Information on EC 3.4.11.22 - aminopeptidase I

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

EC NUMBER
COMMENTARY hide
3.4.11.22
-
RECOMMENDED NAME
GeneOntology No.
aminopeptidase I
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
Release of an N-terminal amino acid, preferably a neutral or hydrophobic one, from a polypeptide. Aminoacyl-arylamides are poor substrates
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
CAS REGISTRY NUMBER
COMMENTARY hide
9031-94-1
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain ATCC 42249, single copy lap gene
SwissProt
Manually annotated by BRENDA team
giant alga
-
-
Manually annotated by BRENDA team
marine psychrophile, strain 34H
-
-
Manually annotated by BRENDA team
strain NIB 8924
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Morimus funereus
2 enzyme forms
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
strain BY4741
-
-
Manually annotated by BRENDA team
isozyme ERAP1 and ERAP2
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
AAEAAG-NH2 + H2O
L-Ala + AEAAG-NH2
show the reaction diagram
-
-
-
-
?
AAVVAAG-NH2 + H2O
L-Ala + AVVAAG-NH2
show the reaction diagram
-
-
-
-
?
AEAA-NH2 + H2O
L-Ala + EAA-NH2
show the reaction diagram
-
-
-
-
?
Ala 2-naphthylamide + H2O
Ala + 2-naphthylamine
show the reaction diagram
-
-
-
-
Ala 4-nitroanilide + H2O
Ala + 4-nitroaniline
show the reaction diagram
-
-
-
-
Ala-4-nitroanilide + H2O
Ala + 4-nitroaniline
show the reaction diagram
Ala-Ala-Pro-Tyr-Lys-amide + H2O
Ala + Ala-Pro-Tyr-Lys-amide
show the reaction diagram
Ala-beta-naphthylamide + H2O
Ala + beta-naphthylamine
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
-
-
-
-
Arg-4-nitroanilide + H2O
Arg + 4-nitroaniline
show the reaction diagram
-
-
?
Asp 2-naphthylamide + H2O
Asp + 2-naphthylamine
show the reaction diagram
-
very slight activity
-
-
Asp-4-nitroanilide + H2O
Asp + 4-nitroaniline
show the reaction diagram
-
-
-
?
AYWANATRSG-D-Ala + H2O
L-Ala + AYWANATRSG-D-Ala
show the reaction diagram
-
-
-
-
?
AYWANATRSGA + H2O
L-Ala + YWANATRSGA
show the reaction diagram
-
high activity compared to other peptide substrates
-
-
?
azocasein + H2O
protein fragments of azocasein of MW 71 kDa, 83 kDa, and 22 kDa
show the reaction diagram
-
-
-
-
?
Cystinyl 4-nitroanilide + H2O
Cystine + 4-nitroaniline
show the reaction diagram
-
-
-
-
DRVYIHPFHL + H2O
L-Asp + L-Arg + VYIHPFHL
show the reaction diagram
-
angiotensin I
-
-
?
E-cadherin + H2O
?
show the reaction diagram
-
-
-
-
?
EAA-NH2 + H2O
L-Glu + AA-NH2
show the reaction diagram
-
-
-
-
?
EFAPGNYPAD + H2O
L-Glu + FAPGNYPAD
show the reaction diagram
-
low activity compared to other peptide substrates
-
-
?
EFAPGNYPAK + H2O
L-Glu + FAPGNYPAK
show the reaction diagram
-
low activity compared to other peptide substrates
-
-
?
EFAPGNYPAL + H2O
L-Glu + FAPGNYPAL
show the reaction diagram
-
high activity compared to other peptide substrates
-
-
?
GDRIYVH + H2O
?
show the reaction diagram
-
-
-
-
?
Glu 4-nitroanilide + H2O
Glu + 4-nitroaniline
show the reaction diagram
-
-
-
-
Glu-4-nitroanilide + H2O
Glu + 4-nitroaniline
show the reaction diagram
Glu-Ala-Pro-Tyr-Lys-amide + H2O
Glu + Ala-Pro-Tyr-Lys-amide
show the reaction diagram
Gly 4-nitroanilide + H2O
Gly + 4-nitroaniline
show the reaction diagram
-
-
-
-
Gly-4-nitroanilide + H2O
Gly + 4-nitroaniline
show the reaction diagram
Gly-Ala-Pro-Tyr-Lys-amide + H2O
Gly + Ala-Pro-Tyr-Lys-amide
show the reaction diagram
Gly-Leu-Tyr + H2O
Gly + Leu-Tyr
show the reaction diagram
-
-
-
-
?
