BRENDA - Enzyme Database
show all sequences of 3.4.24.28

Purification and characterization of a new metallo-neutral protease for beer brewing from Bacillus amyloliquefaciens SYB-001

Wang, J.; Xu, A.; Wan, Y.; Li, Q.; Appl. Biochem. Biotechnol. 170, 2021-2033 (2013)

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
Tween-20
1.61fold activation at 50 mM
Bacillus amyloliquefaciens
Tween-80
1.34fold activation at 50 mM
Bacillus amyloliquefaciens
Application
Application
Commentary
Organism
food industry
in the beer brewing process, the neutral protease during mashing process can release more amino acids from wort such as aspartic acid, arginine, methione, and histidine, resulting in a better amino acid profile in wort
Bacillus amyloliquefaciens
Inhibitors
Inhibitors
Commentary
Organism
Structure
2-mercaptoethanol
27% inhibition at 50 mM
Bacillus amyloliquefaciens
Ba2+
88% inhibition at 10 mM
Bacillus amyloliquefaciens
Cu2+
30% inhibition at 10 mM
Bacillus amyloliquefaciens
dithio-bis-nitrobenzoic acid
64% inhibition at 50 mM
Bacillus amyloliquefaciens
dithiothreitol
70% inhibition at 50 mM
Bacillus amyloliquefaciens
EDTA
complete inhibition at 50 mM, can be reversed by Zn2+
Bacillus amyloliquefaciens
Fe2+
86% inhibition at 10 mM
Bacillus amyloliquefaciens
Fe3+
98% inhibition at 10 mM
Bacillus amyloliquefaciens
SDS
37% inhibition at 50 mM
Bacillus amyloliquefaciens
Triton X-100
slight inhibition at 50 mM
Bacillus amyloliquefaciens
Zn2+
19% inhibition at 10 mM
Bacillus amyloliquefaciens
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
purified enzyme, Km value of 3.97 mg/ml and Vmax value of 657 U/mg/min of substrate casein
Bacillus amyloliquefaciens
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Ca2+
activates 20% at 10 mM
Bacillus amyloliquefaciens
Li+
activates 20% at 10 mM
Bacillus amyloliquefaciens
Mg2+
activates 20% at 10 mM
Bacillus amyloliquefaciens
Mn2+
activates 2.90fold at 10 mM
Bacillus amyloliquefaciens
Zn2+
a zinc metalloprotease
Bacillus amyloliquefaciens
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
36800
-
x * 37000, SDS-PAGE, x * 36800, about, mass spectrometry
Bacillus amyloliquefaciens
37000
-
x * 37000, SDS-PAGE, x * 36800, about, mass spectrometry
Bacillus amyloliquefaciens
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
casein + H2O
Bacillus amyloliquefaciens
-
?
-
-
?
casein + H2O
Bacillus amyloliquefaciens SYB-001
-
?
-
-
?
Organism
Organism
UniProt
Commentary
Textmining
Bacillus amyloliquefaciens
-
isolated from soil
-
Bacillus amyloliquefaciens SYB-001
-
isolated from soil
-
Purification (Commentary)
Purification (Commentary)
Organism
native extracellular enzyme 5.6fold from culture supernatant by ammonium sulfate fractionation, anion exchange and hydrophobic interaction chromatography, and gel filtration
Bacillus amyloliquefaciens
Specific Activity [micromol/min/mg]
Specific Activity Minimum [mol/min/mg]
Specific Activity Maximum [mol/min/mg]
Commentary
Organism
11280
-
purified native enzyme, pH 7.0, 40C
Bacillus amyloliquefaciens
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
casein + H2O
-
733130
Bacillus amyloliquefaciens
?
-
-
-
?
casein + H2O
-
733130
Bacillus amyloliquefaciens SYB-001
?
-
-
-
?
