BRENDA - Enzyme Database show
show all sequences of 3.4.11.22

Bacillus aminopeptidase I

Motoshima, H.; Kaminogawa, S.; Handbook of Proteolytic Enzymes (Barrett, J. ; Rawlings, N. D. ; Woessner, J. F. , eds) 1, 968-970 (2004)
No PubMed abstract available

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
tert-butanol
20% activation at 10% at 20-90°C
Geobacillus stearothermophilus
Inhibitors
Inhibitors
Commentary
Organism
Structure
EDTA
10 mM, no inhibition at pH 8.1, but conversion into the apoenzyme at pH 6.0
Geobacillus stearothermophilus
Urea
at 8 M, inhibition of 7% of the enzyme activity with Gly-Leu-Tyr, but 75% of the activity with L-Leu-4-nitroanilide
Geobacillus stearothermophilus
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
membrane
the enzyme exists in a membrane and a soluble variant with slightly differing substrate specificities and thermostabilities
Geobacillus stearothermophilus
16020
-
soluble
the enzyme exists in a membrane and a soluble variant with slightly differing substrate specificities and thermostabilities
Geobacillus stearothermophilus
-
-
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Co2+
binding results in much higher activity compared to Zn2+, Co2+ or Zn2+ is required for maximal activity, metallopeptidase
Geobacillus stearothermophilus
Zn2+
binding results in much lower activity compared to Co2+, very tight binding, Co2+ or Zn2+ is required for maximal activity, metallopeptidase
Geobacillus stearothermophilus
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
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
Geobacillus stearothermophilus
400000
-
sedimentation equilibrium centrifugation analysis
Geobacillus stearothermophilus
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Geobacillus stearothermophilus
-
-
-
Purification (Commentary)
Commentary
Organism
native enzyme 19fold
Geobacillus stearothermophilus
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Gly-Leu-Tyr + H2O
-
665108
Geobacillus stearothermophilus
Gly + Leu-Tyr
-
-
-
?
L-Leu-4-nitroanilide + H2O
substrate of the alpha-subunit, but not of the beta-subunit
665108
Geobacillus stearothermophilus
L-Leu + 4-nitroaniline
-
-
-
?
additional information
the alpha-subunits hydrolyzes peptides with neutral N-terminal amino acids while the beta-subunit acts on peptides with acidic N-terminal Glu or Asp residues
665108
Geobacillus stearothermophilus
?
-
-
-
-
Subunits
Subunits
Commentary
Organism
dodecamer
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
Geobacillus stearothermophilus
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
65
-
with substrate Gly-Leu-Tyr
Geobacillus stearothermophilus
90
-
with substrate L-Leu-4-nitroanilide
Geobacillus stearothermophilus
Temperature Stability [°C]
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
additional information
-
the apo- and cobalt-free enzyme is thermolabile
Geobacillus stearothermophilus
80
-
loss of 20% activity within 30 min, stable for several hours
Geobacillus stearothermophilus
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
8
with substrate L-Leu-4-nitroanilide
Geobacillus stearothermophilus
9.2
9.5
with substrate Gly-Leu-Tyr
Geobacillus stearothermophilus
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
tert-butanol
20% activation at 10% at 20-90°C
Geobacillus stearothermophilus
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
EDTA
10 mM, no inhibition at pH 8.1, but conversion into the apoenzyme at pH 6.0
Geobacillus stearothermophilus
Urea
at 8 M, inhibition of 7% of the enzyme activity with Gly-Leu-Tyr, but 75% of the activity with L-Leu-4-nitroanilide
Geobacillus stearothermophilus
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
membrane
the enzyme exists in a membrane and a soluble variant with slightly differing substrate specificities and thermostabilities
Geobacillus stearothermophilus
16020
-
soluble
the enzyme exists in a membrane and a soluble variant with slightly differing substrate specificities and thermostabilities
Geobacillus stearothermophilus
-
-
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Co2+
binding results in much higher activity compared to Zn2+, Co2+ or Zn2+ is required for maximal activity, metallopeptidase
Geobacillus stearothermophilus
Zn2+
binding results in much lower activity compared to Co2+, very tight binding, Co2+ or Zn2+ is required for maximal activity, metallopeptidase
Geobacillus stearothermophilus
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
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
Geobacillus stearothermophilus
400000
-
sedimentation equilibrium centrifugation analysis
Geobacillus stearothermophilus
Purification (Commentary) (protein specific)
Commentary
Organism
native enzyme 19fold
Geobacillus stearothermophilus
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Gly-Leu-Tyr + H2O
-
665108
Geobacillus stearothermophilus
Gly + Leu-Tyr
-
-
-
?