HSDAVFTDNYTRLRKQMAVKKYLNSILN + H2O
His + SDAVFTDNYTRLRKQM + AVKKYLN + SILN
show the reaction diagram
-
protein VIP
-
-
?
Ile-4-nitroanilide + H2O
Ile + 4-nitroaniline
show the reaction diagram
-
-
-
?
L-Ala-4-nitroanilide + H2O
L-Ala + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
L-Ala-7-amido-4-methylcoumarin + H2O
L-Ala + 7-amino-4-methylcoumarin
show the reaction diagram
L-Ala-Ala-Pro-Leu-4-nitroanilide + H2O
L-Ala-Ala-Pro-Leu + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
L-Ala-Gly + H2O
L-Ala + Gly
show the reaction diagram
-
-
-
-
-
L-Ala-Gly-Gly + H2O
?
show the reaction diagram
-
-
-
-
-
L-Ala-L-Asp-L-Phe methyl ester + H2O
?
show the reaction diagram
-
-
-
-
-
L-Ala-L-Leu + H2O
L-Ala + L-Leu
show the reaction diagram
-
-
-
-
-
L-Ala-L-Thr-Gly methyl ester + H2O
?
show the reaction diagram
-
-
-
-
-
L-Ala-L-Thr-L-Ala + H2O
?
show the reaction diagram
-
-
-
-
-
L-Ala-L-Thr-L-Ala methyl ester + H2O
?
show the reaction diagram
-
-
-
-
-
L-Ala-p-nitroanilide + H2O
L-Ala + p-nitroaniline
show the reaction diagram
-
preferred substrate
-
-
?
L-Arg-4-nitroanilide + H2O
L-Arg + 4-nitroaniline
show the reaction diagram
L-Arg-7-amido-4-methylcoumarin + H2O
L-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
L-Arg-L-Phe + H2O
L-Arg + L-Phe
show the reaction diagram
-
-
-
-
?
L-Arg-p-nitroanilide + H2O
L-Arg + p-nitroaniline
show the reaction diagram
-
-
-
-
?
L-Leu-2-naphthylamide + H2O
L-Leu + 2-naphthylamine
show the reaction diagram
-
preferred substrate
-
-
?
L-Leu-4-nitroanilide + H2O
L-Leu + 4-nitroaniline
show the reaction diagram
L-Leu-7-amido-4-methylcoumarin + H2O
L-Leu + 7-amino-4-methylcoumarin
show the reaction diagram
L-Leu-Gly + H2O
L-Leu + Gly
show the reaction diagram
-
-
-
-
-
L-Leu-Gly-Gly + H2O
?
show the reaction diagram
-
-
-
-
-
L-Leu-L-Ala + H2O
L-Leu + L-Ala
show the reaction diagram
-
-
-
-
-
L-Leu-L-Leu + H2O
L-Leu + L-Leu
show the reaction diagram
-
-
-
-
-
L-Leu-L-Phe + H2O
L-Leu + L-Phe
show the reaction diagram
-
-
-
-
?
L-Leu-p-nitroanilide + H2O
L-Leu + p-nitroaniline
show the reaction diagram
-
-
-
-
?
L-leucine 4-nitroanilide + H2O
L-leucine + 4-nitroaniline
show the reaction diagram
-
-
-
?
L-leucine-4-anisidide + H2O
L-leucine + anisidine
show the reaction diagram
-
-
-
?
L-leucine-4-methylcoumaryl-7-amide + H2O
L-leucine + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
L-leucine-anilide + H2O
L-leucine + aniline
show the reaction diagram
-
-
-
?
L-Lys-2-naphthylamide + H2O
L-Lys + 2-naphthylamine
show the reaction diagram
-
low activity
-
-
?
L-Lys-4-nitroanilide + H2O
L-Lys + 4-nitroaniline
show the reaction diagram
L-Met-4-nitroanilide + H2O
L-Met + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
L-Met-7-amido-4-methylcoumarin + H2O
L-Met + 7-amino-4-methylcoumarin
show the reaction diagram
L-Met-L-Phe + H2O
L-Met + L-Phe
show the reaction diagram
-
-
-
-
?