Subunits
Subunits
Commentary
Organism
?
x * 37000, SDS-PAGE, x * 36800, about, mass spectrometry
Bacillus amyloliquefaciens
Synonyms
Synonyms
Commentary
Organism
metallo-neutral protease
-
Bacillus amyloliquefaciens
Neutral protease
-
Bacillus amyloliquefaciens
Temperature Optimum [C]
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
50
-
-
Bacillus amyloliquefaciens
Temperature Range [C]
Temperature Minimum [C]
Temperature Maximum [C]
Commentary
Organism
30
70
activity range, 41% of maximal activity at 30C, 50% at 70C
Bacillus amyloliquefaciens
Temperature Stability [C]
Temperature Stability Minimum [C]
Temperature Stability Maximum [C]
Commentary
Organism
40
50
purified extracellular enzyme, pH 7.0, about 70% activity remaining after 60 min, rapid loss of activity above 60C
Bacillus amyloliquefaciens
60
-
purified extracellular enzyme, pH 7.0, loss of over 80% activity after 10 min, inactivation after 60 min
Bacillus amyloliquefaciens
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7
-
-
Bacillus amyloliquefaciens
pH Range
pH Minimum
pH Maximum
Commentary
Organism
6
10
-
Bacillus amyloliquefaciens
pH Stability
pH Stability
pH Stability Maximum
Commentary
Organism
4
5
purified extracellular enzyme, 50C, loss of 70% activity after 60 min
Bacillus amyloliquefaciens
6
-
purified extracellular enzyme, 50C, no loss of activity after 60 min, stable at
Bacillus amyloliquefaciens
7
-
purified extracellular enzyme, 50C, loss of 20% activity after 60 min
Bacillus amyloliquefaciens
8
10
purified extracellular enzyme, 50C, loss of 40% activity after 60 min
Bacillus amyloliquefaciens
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
Tween-20
1.61fold activation at 50 mM
Bacillus amyloliquefaciens
Tween-80
1.34fold activation at 50 mM
Bacillus amyloliquefaciens
Application (protein specific)
Application
Commentary
Organism
food industry
in the beer brewing process, the neutral protease during mashing process can release more amino acids from wort such as aspartic acid, arginine, methione, and histidine, resulting in a better amino acid profile in wort
Bacillus amyloliquefaciens
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
2-mercaptoethanol
27% inhibition at 50 mM
Bacillus amyloliquefaciens
Ba2+
88% inhibition at 10 mM
Bacillus amyloliquefaciens
Cu2+
30% inhibition at 10 mM
Bacillus amyloliquefaciens
dithio-bis-nitrobenzoic acid
64% inhibition at 50 mM
Bacillus amyloliquefaciens
dithiothreitol
70% inhibition at 50 mM
Bacillus amyloliquefaciens
EDTA
complete inhibition at 50 mM, can be reversed by Zn2+
Bacillus amyloliquefaciens
Fe2+
86% inhibition at 10 mM
Bacillus amyloliquefaciens
Fe3+
98% inhibition at 10 mM
Bacillus amyloliquefaciens
SDS
37% inhibition at 50 mM
Bacillus amyloliquefaciens
Triton X-100
slight inhibition at 50 mM
Bacillus amyloliquefaciens
Zn2+
19% inhibition at 10 mM
Bacillus amyloliquefaciens
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
purified enzyme, Km value of 3.97 mg/ml and Vmax value of 657 U/mg/min of substrate casein
Bacillus amyloliquefaciens
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Ca2+
activates 20% at 10 mM
Bacillus amyloliquefaciens
Li+
activates 20% at 10 mM
Bacillus amyloliquefaciens
Mg2+
activates 20% at 10 mM
Bacillus amyloliquefaciens
Mn2+
activates 2.90fold at 10 mM
Bacillus amyloliquefaciens
Zn2+
a zinc metalloprotease
Bacillus amyloliquefaciens
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
36800
-
x * 37000, SDS-PAGE, x * 36800, about, mass spectrometry
Bacillus amyloliquefaciens
37000
-
x * 37000, SDS-PAGE, x * 36800, about, mass spectrometry
Bacillus amyloliquefaciens
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
casein + H2O
Bacillus amyloliquefaciens
-
?
-
-
?
casein + H2O
Bacillus amyloliquefaciens SYB-001
-
?
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
native extracellular enzyme 5.6fold from culture supernatant by ammonium sulfate fractionation, anion exchange and hydrophobic interaction chromatography, and gel filtration
Bacillus amyloliquefaciens
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [mol/min/mg]
Specific Activity Maximum [mol/min/mg]
Commentary
Organism
11280
-
purified native enzyme, pH 7.0, 40C
Bacillus amyloliquefaciens
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
casein + H2O
-
733130
Bacillus amyloliquefaciens
?
-
-
-
?
casein + H2O
-
733130
Bacillus amyloliquefaciens SYB-001
?
