BRENDA - Enzyme Database
show all sequences of 4.1.1.11

Molecular engineering of L-aspartate-alpha-decarboxylase for improved activity and catalytic stability

Pei, W.; Zhang, J.; Deng, S.; Tigu, F.; Li, Y.; Li, Q.; Cai, Z.; Li, Y.; Appl. Microbiol. Biotechnol. 101, 6015-6021 (2017)

Data extracted from this reference:

Cloned(Commentary)
Cloned (Commentary)
Organism
gene panD, recombinant expression of N-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3), the recombinant ADC protein is mainly in its inactive uncleaved form, possibly because of insufficience of panZ, an activator involved in the cleavage of ADCE
Escherichia coli
gene panD, recombinant expression of N-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3). The cleavage of the recombinant ADC protein from Bacillus subtilis after expression in Escherichia coli is almost complete
Bacillus subtilis
gene panD, recombinant expression of N-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3). The cleavage of the recombinant ADC protein from Corynebacteriums glutamicum after expression in Escherichia coli is almost complete
Corynebacterium glutamicum
Engineering
Protein Variants
Commentary
Organism
I188M
site-directed mutagenesis, the mutant shows increased thermostability compared to the wild-type
Bacillus subtilis
additional information
mutation of nucleotide L127 increases the enzyme's thermostability compared to the wild-type, while mutation of nuclotide V68 does not significantly affect the thermostability
Bacillus subtilis
Inhibitors
Inhibitors
Commentary
Organism
Structure
additional information
enzyme ADC is also subject to mechanism-based inactivation, which has been reported for many other pyruvoyl-dependent. Mechanism-based inactivation only occurs during catalysis
Bacillus subtilis
additional information
enzyme ADC is also subject to mechanism-based inactivation, which has been reported for many other pyruvoyl-dependent. Mechanism-based inactivation only occurs during catalysis
Corynebacterium glutamicum
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
Michaelis-Menten kinetics
Bacillus subtilis
additional information
-
additional information
Michaelis-Menten kinetics
Corynebacterium glutamicum
additional information
-
additional information
Michaelis-Menten kinetics
Escherichia coli
1.63
-
L-aspartate
pH 7.0, 37°C, recombinant mutant I188M
Bacillus subtilis
1.66
-
L-aspartate
pH 7.0, 37°C, recombinant mutant L127X
Bacillus subtilis
2.02
-
L-aspartate
pH 7.0, 37°C, recombinant wild-type enzyme
Bacillus subtilis
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
L-aspartate
Corynebacterium glutamicum
-
beta-alanine + CO2
-
-
?
L-aspartate
Escherichia coli
-
beta-alanine + CO2
-
-
?
L-aspartate
Bacillus subtilis
-
beta-alanine + CO2
-
-
?
L-aspartate
Bacillus subtilis 168
-
beta-alanine + CO2
-
-
?
L-aspartate
Corynebacterium glutamicum ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025
-
beta-alanine + CO2
-
-
?
L-aspartate
Escherichia coli K-12 / DH5alpha
-
beta-alanine + CO2
-
-
?
Organism
Organism
UniProt
Commentary
Textmining
Bacillus subtilis
P52999
-
-
Bacillus subtilis 168
P52999
-
-
Corynebacterium glutamicum
Q9X4N0
-
-
Corynebacterium glutamicum ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025
Q9X4N0
-
-
Escherichia coli
P0A790
-
-
Escherichia coli K-12 / DH5alpha
P0A790
-
-
Posttranslational Modification
Posttranslational Modification
Commentary
Organism
proteolytic modification
the ADC protein is initially translated as an inactive Pi-protein and then proteolytically cleaved at a site to generate the active species comprising the pyruvoyl-containing alpha-subunit and a smaller beta-subunit. The cleavage of the recombinant ADC protein from Bacillus subtilis after expression in Escherichia coli is almost complete
Bacillus subtilis
proteolytic modification
the ADC protein is initially translated as an inactive Pi-protein and then proteolytically cleaved at a site to generate the active species comprising the pyruvoyl-containing alpha-subunit and a smaller beta-subunit. The cleavage of the recombinant ADC protein from Corynebacterium glutamicum after expression in Escherichia coli is almost complete
Corynebacterium glutamicum
proteolytic modification
the ADC protein is initially translated as an inactive Pi-protein (14 kDa) and then proteolytically cleaved at the Gly24-Ser25 site to generate the active species comprising the pyruvoyl-containing alpha-subunit (11 kDa) and a smaller beta-subunit (3 kDa). The enzyme requires PanZ as an activator involved in the cleavage of ADCE. The recombinant ADC protein expressed from Escherichia coli strain BL21(DE3) is mainly in its inactive uncleaved form, possibly because of insufficience of panZ, an activator involved in the cleavage of ADCE
Escherichia coli
Purification (Commentary)
Purification (Commentary)
Organism
recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography to over 90% purity
Bacillus subtilis
recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography to over 90% purity
Corynebacterium glutamicum
recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography to over 90% purity
Escherichia coli
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
L-aspartate
-
746859
Corynebacterium glutamicum
beta-alanine + CO2
-
-
-
?