L-Leu-4-nitroanilide + H2O
substrate of the alpha-subunit, but not of the beta-subunit
665108
Geobacillus stearothermophilus
L-Leu + 4-nitroaniline
-
-
-
?
additional information
the alpha-subunits hydrolyzes peptides with neutral N-terminal amino acids while the beta-subunit acts on peptides with acidic N-terminal Glu or Asp residues
665108
Geobacillus stearothermophilus
?
-
-
-
-
Subunits (protein specific)
Subunits
Commentary
Organism
dodecamer
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
Geobacillus stearothermophilus
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
65
-
with substrate Gly-Leu-Tyr
Geobacillus stearothermophilus
90
-
with substrate L-Leu-4-nitroanilide
Geobacillus stearothermophilus
Temperature Stability [°C] (protein specific)
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
additional information
-
the apo- and cobalt-free enzyme is thermolabile
Geobacillus stearothermophilus
80
-
loss of 20% activity within 30 min, stable for several hours
Geobacillus stearothermophilus
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
8
with substrate L-Leu-4-nitroanilide
Geobacillus stearothermophilus
9.2
9.5
with substrate Gly-Leu-Tyr
Geobacillus stearothermophilus
Other publictions for EC 3.4.11.22
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
732014
Goto
Substrate-dependent nitric oxi ...
Mus musculus
J. Biochem.
157
439-449
2015
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732285
Aldhamen
Autoimmune disease-associated ...
Homo sapiens
J. Innate Immun.
7
275-289
2015
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731234
Chen
Critical role of endoplasmic r ...
Homo sapiens
Arthritis Rheum.
66
284-294
2014
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732737
Aldhamen
Endoplasmic reticulum aminopep ...
Mus musculus
PLoS ONE
8
e69539
2013
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717825
Goto
Secretion of endoplasmic retic ...
Mus musculus
J. Biol. Chem.
286
21906-21914
2011
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718148
Kim
Human cytomegalovirus microRNA ...
Homo sapiens
Nat. Immunol.
12
984-991
2011
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718329
Kochan
Crystal structures of the endo ...
Homo sapiens
Proc. Natl. Acad. Sci. USA
108
7745-7750
2011
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1
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707156
Tsui
Association of an ERAP1 ERAP2 ...
Homo sapiens
Ann. Rheum. Dis.
69
733-736
2010
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707111
Evnouchidou
A continuous fluorigenic assay ...
Homo sapiens
Anal. Biochem.
395
33-40
2009
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2
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707315
Maksymowych
Association of a specific ERAP ...
Homo sapiens
Arthritis Rheum.
60
1317-1323
2009
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707657
Adamis
Lap4, a vacuolar aminopeptidas ...
Saccharomyces cerevisiae, Saccharomyces cerevisiae BY4741
Biometals
22
243-249
2009
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708255
Evnouchidou
A new role for Zn(II) aminopep ...
Mus musculus
Curr. Pharm. Des.
15
3656-3670
2009
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13
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708650
Johnson
The ERAP2 gene is associated w ...
Homo sapiens
Hum. Genet.
126
655-666
2009
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681600
Chen
Peptide hydrolysis by the binu ...