L-Phe-4-nitroanilide + H2O
L-Phe + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
L-Phe-7-amido-4-methylcoumarin + H2O
L-Phe + 7-amino-4-methylcoumarin
show the reaction diagram
L-Phe-Gly + H2O
L-Phe + Gly
show the reaction diagram
-
-
-
-
-
L-Phe-Gly-Gly + H2O
?
show the reaction diagram
-
-
-
-
-
L-Phe-L-Ala + H2O
L-Phe + L-Ala
show the reaction diagram
-
-
-
-
?
L-Phe-L-Arg + H2O
L-Phe + L-Arg
show the reaction diagram
-
-
-
-
?
L-Phe-L-Ile + H2O
L-Phe + L-Ile
show the reaction diagram
-
-
-
-
?
L-Phe-L-Leu + H2O
L-Phe + L-Leu
show the reaction diagram
-
-
-
-
?
L-Phe-L-Met + H2O
L-Phe + L-Met
show the reaction diagram
-
-
-
-
?
L-Phe-L-Met-D-Arg-L-Phe-NH2 + H2O
L-Phe + L-Phe-L-Met-D-Arg-NH2
show the reaction diagram
-
-
-
-
?
L-Phe-L-Met-L-Arg-L-Phe-NH2 + H2O
L-Phe + L-Phe-L-Met-L-Arg-NH2
show the reaction diagram
-
bioactive molluscan cardioexcitatory neuropeptide
-
-
?
L-Phe-L-Phe + H2O
L-Phe + L-Phe
show the reaction diagram
-
best substrate
-
-
?
L-Phe-L-Trp + H2O
L-Phe + L-Trp
show the reaction diagram
-
-
-
-
?
L-Phe-L-Tyr + H2O
L-Phe + L-Tyr
show the reaction diagram
-
-
-
-
?
L-Tyr-7-amido-4-methylcoumarin + H2O
L-Tyr + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
L-Tyr-L-Phe + H2O
L-Tyr + L-Phe
show the reaction diagram
-
-
-
-
?
L-Val-4-nitroanilide + H2O
L-Val + 4-nitroaniline
show the reaction diagram
-
low activity
-
-
?
Leu 2-naphthylamide + H2O
Leu + 2-naphthylamine
show the reaction diagram
-
-
-
-
Leu 4-nitroanilide + H2O
Leu + 4-nitroaniline
show the reaction diagram
Leu-4-nitroanilide + H2O
Leu + 4-nitroaniline
show the reaction diagram
Leu-Ala-Pro-Tyr-Lys-amide + H2O
Leu + Ala-Pro-Tyr-Lys-amide
show the reaction diagram
Leu-beta-naphthylamide + H2O
Leu + beta-naphthylamine
show the reaction diagram
-
-
-
-
?
leucine enkephalin + H2O
?
show the reaction diagram
-
recombinant enzyme, release of Tyr, Gly, Phe and Leu
-
?
Lys 2-naphthylamide + H2O
Lys + 2-naphthylamine
show the reaction diagram
-
-
-
-
Lys 4-nitroanilide + H2O
Lys + 4-nitroaniline
show the reaction diagram
-
-
-
-
Lys-4-nitroanilide + H2O
Lys + 4-nitroaniline
show the reaction diagram
Met 4-nitroanilide + H2O
Met + 4-nitroaniline
show the reaction diagram
-
-
-
-
Met-4-nitroanilide + H2O
Met + 4-nitroaniline
show the reaction diagram
occludin + H2O
?
show the reaction diagram
-
-
-
-
?
Phe 2-naphthylamide + H2O
Phe + 2-naphthylamine
show the reaction diagram
-
-
-
-
Phe 4-nitroanilide + H2O
Phe + 4-nitroaniline
show the reaction diagram
-
-
-
-
Phe-4-nitroanilide + H2O
Phe + 4-nitroaniline
show the reaction diagram
-
-
?
Pro 2-naphthylamide + H2O
Pro + 2-naphthylamine
show the reaction diagram
-
-
-
-
Pro 4-nitroanilide + H2O
Pro + 4-nitroaniline
show the reaction diagram
-
-
-
-
Pro-4-nitroanilide + H2O
Pro + 4-nitroaniline
show the reaction diagram
low activity
-
?