L-aspartate
-
746859
Escherichia coli
beta-alanine + CO2
-
-
-
?
L-aspartate
-
746859
Bacillus subtilis
beta-alanine + CO2
-
-
-
?
L-aspartate
-
746859
Bacillus subtilis 168
beta-alanine + CO2
-
-
-
?
L-aspartate
-
746859
Corynebacterium glutamicum ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025
beta-alanine + CO2
-
-
-
?
L-aspartate
-
746859
Escherichia coli K-12 / DH5alpha
beta-alanine + CO2
-
-
-
?
additional information
fluorometric method for beta-alanine determination, development of a high-throughput screening method for beta-alanine detection
746859
Corynebacterium glutamicum
?
-
-
-
-
additional information
fluorometric method for beta-alanine determination, development of a high-throughput screening method for beta-alanine detection
746859
Escherichia coli
?
-
-
-
-
additional information
fluorometric method for beta-alanine determination, development of a high-throughput screening method for beta-alanine detection
746859
Bacillus subtilis
?
-
-
-
-
additional information
fluorometric method for beta-alanine determination, development of a high-throughput screening method for beta-alanine detection
746859
Bacillus subtilis 168
?
-
-
-
-
additional information
fluorometric method for beta-alanine determination, development of a high-throughput screening method for beta-alanine detection
746859
Corynebacterium glutamicum ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025
?
-
-
-
-
additional information
fluorometric method for beta-alanine determination, development of a high-throughput screening method for beta-alanine detection
746859
Escherichia coli K-12 / DH5alpha
?
-
-
-
-
Synonyms
Synonyms
Commentary
Organism
ADC
-
Bacillus subtilis
ADC
-
Corynebacterium glutamicum
ADC
-
Escherichia coli
ADCBs
-
Bacillus subtilis
ADCCg
-
Corynebacterium glutamicum
ADCE
-
Escherichia coli
L-Aspartate-alpha-decarboxylase
-
Bacillus subtilis
L-Aspartate-alpha-decarboxylase
-
Corynebacterium glutamicum
L-Aspartate-alpha-decarboxylase
-
Escherichia coli
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
37
-
recombinant enzyme
Bacillus subtilis
37
-
assay at
Corynebacterium glutamicum
37
-
assay at
Escherichia coli
Temperature Range [°C]
Temperature Minimum [°C]
Temperature Maximum [°C]
Commentary
Organism
37
65
maximal activity at 37°C, 95% of maximal activity at 50°C, 80% at 60°C, and 70% at 65°C
Bacillus subtilis
37
65
90% of maximal activity at 37°C, 80% at 50°C, and 40% at 65°C
Corynebacterium glutamicum
Temperature Stability [°C]
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
37
-
purified recombinant enzyme, pH 7.0, about 30% activity remaining after 4 h
Bacillus subtilis
37
-
purified recombinant enzyme, pH 7.0, about 50% activity remaining after 4 h
Corynebacterium glutamicum
50
-
purified recombinant enzyme, pH 7.0, below 10% activity remaining after 2.5 h
Bacillus subtilis
50
-
purified recombinant enzyme, pH 7.0, about 20% activity remaining after 2.5 h
Corynebacterium glutamicum
60
-
purified recombinant enzyme, pH 7.0, inactivation after 1 h
Bacillus subtilis
60
-
purified recombinant enzyme, pH 7.0, below 10% activity remaining after 1 h
Corynebacterium glutamicum
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
5.28
-
L-aspartate
pH 7.0, 37°C, recombinant mutant L127X
Bacillus subtilis
6.26
-
L-aspartate
pH 7.0, 37°C, recombinant wild-type enzyme
Bacillus subtilis
6.6
-
L-aspartate
pH 7.0, 37°C, recombinant mutant I188M
Bacillus subtilis
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7
-
assay at
Bacillus subtilis
7
-
assay at
Corynebacterium glutamicum
7
-
assay at
Escherichia coli
Cofactor
Cofactor
Commentary
Organism
Structure
additional information
the enzyme requires PanZ, an activator involved in the cleavage of ADCE
Escherichia coli
Cloned(Commentary) (protein specific)
Commentary
Organism
gene panD, recombinant expression of N-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3), the recombinant ADC protein is mainly in its inactive uncleaved form, possibly because of insufficience of panZ, an activator involved in the cleavage of ADCE
Escherichia coli
gene panD, recombinant expression of N-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3). The cleavage of the recombinant ADC protein from Bacillus subtilis after expression in Escherichia coli is almost complete