Vibrio proteolyticus
J. Phys. Chem. B
112
2494-2500
2008
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700001
Schu
Aminopeptidase I enzymatic act ...
Saccharomyces cerevisiae
Methods Enzymol.
451
67-78
2008
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677369
Adachi
Crystallization of Saccharomyc ...
Saccharomyces cerevisiae
Acta Crystallogr. Sect. F
63
200-203
2007
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678993
Tishinov
-
Isolation and characterization ...
Helianthus annuus
C. R. Acad. Bulg. Sci.
60
1007-1010
2007
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679310
Kostecka
-
Partial purification of larval ...
Musca domestica
Collect. Symp. Ser. Academy Sci. Czech Republic
9
66-68
2007
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666422
Hammer
The aminopeptidase ERAAP shape ...
Mus musculus
Nat. Immunol.
7
103-112
2006
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666760
York
Endoplasmic reticulum aminopep ...
Mus musculus
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2006
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680333
Cortes
Purification of a novel aminop ...
Parietaria judaica
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2
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9
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1
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1
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1
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665275
Nagata
Characteristics of an aminopep ...
Cryptomeria japonica
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5445-5448
2005
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5
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2
1
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1
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16
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1
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1
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666737
Chang
The ER aminopeptidase, ERAP1, ...
Sus scrofa
Proc. Natl. Acad. Sci. USA
102
17107-17112
2005
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1
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22
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1
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1
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663693
Huston
Purification, characterization ...
Colwellia psychrerythraea
Appl. Environ. Microbiol.
70
3321-3328
2004
1
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1
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3
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6
1
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4
3
1
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665104
Caprioglio
-
Yeast aminopeptidases Ape2, Aa ...
Saccharomyces cerevisiae
Handbook of Proteolytic Enzymes (Barrett, J. ; Rawlings, N. D. ; Woessner, J. F. , eds)
1
316-318
2004
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7
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1
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7
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1
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6
1
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-
1
-
-
-
-
-
-
665106
Suarez-Rendueles
-
Aminopeptidase I ...
Saccharomyces cerevisiae
Handbook of Proteolytic Enzymes (Barrett, J. ; Rawlings, N. D. ; Woessner, J. F. , eds)
1
940-941
2004
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1
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1
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2
2
2
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2
2
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1
-
-
-
-
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-
665108
Motoshima
-
Bacillus aminopeptidase I ...
Geobacillus stearothermophilus
Handbook of Proteolytic Enzymes (Barrett, J. ; Rawlings, N. D. ; Woessner, J. F. , eds)
1
968-970
2004
1
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2
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3
1
2
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2
-
2
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650891
Bozic
Partial purification and chara ...
Morimus funereus
Comp. Biochem. Physiol. B
134
231-241
2003
3
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2
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1
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1
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1
-
1
1
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1
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-
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650924
Kuo
Overexpression, purification, ...
Geobacillus stearothermophilus, Geobacillus stearothermophilus NIB 8924
Curr. Microbiol.
47
40-45
2003
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1
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10
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1
1
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4
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1
1
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1
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6
1
1
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1
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1
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10
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1
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1
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1
-
6
1
1
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1
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-
-
-
-
-
-
-
-
650142
Bienvenue
Hydrolysis of thionopeptides b ...
Vibrio proteolyticus
Biochemistry
41
3712-3719
2002
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-
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2
16
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3
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1
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1
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5
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1
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18
1
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2
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2
2
16
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3
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1
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5
-
1
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18
1
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-
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650364
Chien
Purification, characterization ...
Aspergillus sojae
Biochim. Biophys. Acta
1576
119-126
2002
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1
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1
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8
2
1
1
2
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1
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1
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2
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1
2
2
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1
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1
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8
2
1
1
2
-
1
1
-
-
-
-
-
-
-
-
653895
Desmarais
The 1.20 A resolution crystal ...
Vibrio proteolyticus
Structure
10
1063-1072
2002
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1
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1
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-
-
-
-
-
-
-
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665257
Noguchi
Isolation and characterization ...