Pro-Ala-Pro-Tyr-Lys-amide + H2O
Pro + Ala-Pro-Tyr-Lys-amide
show the reaction diagram
QITANRELIQQEL + H2O
? + TANRELIQQEL
show the reaction diagram
-
-
intermediate product TANRELIQQEL is further processed
-
?
QLESIINFEK + H2O
L-Gln + LESIINFEK
show the reaction diagram
-
low activity compared to other peptide substrates
-
-
?
QLESIINFEKA + H2O
L-Gln + LESIINFEKA
show the reaction diagram
-
high activity compared to other peptide substrates
-
-
?
QLESIINFEKD + H2O
L-Gln + LESIINFEKD
show the reaction diagram
-
low activity compared to other peptide substrates
-
-
?
QLESIINFEKK + H2O
L-Gln + LESIINFEKK
show the reaction diagram
-
low activity compared to other peptide substrates
-
-
?
QLESIINFEKL + H2O
L-Gln + LESIINFEKL
show the reaction diagram
-
best peptide substrate
-
-
?
QLESIINFEKL-amide + H2O
L-Gln + LESIINFEKL-amide
show the reaction diagram
-
high activity compared to other peptide substrates
-
-
?
QLESIINFEKR + H2O
L-Gln + LESIINFEKR
show the reaction diagram
-
low activity compared to other peptide substrates
-
-
?
QLESIINFEKY + H2O
L-Gln + LESIINFEKY
show the reaction diagram
-
high activity compared to other peptide substrates
-
-
?
QLESIINFELK + H2O
L-Gln + LESIINFELK
show the reaction diagram
-
-
-
-
?
RPKPQQFFGLM + H2O
RPKPQ + QFF + GLM
show the reaction diagram
-
substance P
-
-
?
RPPGFSPFR + H2O
Arg + PPGF + SPFR
show the reaction diagram
-
bradykinin
-
-
?
S-Benzoyl-Cys 4-nitroanilide + H2O
S-Benzoyl-Cys + 4-nitroaniline
show the reaction diagram
-
-
-
-
Ser 2-naphthylamide + H2O
Ser + 2-naphthylamine
show the reaction diagram
-
-
-
-
SIINFEKL + H2O
L-Ser + IINFEKL
show the reaction diagram
-
-
-
-
?
thionoleucine-4-anisidide + H2O
thionoleucine + anisidine
show the reaction diagram
-
-
-
?
thionoleucine-S-anilide + H2O
thionoleucine + aniline
show the reaction diagram
-
-
-
?
TTQRTRALV-NH2 + H2O
L-Thr + TQRTRALV-NH2
show the reaction diagram
-
-
-
-
?
Tyr 2-naphthylamide + H2O
Tyr + 2-naphthylamine
show the reaction diagram
-
-
-
-
Val 2-naphthylamide + H2O
Val + 2-naphthylamine
show the reaction diagram
-
slight activity
-
-
Val 4-nitroanilide + H2O
Val + 4-nitroaniline
show the reaction diagram
-
-
-
-
Val-4-nitroanilide + H2O
Val + 4-nitroaniline
show the reaction diagram
WEVYEKCALK + H2O
L-Trp + EVYEKCALK
show the reaction diagram
-
-
-
-
?
WRVYEKCALK + H2O
L-Trp + RVYEKCALK
show the reaction diagram
-
-
-
-
?
WRVYEKMALKC + H2O
L-Trp + RVYEKMALKC
show the reaction diagram
-
-
-
-
?
additional information
?
