-L-alanyl-L-alanine 4-nitroanilide + H2O
L-alanine + L-alanyl-L-alanine 4-nitroanilide
show the reaction diagram
-
L-alanyl-L-alanine 4-nitroanilide is produced, but also consumed by the enzyme while 4-nitroaniline is generated after a lag phase. At 26 min the ratios L-alanyl-L-alanine 4-nitroaniline/4-nitroaniline and L-alanyl 4-nitroanilide/4-nitroaniline are 8 and 33 respectively
-
-
?
L-arginine 4-nitroanilide + H2O
L-arginine + 4-nitroaniline
show the reaction diagram
L-glutamate 4-nitroanilide + H2O
L-glutamate + 4-nitroaniline
show the reaction diagram
-
20.1% of the activity compared to L-lysine 4-nitroanilide
-
-
?
L-leucine 4-nitroanilide + H2O
L-leucine + 4-nitroaniline
show the reaction diagram
L-leucine p-nitroanilide + H2O
L-leucine + p-nitroaniline
show the reaction diagram
-
-
-
-
?
L-lysine 4-nitroanilide + H2O
L-lysine + 4-nitroaniline
show the reaction diagram
L-lysyl-4-nitroanilide + H2O
L-lysine + 4-nitroaniline
show the reaction diagram
-
maximal hydrolysis rates are obtained when lysine is in the N-position (Lys-pNA)
-
-
?
L-proline 4-nitroanilide + H2O
L-proline + 4-nitroaniline
show the reaction diagram
6% of the activity compared to Lys-4-nitroanilide, recombinant enzyme
-
-
?
Leu-4-nitroanilide + H2O
Leu + 4-nitroaniline
show the reaction diagram
-
-
-
ir
Leu-7-amido-4-methylcoumarin + H2O
Leu + 7-amino-4-methylcoumarin
show the reaction diagram
Leu-Arg-Arg-Ala-Ser-Leu-Gly + H2O
Leu + Arg-Arg-Ala-Ser-Leu-Gly
show the reaction diagram
-
-
-
ir
Leu-Leu + H2O
Leu + Leu
show the reaction diagram
-
-
-
ir
Leu-Leu-OMe + H2O
Leu + Leu-OMe
show the reaction diagram
-
-
-
ir
Lys-4-nitroanilide + H2O
Lys + 4-nitroaniline
show the reaction diagram
Lys-7-amido-4-methylcoumarin + H2O
Lys + 7-amino-4-methylcoumarin
show the reaction diagram
Lys-Ala + H2O
Lys + Ala
show the reaction diagram
-
-
-
?
Lys-Ala-4-methylcoumaryl-7-amide + H2O
Lys + Ala-4-methylcoumaryl-7-amide
show the reaction diagram
-
-
-
ir
Lys-Gly-Gly + H2O
Lys + Gly-Gly
show the reaction diagram
-
-
-
?
Lys-Gly-Gly-Lys + H2O
Lys + Gly-Gly-Lys
show the reaction diagram
-
-
-
?
Lys-Leu + H2O
Lys + Leu
show the reaction diagram
-
-
-
?
Lys-Lys-Lys + H2O
Lys + Lys-Lys
show the reaction diagram
-
-
-
?
Lys-Lys-Lys-Lys + H2O
Lys + Lys-Lys-Lys
show the reaction diagram
-
-
-
?
Lys-Phe + H2O
Lys + Phe
show the reaction diagram
-
-
-
?
Met-7-amido-4-methylcoumarin + H2O
Met + 7-amino-4-methylcoumarin
show the reaction diagram
Met-Ala-Ser + H2O
Met + Ala-Ser
show the reaction diagram
-
-
-
ir
Met-Arg-Phe + H2O
Met + Arg-Phe
show the reaction diagram
-
-
-
ir
Met-Gly-Gly + H2O
Met + Gly-Gly
show the reaction diagram
-
-
-
ir
Pro-Phe-Arg-4-methylcoumaryl-7-amide + H2O
Pro + Phe-Arg-4-methylcoumaryl-7-amide
show the reaction diagram
-
-
-
ir
Ser-7-amido-4-methylcoumarin + H2O
Ser + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
ir
Tyr-Gly-Gly-Phe-Leu + H2O
Tyr + Gly-Gly-Phe-Leu
show the reaction diagram
-
-
-
ir
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Cu2+
-
can partly replace Co2+
KCl
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the enzyme is optimally active at salt concentration between 0.075 and 0.25 M KCl. More than 70% of the activity is maintained at 2 M KCl
Ni2+
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can partly replace Co2+
Zn2+
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native protein
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10 phenanthroline
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1,10-phenanthroline
amastatin
antipain
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19% inhibition at 0.05 mg/ml
bestatin
Ca2+
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1 mM,% inhibition
Cd2+
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1 mM,% inhibition
CHAPS buffer
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chymostatin
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1 mM, 22% inhibition
Co2+
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25fold enhancement of hydrolysis of Arg-7-amido-4-methylcoumarin and Lys-7-amido-4-methylcoumarin. Hydrolysis of substrates longer than tripeptide or dipeptide-7-amido-4-methylcoumarin is inhibited, IC50: 0.1 mM
diphosphate
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93% inhibition at 1 mM
dithiothreitol
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94% inhibition at 1 mM
EGTA
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99.9% inhibition at 1 mM
leupeptin
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Mg2+
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1 mM,% inhibition
p-chloromercuribenzoic acid
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81% inhibition at 0.1 mM
pefabloc
Triphosphate
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99.9% inhibition at 1 mM
additional information
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the enzyme is insensitive to the papain and trypsin inhibitor antipain, to the cysteine proteases inhibitor E-64, to the serine and cysteine proteases inhibitor leupeptin, to the aspartate proteases inhibitor pepstatin, and to the metalloendopeptidases inhibitor phosphoramidon. Puromycin, an inhibitor of some exopeptidases, has practically no effect on the activity of PhTET3