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
?
x * 37000, SDS-PAGE, x * 36800, about, mass spectrometry
Bacillus amyloliquefaciens
Temperature Optimum [C] (protein specific)
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
50
-
-
Bacillus amyloliquefaciens
Temperature Range [C] (protein specific)
Temperature Minimum [C]
Temperature Maximum [C]
Commentary
Organism
30
70
activity range, 41% of maximal activity at 30C, 50% at 70C
Bacillus amyloliquefaciens
Temperature Stability [C] (protein specific)
Temperature Stability Minimum [C]
Temperature Stability Maximum [C]
Commentary
Organism
40
50
purified extracellular enzyme, pH 7.0, about 70% activity remaining after 60 min, rapid loss of activity above 60C
Bacillus amyloliquefaciens
60
-
purified extracellular enzyme, pH 7.0, loss of over 80% activity after 10 min, inactivation after 60 min
Bacillus amyloliquefaciens
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7
-
-
Bacillus amyloliquefaciens
pH Range (protein specific)
pH Minimum
pH Maximum
Commentary
Organism
6
10
-
Bacillus amyloliquefaciens
pH Stability (protein specific)
pH Stability
pH Stability Maximum
Commentary
Organism
4
5
purified extracellular enzyme, 50C, loss of 70% activity after 60 min
Bacillus amyloliquefaciens
6
-
purified extracellular enzyme, 50C, no loss of activity after 60 min, stable at
Bacillus amyloliquefaciens
7
-
purified extracellular enzyme, 50C, loss of 20% activity after 60 min
Bacillus amyloliquefaciens
8
10
purified extracellular enzyme, 50C, loss of 40% activity after 60 min
Bacillus amyloliquefaciens
Other publictions for EC 3.4.24.28
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
Synonyms
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)
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Rudakova
Features of gene expression o ...
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884-891
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-
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-
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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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Erban
Feces derived allergens of ty ...
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Front. Physiol.
7
53
2016
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1
-
-
-
-
-
-
-
-
-
-
-
1
-
-
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1
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-
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-
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-
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754796
Bavaro
Immobilization of neutral pro ...
Bacillus subtilis
Molecules
21
E1621
2016
-
1
-
-
-
1
-
-
-
-
-
-
3
3
-
-
-
-
-
-
-
-
-
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2
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1
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1
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3
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-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
733469
Saxena
MALDI-TOF MS and CD spectral a ...
Bacillus cereus, Bacillus cereus B80
BioMed Res. Int.
2015
527015
2015
-
-
1
-
-
-
-
1
-
1
1
-
1
2
-
-
1
-
-
-
1
-
11
1
-
1
1
4
-
1
1
2
-
-
-
-
-
-
1
-
-
-
-
-
-
-
1
-
1
1
-
1
-
-
1
-
-
1
-
11
1
1
1
4
-
1
1
2
-
-
1
1
-
-
-
733978
Guinane
-
Generation of the antimicrobia ...
Bacillus subtilis
Int. Dairy J.
49
1-7
2015
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
1
-
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1
-
4
1
-
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1
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1
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
734363
Hatta
-
Bacillolysin, papain, and subt ...
Bacillus amyloliquefaciens
J. Cereal Sci.
61
41-47
2015
-
1
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
1
-
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-
1
-
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-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
733130
Wang
Purification and characterizat ...
Bacillus amyloliquefaciens, Bacillus amyloliquefaciens SYB-001
Appl. Biochem. Biotechnol.
170
2021-2033
2013
2
1
-
-
-
-
11
1
-
5
2
2
-
4
-
-
1
-
-
-
1
-
2
1
2
1
1
2
-
1
1
4
-
-
-
-
2
1
-
-
-
-
-
-
11
-
1
-
5
2
2
-
-
-
1
-
-
1
-
2
1
1
1
2
-
1
1
4
-
-
-
-
-
-
-
733167
Luo
Bacillus thuringiensis metallo ...
Bacillus thuringiensis, Bacillus thuringiensis YBT-1518
Appl. Environ. Microbiol.
79
460-468
2013
-
-
1
-
-
-
8
-
-
3
-
2
-
5
-
-
1
-
-
-
-
-
4
-
1
1
1
-
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1
1
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1
-
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8
-
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3
-
2
-
-
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1
-
-
-
-
4
-
1
1
-
-
1
1
-
-
-
2
2
-
-
-
733545
Zhu
Optimization of neutral protea ...
Bacillus subtilis, Bacillus subtilis DES-59
Biotechnol. Appl. Biochem.
60
336-342
2013
-
-
-
-
-
-
-
-
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-
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7
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4
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4
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-
-
718012
Niu
Overexpression of the key viru ...