-
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
Br-
-
activation
Cd2+
-
the bimetallic enzyme contains eihter 2 Zn2+ or 2 Cd2+ or Zn2+ and Cd2+
Mg2+
-
22% activation at 10
NaCl
-
absolutely required for activity
Zinc
-
1 atom per enzyme molecule, contains the HEXXH motif
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10 phenanthroline
1,10-phenanthroline
1-ethyl-3-(3-dimethylaminopropyl)carbodiimide
-
inactivation by modification of pK 5.8 carboxylate, presence arginine hydroxamate decreases inhibitory potency, hydroxylamine does not recover enzyme activity
1-Phenyl-2-thiourea
-
competitive
2,2'-dipyridyl
-
-
2,3-Dimercaptopropanol
-
-
actinonin
-
-
amastatin
arginine hydroxamate
-
competitive
Arphamenine A
-
-
Arphamenine B
-
-
bestatin
captopril
-
-
chymostatin
-
39% residual activity at 0.1 mM
crystal delta-endotoxin from Bacillus thuringiensis
-
-
-
diethyldicarbonate
-
inactivation by modification of an imidazole, presence of arginine hydroxamate decreases inhibitory potency, hydroxylamine partially recovers enzyme activity after inactivation
dipicolinic acid
97% inhibition at 5 mM, Mg2+, Zn2+, and Co2+ partly protect
Heavy metals
Morimus funereus
-
-
-
Hg2+
-
99% inhibition at 1 mM, recombinant enzyme
iodoacetate
-
-
leucinethiol
leuhistin
-
-
matlystatin A
-
-
Methionine hydroxamate
-
competitive
N-(hydroxyethyl)iminodiacetic acid
-
i.e. Himda
N-p-tosyl-L-lysine chloromethyl ketone
-
64% residual activity at 0.1 mM
N-p-tosyl-L-phenylalanine chloromethyl ketone
-
8% residual activity at 0.1 mM
N-tosyl-L-Phe chloromethyl ketone
-
slightly inhibitory
Ni2+
-
89% inhibition at 1 mM
nitriloacetic acid
-
-
nitrobestatin
-
95.1% inhibition at 0.133 mM
o-phenanthroline
p-chloromercuribenzoate
-
-
phebestin
-
i.e. [(2S,3R)-3-amino-2-hydroxy-4-phenylbutanoyl-L-valyl]-L-phenylalanine
Phenylglyoxal
-
-
Phenylmethylsulfonylfluoride
-
6% residual activity at 1 mM
probestin
-
-
puromycin
-
-
RB 101(S)
-
-
Tetranitromethane
-
changes the Km of the enzyme without affecting Vmax by modifying a phenol group, presence arginine hydroxamate decreases inhibitory potency
Tris
-
chelated to active site Zn2+
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
EGTA
Morimus funereus
-
-
ethanol
Morimus funereus
-
-
methanol
Morimus funereus
-
-
tert-butanol
-
20% activation at 10% at 20-90C
additional information
-
the enzyme is cold-active
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
6.7
Ala beta-naphthylamide
-
pH 7.5, 21C, native enzyme
3.5 - 14
Ala-4-nitroanilide
12
Ala-Gly-Gly
-
-
14
Ala-Gly-Gly ethyl ester
-
-
3.2
Ala-Thr-Ala
-
-
2.7
Ala-Thr-Ala methyl ester
-
-
0.253
AYWANATRSG-D-Ala
-
pH 7.5, 37C
0.09
AYWANATRSGA
-
pH 7.5, 37C
0.0225
Cystinyl 4-nitroanilide
-
-
1.325
EFAPGNYPAD
-
pH 7.5, 37C
1.5
EFAPGNYPAK
-
pH 7.5, 37C
0.148
EFAPGNYPAL
-
pH 7.5, 37C
1.5
Glu-4-nitroanilide
-
pH 7.5, 21C, recombinant enzyme
51
Ile-4-nitroanilide
-
pH 7.5, 21C, recombinant enzyme
0.043 - 0.072
L-Ala-Ala-Pro-Leu-4-nitroanilide
0.4
L-Ala-p-nitroanilide
-
in 50 mM Tris-HCl, pH 8.1, at 30C
0.35
L-Leu-4-nitroanilide
-
pH 8.5, 65C
45
L-leucin-anilide
-
pH 8.0, 25C, enzyme with Zn2+ and Cd2+ bound
4.6 - 15
L-leucine 4-nitroanilide
32 - 50
L-leucine-4-anisidide
61 - 78
L-leucine-anilide
0.31
L-Phe-4-nitroanilide
-
pH 8.5, 65C
0.09
L-Val-4-nitroanilide
-
pH 8.5, 65C
7
Leu-4-nitroanilide
-
pH 7.5, 21C, recombinant enzyme
7
Leu-Gly-Leu
-
-
9
Lys-4-nitroanilide
-
pH 7.5, 21C, recombinant enzyme
15
Pro-4-nitroanilide
-
pH 7.5, 21C, recombinant enzyme
0.124
QLESIINFEKA
-
pH 7.5, 37C
0.7
QLESIINFEKD
-
pH 7.5, 37C
0.8
QLESIINFEKK
-
pH 7.5, 37C
0.124
QLESIINFEKL
-
pH 7.5, 37C
0.138
QLESIINFEKL-amide
-
pH 7.5, 37C
0.91
QLESIINFEKR
-
pH 7.5, 37C
0.111
QLESIINFEKY
-
pH 7.5, 37C
4 - 7
thionoleucine-4-anisidide
4 - 11
thionoleucine-S-anilide
13
Val-4-nitroanilide
-