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.4
L-arginine 4-nitroanilide
pH 8.0, 100C, recombinant enzyme
4 - 4.6
L-lysine 4-nitroanilide
0.00086
L-Lysyl-4-nitroanilide
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-
1.8 - 2.7
Lys-Gly-Gly
additional information
L-lysine 4-nitroanilide
-
KM-value as a function of pressure
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
769
L-arginine 4-nitroanilide
Pyrococcus furiosus
Q8TZW4
pH 8.0, 100C, recombinant enzyme
1260 - 1840
L-lysine 4-nitroanilide
305 - 1460
Lys-Gly-Gly
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
550
L-arginine 4-nitroanilide
Pyrococcus furiosus
Q8TZW4
pH 8.0, 100C, recombinant enzyme
42478
274 - 460
L-lysine 4-nitroanilide
15355
169 - 540
Lys-Gly-Gly
13632
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.1
Co2+
Saccharomyces cerevisiae
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25fold enhancement of hydrolysis of Arg-7-amido-4-methylcoumarin and Lys-7-amido-4-methylcoumarin. Hydrolysis of substrates longer than tripeptide or dipeptide-7-amido-4-methylcoumarin is inhibited, IC50: 0.1 mM
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.2
-
minimum, substrate-dependent
43.32
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maximum, substrate-dependent
220
pH 8.0, 100C, 0.2 mM Co2+, purified enzyme from Pyrococcus furiosus
1900
pH 8.0, 100C, 0.2 mM Co2+, purified enzyme from Pyrococcus furiosus
additional information
-
substrate-dependent
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.8
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assay with Arg-beta-naphthylamide
7.5
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in presence of cobalt
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 8.5
-
pH 6: about 50% of maximal activity, pH 8.0: about 90% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
100
activity of enzyme from Pyrococcus furiosus and recombinant enzyme increase from 40C to 100C
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60 - 100
at 60C the recombinant enzyme shows about 35% of the activity at 100C. At 60C the enzyme from Pyrococcus furiosus shows about 60% of the activity at 100C
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10000
-
gel filtration
38214
4 * 38214, calculated from sequence
53000
-
calculated from amino acid sequence, SDS-PAGE after removal of sugar chains
75000
-
molecular form b, proform, gel filtration
97000
-
SDS-PAGE
160000
gel filtration
500000
-
dodecameric complex, gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dodecamer
monomer
tetramer
4 * 38214, calculated from sequence; 4 * 40000, SDS-PAGE
trimer
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
proteolytic modification
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
the 12-subunit PhTET3 complex is crystallized and its 3D structure is solved at a resolution of 1.9 A by molecular replacement
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x-ray crystal structure of the Co(II)-loaded form ([CoCo(AAP)]) is solved to 2.2 A resolution. [CoCo(AAP)] folds into an alpha/beta globular domain with a twisted beta-sheet hydrophobic core sandwiched between alpha-helices, identical to [ZnZn(AAP)]. Tris(hydroxymethyl)aminomethane coordinates to the dinuclear Co(II) active site of AAP with one of the Tris hydroxyl oxygen atoms (O4) forming a single oxygen atom bridge between the two Co(II) ions. This is the only Tris atom coordinated to the metals with Co1-O and Co2-O bonds distances of 2.2 and 1.9 A, respectively. Each of the Co(II) ions resides in a distorted trigonal bipyramidal geometry
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 9
-
-
683483
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
80
-
half-life: 17.83 min
90
-
half-life: 3.44 min
95
-
half-life: 55.1 min
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
high robustness of the oligomeric enzyme under high pressure of up to 300 MPa at 25C as well as at 90C
-
the enzyme is stable and functional under hypersaline conditions
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
by selective fractionation with ammonium sulfate and anion exchange, hydrophobic interaction and gel filtration chromatography
-
native and recombinant enzyme
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli, correspondence between gene and enzyme confirmed by gene-disruption-study
-
the recombinant protein containing a polyhistidine tag at the N terminus is produced in Escherichia coli
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
LapB mutant NU322 (defective for lapB gene) shows a complete loss of lysine aminopeptidase activity and a partial reduction in arginine aminopeptidase activity. When an intact copy of lapB is reintroduced into NU322 aminopeptidase activity is restored
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