Hathewaya histolytica, Paenibacillus polymyxa
J. Mol. Microbiol. Biotechnol.
21
130-137
2011
-
-
-
-
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-
-
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2
-
2
-
-
10
-
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2
-
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6
2
5
2
-
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2
-
2
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2
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6
2
2
-
-
-
-
-
-
-
-
-
-
-
-
-
711482
Duerrschmidt
Refolding of the non-specific ...
Geobacillus stearothermophilus
Biophys. Chem.
147
66-73
2010
-
-
-
-
1
1
-
-
-
2
-
-
-
2
-
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1
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2
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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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2
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-
-
-
-
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-
-
-
717233
Rudakova
Characteristics of a novel sec ...
Bacillus intermedius
Biochemistry (Moscow)
75
1294-1301
2010
-
-
1
-
-
-
10
1
1
3
1
-
-
3
-
-
1
-
-
-
7
-
8
1
1
1
1
-
1
1
-
-
-
-
1
-
-
-
1
-
-
-
-
-
10
-
1
1
3
1
-
-
-
-
1
-
-
7
-
8
1
1
1
-
1
1
-
-
1
-
1
1
-
-
-
701210
Zhang
Expression, purification, and ...
Geobacillus stearothermophilus
Sci. China C Life Sci.
51
52-59
2008
-
-
1
-
-
-
-
-
-
-
1
-
-
4
-
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1
-
-
-
1
-
1
1
-
1
-
1
-
1
2
-
-
-
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-
1
-
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-
1
-
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1
-
-
1
-
1
1
1
-
1
-
1
2
-
-
-
-
-
-
-
-
685711
Mansfeld
The stability of engineered th ...
Geobacillus stearothermophilus
Biotechnol. Bioeng.
97
672-679
2007
-
-
-
-
1
-
-
-
-
-
-
-
7
1
-
-
-
-
-
-
8
-
2
-
-
3
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Niu
A neutral protease from Bacill ...
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668546
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An engineered disulfide bridge ...
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669317
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Bacillolysin MA, a novel bacte ...
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1
1
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3
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670771
Mansfeld
The propeptide is not required ...
Geobacillus stearothermophilus
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651101
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Differentiation between confor ...
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1
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650655
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Rendering one autolysis site i ...
Bacillus subtilis
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4
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31162
Tsuru
Zinc protease of Bacillus subt ...
Bacillus subtilis
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1993
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31151
Holland
Structural comparison suggests ...
Bacillus cereus
Biochemistry
31
11310-11316
1992
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31166
Paberit
-
Inhibition of thermolysin and ...
Brevibacillus brevis
Quant. Struct. -Act. Relat.
11
28-33
1992
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1
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31157
Stoeva
Primary structure of a zinc pr ...
Bacillus pumilus, Bacillus pumilus 76
Biochemistry
29
527-534
1990
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31158
Pauptit
Crystal structure of neutral p ...
Bacillus cereus
J. Mol. Biol.
199
525-537
1988
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31154
Sidler
The primary structure of Bacil ...
Bacillus cereus, Bacillus subtilis
Biol. Chem. Hoppe-Seyler
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1986
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31156
Takagi
Nucleotide sequence and promot ...
Geobacillus stearothermophilus
J. Bacteriol.
163
824-831
1985
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31155
Vasantha
Genes for alkaline protease an ...
Bacillus amyloliquefaciens
J. Bacteriol.
159
811-819
1984
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31161
Yang
Cloning of the neutral proteas ...
Bacillus subtilis
J. Bacteriol.
160
15-21
1984
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31163
Sidler
-
Isolation procedures for therm ...
Geobacillus stearothermophilus
Eur. J. Appl. Microbiol. Biotechnol.
10
197-209
1980
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31112
Holmquist
Esterase activity of zinc neut ...
Bacillus subtilis
Biochemistry
15
101-107
1976
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3
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31165
Sidler
Neutral proteases with differe ...
Geobacillus stearothermophilus
FEBS Lett.
25
292-294
1972
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31159
Feder
Bacillus cereus neutral protea ...
Bacillus cereus
Biochim. Biophys. Acta
251
74-78
1971
-
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2
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1
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2
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1
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1
1
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8
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1
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1
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1
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8
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31160
Millet
Specificity of megateriopeptid ...
Bacillus megaterium
Eur. J. Biochem.
9
456-462
1969
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31150
Morihara
Comparison of the specificitie ...
Bacillus subtilis
Arch. Biochem. Biophys.
123
572-588
1968
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