Cryptomeria japonica
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50
3540-3543
2002
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4
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2
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2
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1
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2
1
1
5
1
1
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1
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2
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4
2
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2
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1
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2
1
1
5
1
1
-
-
-
1
-
-
-
-
-
-
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-
666143
Millership
Characterization of aminopepti ...
Encephalitozoon cuniculi, Encephalitozoon hellem
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843-848
2002
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2
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2
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10
-
2
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7
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2
2
2
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2
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2
-
-
10
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
652119
Byun
Aminopeptidase from Sphingomon ...
Novosphingobium capsulatum
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276
17902-17907
2001
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1
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5
2
2
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1
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1
1
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1
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20
1
1
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2
3
1
-
-
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3
-
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1
-
-
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5
3
2
2
2
1
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1
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1
-
20
1
1
-
2
3
1
-
-
-
-
-
-
-
-
-
664347
Nishiwaki
Purification and characterizat ...
Grifola frondosa
Biosci. Biotechnol. Biochem.
65
424-427
2001
-
1
-
-
-
-
9
3
-
1
2
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1
-
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1
-
-
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1
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4
1
1
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1
3
1
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1
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1
-
-
-
-
-
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9
-
3
-
1
2
-
-
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1
-
-
1
-
4
1
1
-
1
3
1
-
1
-
-
-
-
-
-
-
665255
Byun
Synergistic action of an X-pro ...
Aspergillus oryzae
J. Agric. Food Chem.
49
2061-2063
2001
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-
-
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2
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2
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1
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1
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-
-
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-
-
-
-
-
2
-
1
-
-
-
1
-
-
-
-
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-
-
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665476
Andrei-Selmer
A new class of mutants deficie ...
Saccharomyces cerevisiae
J. Biol. Chem.
276
11606-11614
2001
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1
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1
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-
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2
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1
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1
1
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-
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1
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1
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1
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2
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1
1
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-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
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650310
Cristofoletti
The role of amino acid residue ...
Tenebrio molitor
Biochim. Biophys. Acta
1479
185-195
2000
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11
1
2
1
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1
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1
1
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2
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1
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1
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1
1
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4
-
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-
-
-
-
-
-
-
11
4
1
2
1
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-
-
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1
-
2
-
-
1
-
-
1
-
-
1
1
-
-
-
-
-
-
-
-
650315
Blinkovsky
A non-specific aminopeptidase ...
Aspergillus oryzae
Biochim. Biophys. Acta
1480
171-181
2000
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1
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3
7
1
1
2
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4
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1
1
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-
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2
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12
1
1
-
2
18
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
3
-
7
1
1
2
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-
1
1
-
-
2
-
12
1
1
-
2
18
1
-
-
-
-
-
-
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-
665822
Desimone
Purification and characterizat ...
Hordeum vulgare
J. Chromatogr. B
737
285-293
2000
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3
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1
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1
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1
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6
1
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-
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-
-
-
-
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3
-
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1
1
2
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1
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1
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6
1
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28283
Klionsky
Nonclassical protein sorting t ...
Saccharomyces cerevisiae
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273
10807-10810
1998
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1
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28284
Martinez
Folding of the presequence of ...
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1124-1138
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1
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28285
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Transport of a large oligomeri ...
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3
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28286
Scott
Aminopeptidase I is targeted t ...
Saccharomyces cerevisiae
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28287
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Identification of a cytoplasm ...
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28288
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In vitro reconstitution of cyt ...
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28289
Segui-Real
Yeast aminopeptidase I is post ...
Saccharomyces cerevisiae
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28290
Tisljar
Purification and characterizat ...
Saccharomyces cerevisiae
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Cueva
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Moriyasu
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Hetz
Interaction of chloride with y ...
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Röhm.
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Schwencke
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Löffler
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Metz
The quarternary structure of y ...
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Metz
Yeast aminopeptidase I. Chemic ...
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