Bacillus subtilis
gene panD, recombinant expression of N-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3). The cleavage of the recombinant ADC protein from Corynebacteriums glutamicum after expression in Escherichia coli is almost complete
Corynebacterium glutamicum
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
additional information
the enzyme requires PanZ, an activator involved in the cleavage of ADCE
Escherichia coli
Engineering (protein specific)
Protein Variants
Commentary
Organism
I188M
site-directed mutagenesis, the mutant shows increased thermostability compared to the wild-type
Bacillus subtilis
additional information
mutation of nucleotide L127 increases the enzyme's thermostability compared to the wild-type, while mutation of nuclotide V68 does not significantly affect the thermostability
Bacillus subtilis
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
additional information
enzyme ADC is also subject to mechanism-based inactivation, which has been reported for many other pyruvoyl-dependent. Mechanism-based inactivation only occurs during catalysis
Bacillus subtilis
additional information
enzyme ADC is also subject to mechanism-based inactivation, which has been reported for many other pyruvoyl-dependent. Mechanism-based inactivation only occurs during catalysis
Corynebacterium glutamicum
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
Michaelis-Menten kinetics
Bacillus subtilis
additional information
-
additional information
Michaelis-Menten kinetics
Corynebacterium glutamicum
additional information
-
additional information
Michaelis-Menten kinetics
Escherichia coli
1.63
-
L-aspartate
pH 7.0, 37°C, recombinant mutant I188M
Bacillus subtilis
1.66
-
L-aspartate
pH 7.0, 37°C, recombinant mutant L127X
Bacillus subtilis
2.02
-
L-aspartate
pH 7.0, 37°C, recombinant wild-type enzyme
Bacillus subtilis
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
L-aspartate
Corynebacterium glutamicum
-
beta-alanine + CO2
-
-
?
L-aspartate
Escherichia coli
-
beta-alanine + CO2
-
-
?
L-aspartate
Bacillus subtilis
-
beta-alanine + CO2
-
-
?
L-aspartate
Bacillus subtilis 168
-
beta-alanine + CO2
-
-
?
L-aspartate
Corynebacterium glutamicum ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025
-
beta-alanine + CO2
-
-
?
L-aspartate
Escherichia coli K-12 / DH5alpha
-
beta-alanine + CO2
-
-
?
Posttranslational Modification (protein specific)
Posttranslational Modification
Commentary
Organism
proteolytic modification
the ADC protein is initially translated as an inactive Pi-protein and then proteolytically cleaved at a site to generate the active species comprising the pyruvoyl-containing alpha-subunit and a smaller beta-subunit. The cleavage of the recombinant ADC protein from Bacillus subtilis after expression in Escherichia coli is almost complete
Bacillus subtilis
proteolytic modification
the ADC protein is initially translated as an inactive Pi-protein and then proteolytically cleaved at a site to generate the active species comprising the pyruvoyl-containing alpha-subunit and a smaller beta-subunit. The cleavage of the recombinant ADC protein from Corynebacterium glutamicum after expression in Escherichia coli is almost complete
Corynebacterium glutamicum
proteolytic modification
the ADC protein is initially translated as an inactive Pi-protein (14 kDa) and then proteolytically cleaved at the Gly24-Ser25 site to generate the active species comprising the pyruvoyl-containing alpha-subunit (11 kDa) and a smaller beta-subunit (3 kDa). The enzyme requires PanZ as an activator involved in the cleavage of ADCE. The recombinant ADC protein expressed from Escherichia coli strain BL21(DE3) is mainly in its inactive uncleaved form, possibly because of insufficience of panZ, an activator involved in the cleavage of ADCE
Escherichia coli
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography to over 90% purity
Bacillus subtilis
recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography to over 90% purity
Corynebacterium glutamicum
recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography to over 90% purity
Escherichia coli
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
L-aspartate
-
746859
Corynebacterium glutamicum
beta-alanine + CO2
-
-
-
?