pH 7.5, 21C, recombinant enzyme
0.328
WEVYEKCALK
-
at 37C
0.075
WRVYEKCALK
-
at 37C
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.68 - 138
Ala-4-nitroanilide
3.13 - 4.34
Ala-Ala-Pro-Tyr-Lys-amide
0.52
Ala-beta-naphthylamide
Novosphingobium capsulatum
-
pH 7.5, 21C, native enzyme
33300
Ala-Thr-Ala
Saccharomyces cerevisiae
-
-
0.13
Glu-4-nitroanilide
Aspergillus oryzae
-
pH 7.5, 21C, recombinant enzyme
0.72 - 6.08
Glu-Ala-Pro-Tyr-Lys-amide
0.88 - 6.08
Gly-Ala-Pro-Tyr-Lys-amide
0.18
Ile-4-nitroanilide
Aspergillus oryzae
-
pH 7.5, 21C, recombinant enzyme
0.043 - 0.36
L-Ala-Ala-Pro-Leu-4-nitroanilide
1.43
L-Leu-4-nitroanilide
Grifola frondosa
-
pH 8.5, 65C
3 - 60
L-leucine 4-nitroanilide
3.8 - 9.5
L-leucine-4-anisidide
6.3 - 16
L-leucine-anilide
0.95
L-Phe-4-nitroanilide
Grifola frondosa
-
pH 8.5, 65C
0.02
L-Val-4-nitroanilide
Grifola frondosa
-
pH 8.5, 65C
3.5
Leu-4-nitroanilide
Aspergillus oryzae
-
pH 7.5, 21C, recombinant enzyme
3.13 - 3.67
Leu-Ala-Pro-Tyr-Lys-amide
1.8
Lys-4-nitroanilide
Aspergillus oryzae
-
pH 7.5, 21C, recombinant enzyme
0.08
Pro-4-nitroanilide
Aspergillus oryzae
-
pH 7.5, 21C, recombinant enzyme
6.17
Pro-Ala-Pro-Tyr-Lys-amide
Aspergillus oryzae
-
pH 7.5, 21C, recombinant enzyme
7.5 - 12.2
thionoleucine-4-anisidide
7.7 - 23.3
thionoleucine-S-anilide
0.1
Val-4-nitroanilide
Aspergillus oryzae
-
pH 7.5, 21C, recombinant enzyme
additional information
Pro-Ala-Pro-Tyr-Lys-amide
Aspergillus oryzae
-
pH 7.5, 21C, recombinant enzyme
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.2
1,10-phenanthroline
-
pH 7.8, 37C
0.24
1-Phenyl-2-thiourea
-
pH 8.0, 25C
0.6
arginine hydroxamate
-
pH 7.8, 30C
0.11
bestatin
-
pH 7.3, 37C
0.7
EDTA
-
pH 7.8, 37C, in presence of 1,10-phenanthroline
4.2
ferrocyanide
-
pH 7.5, 21C
11
iodate
-
pH 7.5, 21C
0.047
phebestin
-
pH 7.3, 37C
3
phosphate
-
pH 7.5, 21C
4.6
Urea
-
pH 8.0, 25C
0.02
Zn2+
-
pH 7.5, 37C
additional information
additional information
-
inhibition kinetics
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.16
-
pollen extract, in 50 mM Tris-HCl, pH 8.1, at 30C
2.6
-
substrate L-Phe-L-Phe
3 - 8
-
UV-irradiation of cultures increases specific activity
4.12
-
with Leu-4-nitroanilide as substrate, measurement of absorption
4.88
-
after 30.5fold purification, in 50 mM Tris-HCl, pH 8.1, at 30C
6.7
-
purified enzyme
8.55
-
purified enzyme
105
-
purified native enzyme, substrate Ala-4-nitroanilide
425
-
purified recombinant enzyme
980
-
substrate Leu-Gly-Gly
3000
-
substrate Ala-Thr-Ala
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6
-
substrate Leu 2-naphthylamide
6 - 6.5
-
absence of activators
7 - 8
-
substrate Ala 2-naphthylamide
7 - 9
Morimus funereus
-
-
7 - 8
-
substrate cystinyl 4-nitroanilide
7 - 8.5
-
presence of Zn2+ and Cl-
7.5
-
assay at
7.5 - 8
-
with substrate L-Leu-4-nitroanilide
7.5
-
assay at
9.2 - 9.5
-
with substrate Gly-Leu-Tyr
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 9
-
no activity at pH 4 and pH 9, about 33% of maximal activity at pH 6
5 - 8.3
-
pH profile
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
-
assay at room temprature
60
-
recombinant enzyme
90
-
with substrate L-Leu-4-nitroanilide
additional information
-
the enzyme is cold-active
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2 - 60
Morimus funereus
-
broad range
10 - 45
-
-
50 - 80
more than 80% of maximal activity at this range
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.7
-
sequence calculation
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
glycosylated enzyme form
Manually annotated by BRENDA team
-
the enzyme exists in a membrane and a soluble variant with slightly differing substrate specificities and thermostabilities
-
Manually annotated by BRENDA team
additional information
PDB
SCOP
CATH
ORGANISM
UNIPROT
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
27000
-
gel filtration
30000
-
1 * 30000, SDS-PAGE
36500
-
12 * 36500, heterododecamer with two types of subunits with similar MW, the enzyme shows different hybrid types, overview, the enzymatic activity of the alpha-subunit differs from that of the beta-subunit
37000
x * 37000, SDS-PAGE, x * 41061, amino acid sequence calculation
41061
x * 37000, SDS-PAGE, x * 41061, amino acid sequence calculation
42000
-
1 * 42000, SDS-PAGE
43000
-
gel filtration
44000
-
x * 62000 + x * 44000, SDS-PAGE
44500
-
x * 44500, recombinant enzyme, SDS-PAGE
45000
-
x * 45000, SDS-PAGE
50000
-
12 * 50000, the active enzyme is a homododecameric complex of about 600 kDa, and dissociation into two hexamers leads to loss of enzymatic activity
51000
-
12 * 51000, SDS-PAGE
51950
-
x * 56000, deglycosylated recombinant enzyme, SDS-PAGE, x * 51950, mature enzyme, amino acid sequence calculation
52000
-
gel filtration, non-denaturing PAGE
56000
-
x * 56000, deglycosylated recombinant enzyme, SDS-PAGE, x * 51950, mature enzyme, amino acid sequence calculation
60000
-
SDS-PAGE
62000
-
x * 62000 + x * 44000, SDS-PAGE
66000
-
x * 66000, SDS-PAGE
71000
-
gel filtration
72000
-
native PAGE
74000
-
native PAGE
84000
-
1 * 84000, SDS-PAGE
85000 - 90000
-
unglycosylated active enzyme form, gel filtration
93000
-
gel filtration
97634
-
1 * 97634, amino acid sequence calculation
98000
-
SDS-PAGE
100000
105000
120000
-
gel permeation chromatography
140000
-
glycosylated active enzyme form, gel filtration
200000
-
SDS-PAGE
320000
-
hexameric form, sucrose density gradient centrifugation
400000
610000
-
sucrose density gradient centrifugation
640000
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dodecamer
hexamer
homododecamer
-
12 * 50000, the active enzyme is a homododecameric complex of about 600 kDa, and dissociation into two hexamers leads to loss of enzymatic activity
monomer
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
no glycoprotein
proteolytic modification
additional information
-
the zymogen is unglycosylated
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
sitting drop vapor diffusion method
-
sitting drop vapour diffusion method with 0.1 M Tris-HCl pH 6.5, 30% polyethylene glycol 400, 0.1 M MgCl2 and 1.1 M NaCl
-
16 mg/ml enzyme complexed with inhibitory Tris, in 10 mM Tris, pH 8.0, 10 mM KSCN, 0.4 NaCl, vapour diffusion method, with precipitant solution containing 100 mM Tris, pH 8.0, 100 mM KSCN, 4.5 M NaCl, 48 h, X-ray diffraction structure determination and analysis at 1.2 A resolution
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 11
-
4C, 3 weeks, 10% loss of activity
28298
6 - 10.5
-
60 min, purified enzyme, stable
664347
7.5 - 9
-
-
680333
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25 - 60
-
40% activity at 25C, no activity above 60C
40
-
half-life is 38 min
55
-
60 min, purified enzyme, stable
70
-
20 min, 65% residual activity, compared to the activity at 37C
75
-
20 min, 46% residual activity, compared to the activity at 37C
80
-
loss of 20% activity within 30 min, stable for several hours
additional information
-
the apo- and cobalt-free enzyme is thermolabile
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Glycerol
-
effectively stabilized in 50% glycerol at -10C and below
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4C, 50 mM Tris-HCl buffer, pH 7.2, 38% loss of activity after 4 days, 81% loss of activity after 11 days
-
4C, aqueous enzyme solution, in presence of Brij 35, pH 6.0-9.0, stable for a few days
-
frozen, 50 mM ammonium acetate buffer, pH 6.2
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
aminopeptidase yscXVI
-
ammonium sulfate precipitation, ion-exchange chromatography and gel filtration
-
DEAE-Sephacel column chromatography, ammonium sulfate precipitation, Superdex 200 gel filtration, HiTrap Q column chromatography, and arginine-Sepharose column chromatography