L-aspartate
-
746859
Escherichia coli
beta-alanine + CO2
-
-
-
?
L-aspartate
-
746859
Bacillus subtilis
beta-alanine + CO2
-
-
-
?
L-aspartate
-
746859
Bacillus subtilis 168
beta-alanine + CO2
-
-
-
?
L-aspartate
-
746859
Corynebacterium glutamicum ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025
beta-alanine + CO2
-
-
-
?
L-aspartate
-
746859
Escherichia coli K-12 / DH5alpha
beta-alanine + CO2
-
-
-
?
additional information
fluorometric method for beta-alanine determination, development of a high-throughput screening method for beta-alanine detection
746859
Corynebacterium glutamicum
?
-
-
-
-
additional information
fluorometric method for beta-alanine determination, development of a high-throughput screening method for beta-alanine detection
746859
Escherichia coli
?
-
-
-
-
additional information
fluorometric method for beta-alanine determination, development of a high-throughput screening method for beta-alanine detection
746859
Bacillus subtilis
?
-
-
-
-
additional information
fluorometric method for beta-alanine determination, development of a high-throughput screening method for beta-alanine detection
746859
Bacillus subtilis 168
?
-
-
-
-
additional information
fluorometric method for beta-alanine determination, development of a high-throughput screening method for beta-alanine detection
746859
Corynebacterium glutamicum ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025
?
-
-
-
-
additional information
fluorometric method for beta-alanine determination, development of a high-throughput screening method for beta-alanine detection
746859
Escherichia coli K-12 / DH5alpha
?
-
-
-
-
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
37
-
recombinant enzyme
Bacillus subtilis
37
-
assay at
Corynebacterium glutamicum
37
-
assay at
Escherichia coli
Temperature Range [°C] (protein specific)
Temperature Minimum [°C]
Temperature Maximum [°C]
Commentary
Organism
37
65
maximal activity at 37°C, 95% of maximal activity at 50°C, 80% at 60°C, and 70% at 65°C
Bacillus subtilis
37
65
90% of maximal activity at 37°C, 80% at 50°C, and 40% at 65°C
Corynebacterium glutamicum
Temperature Stability [°C] (protein specific)
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
37
-
purified recombinant enzyme, pH 7.0, about 30% activity remaining after 4 h
Bacillus subtilis
37
-
purified recombinant enzyme, pH 7.0, about 50% activity remaining after 4 h
Corynebacterium glutamicum
50
-
purified recombinant enzyme, pH 7.0, below 10% activity remaining after 2.5 h
Bacillus subtilis
50
-
purified recombinant enzyme, pH 7.0, about 20% activity remaining after 2.5 h
Corynebacterium glutamicum
60
-
purified recombinant enzyme, pH 7.0, inactivation after 1 h
Bacillus subtilis
60
-
purified recombinant enzyme, pH 7.0, below 10% activity remaining after 1 h
Corynebacterium glutamicum
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
5.28
-
L-aspartate
pH 7.0, 37°C, recombinant mutant L127X
Bacillus subtilis
6.26
-
L-aspartate
pH 7.0, 37°C, recombinant wild-type enzyme
Bacillus subtilis
6.6
-
L-aspartate
pH 7.0, 37°C, recombinant mutant I188M
Bacillus subtilis
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7
-
assay at
Bacillus subtilis
7
-
assay at
Corynebacterium glutamicum
7
-
assay at
Escherichia coli
KCat/KM [mM/s]
kcat/KM Value [1/mMs-1]
kcat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
3.1
-
L-aspartate
pH 7.0, 37°C, recombinant wild-type enzyme
Bacillus subtilis
3.18
-
L-aspartate
pH 7.0, 37°C, recombinant mutant L127X
Bacillus subtilis
4.05
-
L-aspartate
pH 7.0, 37°C, recombinant mutant I188M
Bacillus subtilis
KCat/KM [mM/s] (protein specific)
KCat/KM Value [1/mMs-1]
KCat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
3.1
-
L-aspartate
pH 7.0, 37°C, recombinant wild-type enzyme
Bacillus subtilis
3.18
-
L-aspartate
pH 7.0, 37°C, recombinant mutant L127X
Bacillus subtilis
4.05
-
L-aspartate
pH 7.0, 37°C, recombinant mutant I188M
Bacillus subtilis
Other publictions for EC 4.1.1.11
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)
749207
Zhang
-
Glu56Ser mutation improves th ...