-
from culture medium, hydroxyapatite chromatography, immobilized metal ion affinity chromatography (Co2+)
-
from culture medium, immobilized metal ion affinity chromatography (Ni2+), gel filtration
-
from culture supernatant
-
further purification of commercial kidney enzyme preparation by affinity and hydrophobic interaction chromatography
-
further purification of the commercial preparation, to homogeneity
glutathione Sepharose 4B column chromatography, Superdex 200 gel filtration, Superdex 75 gel filtration, and Resource RPC column chromatography
-
immobilized metal ion affinity chromatography (Ni2+)
-
isolation of homogeneous dodecameric enzyme
-
native enzyme 178fold to homogeneity by ammonium sulfate fractionation, hydrophobic interaction chromatography, gel filtration, and ion exchange chromatography
-
native enzyme 19fold
-
native enzyme 460fold to homogeneity by ion exchange and hydroxy apatite chromatography, and ion exchange chromatography
-
native enzyme 96fold from pollen by a seven-step procedure comprising ammonium sulfate fractionation, 2 steps of anion exchange chromatography, gel filtration, and hydrophobic interaction chromatography
-
native enzyme either 331fold by ammonium sulfate fractionation, heat precipitation, gel filtration, ion exchange and adsorption chromatography, or by a single step anion exchange chromatography process
-
native from culture supernatant
-
native soluble enzyme from chloroplast stroma to homogeneity by chlorplast preparation, ammonium sulfate fractionation, hydrophobic interaction chromatography, gel filtration, and ion exchange chromatography
-
Ni-NTA column chromatography, MonoQ column chromatography, and Superdex S200 gel filtration
-
partially
partially, preparation of spores and subcellular fractionation
recombinant His-tagged enzyme from Escherichia coli, 9.2fold to homogeneity
-
recombinant wild-type and mutant precursor enzymes
-
Sephadex G-200 gel filtration
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, expression in Bacillus subtilis and Escherichia coli
-
DNA and amino acid sequence determination and analysis, functional overexpression in Fusarium venenatum and Aspergillus oryzae
-
DNA and amino acid sequence determination and analysis, phylogenetic analysis
-
DNA and amino acid sequence determination and analysis, subcloning and expression in Escherichia coli, phylogenetic comparison to other organisms
expressed in Escherichia coli BL21(DE3) cells
-
expressed in insect cells driven by a baculoviral vector
-
expressed in Sf9 insect cells
-
expression in RAW264.7 cell
-
gene APE1, DNA and amino acid sequence determination and analysis, single copy gene, expression of wild-type and mutant precursor enzymes in yeast
-
gene APE1, DNA and amino acid sequence determination and analysis, transcription is regulated by growth phase and by carbon source
-
gene APE2, DNA and amino acid sequence determination and analysis, genetic structure
-
His-tagged protein expressed in insect cells
-
overexpression in Escherichia coli as His-tagged enzyme
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
human cytomegalovirus downregulates expression during viral infection
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K528R
-
less efficient in peptide processing suggesting a defect in the catalytic process, also a naturally occuring mutation associated with reduced ankylosing spondylitis risk
E354Q
-
inactive, Zn2+ binding site disrupted
Q181E
-
different substrate specificity, cleaves basic amino acid residues preferentially
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
nutrition
-
the enzyme is useful to reduce bitterness of food products by hydrolysis of peptides with hydrophobic amino acids causing the bitter taste