Bacillus subtilis, Bacillus subtilis 168, Corynebacterium glutamicum, Corynebacterium glutamicum ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025, Escherichia coli, Lactobacillus plantarum, Lactobacillus plantarum ATCC BAA-793 / NCIMB 8826 / WCFS1
Process Biochem.
70
117-123
2018
-
-
3
-
3
-
-
-
-
-
-
7
-
11
-
4
3
-
-
-
6
-
7
4
20
3
3
-
-
3
3
-
-
-
4
-
-
-
3
-
-
3
-
-
-
-
-
-
-
-
7
-
-
4
3
-
-
6
-
7
4
3
3
-
-
3
3
-
4
-
10
10
-
-
-
746598
Gopal
In vivo-selected pyrazinoic a ...
Mycobacterium tuberculosis
ACS Infect. Dis.
3
492-501
2017
-
-
-
-
18
-
-
-
-
-
-
-
-
5
-
-
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
18
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
746859
Pei
Molecular engineering of L-as ...
Bacillus subtilis 168, Bacillus subtilis, Corynebacterium glutamicum, Corynebacterium glutamicum ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025, Escherichia coli, Escherichia coli K-12 / DH5alpha
Appl. Microbiol. Biotechnol.
101
6015-6021
2017
-
-
3
-
2
-
2
6
-
-
-
6
-
10
-
3
3
-
-
-
-
-
12
-
9
3
2
6
3
3
-
-
1
-
-
-
-
-
3
1
-
2
-
-
2
-
6
-
-
-
6
-
-
3
3
-
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12
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3
2
6
3
3
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3
3
747128
Arnott
The mechanism of regulation o ...
Escherichia coli
Biochemistry
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2017
1
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747799
Gliessman
Pantothenate auxotrophy in Zy ...
Escherichia coli, no activity in Zymomonas mobilis, no activity in Zymomonas mobilis ZM4 / ATCC 31821 / CP4
FEMS Microbiol. Lett.
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2017
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747435
Stuecker
Phylogenetic and amino acid c ...
Bacillus halodurans, Bacillus halodurans ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125, Bordetella pertussis, Bordetella pertussis Tohama I / ATCC BAA-589 / NCTC 13251, Corynebacterium glutamicum, Corynebacterium glutamicum ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025, Helicobacter pylori, Helicobacter pylori 26695, Klebsiella pneumoniae, Klebsiella pneumoniae ATCC 700721 / MGH 78578, Legionella pneumophila, Magnetospirillum magneticum, Magnetospirillum magneticum AMB-1 / ATCC 700264, Moorella thermoacetica, Moorella thermoacetica ATCC 39073 / JCM 9320, Neisseria gonorrhoeae, Neisseria gonorrhoeae ATCC 700825 / FA 1090, Pseudomonas aeruginosa, Pseudomonas aeruginosa ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1, Ralstonia solanacearum, Salmonella enterica subsp. enterica serovar Typhimurium, Salmonella enterica subsp. enterica serovar Typhimurium LT2 / SGSC1412 / ATCC 700720
BMC Res. Notes
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22
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15
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747497
Monteiro
The structure of the PanD/Pan ...
Escherichia coli
Chem. Biol.
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2015
2
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1
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2
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4
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747593
Deng
Characterization of L-asparta ...
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Chin. J. Biotechnol.
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2015
1
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Dai
Aspartate decarboxylase is re ...
Bombyx mori
Sci. Rep.
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Webb
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3
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Cui
Significance of Arg3, Arg54, a ...
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1
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10
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Shen
Synthesis of beta-alanine from ...
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beta-Alanine biosynthesis in M ...
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Shen
Synthesis of beta-alanine fro ...
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An archaeal glutamate decarbo ...
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Lee
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Gene expression and character ...
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Webb
Structure of Escherichia coli ...
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Monteiro
Formation of a heterooctameric ...
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Cysteine sulfinic acid decarbo ...
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Stuecker
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PanM, an acetyl-coenzyme a sen ...
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Nozaki
An activator for pyruvoyl-depe ...
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Stuecker
The missing link in coenzyme A ...
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6
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2
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728571
Sharma
Chemoinformatic identification ...
Mycobacterium tuberculosis
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1
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9
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3
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Sharma
Validation of drug-like inhibi ...
Mycobacterium tuberculosis
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1
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12
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714398
Lomakin
Mechanical properties of the b ...
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2
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714741
de Villiers
3-Fluoroaspartate and pyruvoyl ...
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Arakane
Molecular and functional analy ...
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1
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1
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1
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Phillips
The Drosophila black enigma: T ...
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1
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