Structural and enzymatic characterization of BacD, an L-amino acid dipeptide ligase from Bacillus subtilis
Shomura, Y.; Hinokuchi, E.; Ikeda, H.; Senoo, A.; Takahashi, Y.; Saito, J.; Komori, H.; Shibata, N.; Yonetani, Y.; Higuchi, Y.; Protein Sci. 21, 707-716 (2012) 
Data extracted from this reference:
Application
Application
Commentary
Organism
pharmacology
potential application in industrial protein engineering for the environmentally friendly biological production of useful peptide compounds, such as physiologically active peptides, artificial sweeteners and antibiotics
Bacillus subtilis
Cloned(Commentary)
Cloned (Commentary)
Organism
-
Bacillus subtilis
Crystallization (Commentary)
Crystallization (Commentary)
Organism
crystal structure of the enzyme in complex with ADP and an intermediate analog, phosphorylated phosphinate L-alanyl-L-phenylalanine, refined to 2.5 A resolution, sitting-drop vapor-diffusion method at 20°C
Bacillus subtilis
Engineering
Protein Variants
Commentary
Organism
S1845A
no significant difference in kcat value between the wild type and the mutant enzyme. 2fold increase in Km-value for L-alanine
Bacillus subtilis
Y75F
no significant difference in kcat value between the wild type and the mutant enzyme, 2fold increase in KM-value for L-phenylalanine
Bacillus subtilis
Inhibitors
Inhibitors
Commentary
Organism
Structure
(2S)-3-[[(1R)-1-aminoethyl(hydroxy)]phosphoryl]-2-benzylpropionic acid
competitive inhibition for L-alanine but not for L-phenylalanine
Bacillus subtilis
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
1.5
-
L-alanine
pH 7.1, 37°C, mutant enzyme Y75F
Bacillus subtilis
1.7
-
L-alanine
pH 7.7, 37°C, mutant enzyme Y75F
Bacillus subtilis
2
-
L-alanine
pH 7.7, 37°C, wild-type enzyme
Bacillus subtilis
2.6
-
L-alanine
pH 7.1, 37°C, wild-type enzyme
Bacillus subtilis
4.6
-
L-alanine
pH 7.7, 37°C, mutant enzyme S184A
Bacillus subtilis
4.9
-
L-alanine
pH 7.1, 37°C, mutant enzyme S184F
Bacillus subtilis
16
-
L-phenylalanine
pH 7.7, 37°C, mutant enzyme S184A
Bacillus subtilis
18
-
L-phenylalanine
pH 7.7, 37°C, wild-type enzyme
Bacillus subtilis
38
-
L-phenylalanine
pH 7.1, 37°C, mutant enzyme S184F
Bacillus subtilis
44
-
L-phenylalanine
pH 7.1, 37°C, wild-type enzyme
Bacillus subtilis
45
-
L-phenylalanine
pH 7.7, 37°C, mutant enzyme
Bacillus subtilis
92
-
L-phenylalanine
pH 7.1, 37°C, mutant enzyme
Bacillus subtilis
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
ATP + L-alanine + (1R,2S,6R)-anticapsin
Bacillus subtilis
-
ADP + phosphate + bacilysin
bacilysin i.e. L-alanyl-3-[(1R,2S,6R)-5-oxo-7-oxabicyclo[4.1.0]hept-2-yl]-L-alanine
-
?
ATP + L-alanine + (1R,2S,6R)-anticapsin
Bacillus subtilis 168
-
ADP + phosphate + bacilysin
bacilysin i.e. L-alanyl-3-[(1R,2S,6R)-5-oxo-7-oxabicyclo[4.1.0]hept-2-yl]-L-alanine
-
?
Organism
Organism
UniProt
Commentary
Textmining
Bacillus subtilis
P39641
-
-
Bacillus subtilis 168
P39641
-
-
Purification (Commentary)
Purification (Commentary)
Organism
-
Bacillus subtilis
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
(2S)-3-[[(1R)-1-aminoethyl(hydroxy)]phosphoryl]-2-benzylpropionic acid + ATP
the phosphinate L-alanyl-L-phenylalanine analog binds the active site of the enzyme, and accepts a phosphate group from ATP to form the phosphorylated phosphinate L-alanyl-L-phenylalanine analog
730896
Bacillus subtilis
(2S)-3-[(3)-[(1R)-1-aminoethyl(phosphonooxy)]phosphoryl]-2-benzylpropanoic acid + ADP
-
-
-
?
(2S)-3-[[(1R)-1-aminoethyl(hydroxy)]phosphoryl]-2-benzylpropionic acid + ATP
the phosphinate L-alanyl-L-phenylalanine analog binds the active site of the enzyme, and accepts a phosphate group from ATP to form the phosphorylated phosphinate L-alanyl-L-phenylalanine analog
730896
Bacillus subtilis 168
(2S)-3-[(3)-[(1R)-1-aminoethyl(phosphonooxy)]phosphoryl]-2-benzylpropanoic acid + ADP
-
-
-
?
ATP + L-alanine + (1R,2S,6R)-anticapsin
-
730896
Bacillus subtilis
ADP + phosphate + bacilysin
bacilysin i.e. L-alanyl-3-[(1R,2S,6R)-5-oxo-7-oxabicyclo[4.1.0]hept-2-yl]-L-alanine
-
-
?
ATP + L-alanine + (1R,2S,6R)-anticapsin
-
730896
Bacillus subtilis 168
ADP + phosphate + bacilysin
bacilysin i.e. L-alanyl-3-[(1R,2S,6R)-5-oxo-7-oxabicyclo[4.1.0]hept-2-yl]-L-alanine
-
-
?
ATP + L-alanine + L-phenylalanine
the substrate pair L-alanine and L-phenylalanine shows the highest activity among the combinations of less bulky amino acids (glycine, L-alanine, and L-serine) and uncharged bulky amino acids (L-leucine, L-isolucine, L-methionine, L-phenylalanine, L-tyrosine, L-tryptophane, and L-glutamine). Some D-amino acids (D-alanine, D-serine, D-phenylalanine, and D-glutamine) are tested but show no activity
730896
Bacillus subtilis
ADP + phosphate + L-alanyl-L-phenylalanine
-
-
-
?
ATP + L-alanine + L-phenylalanine
the substrate pair L-alanine and L-phenylalanine shows the highest activity among the combinations of less bulky amino acids (glycine, L-alanine, and L-serine) and uncharged bulky amino acids (L-leucine, L-isolucine, L-methionine, L-phenylalanine, L-tyrosine, L-tryptophane, and L-glutamine). Some D-amino acids (D-alanine, D-serine, D-phenylalanine, and D-glutamine) are tested but show no activity
730896
Bacillus subtilis 168
ADP + phosphate + L-alanyl-L-phenylalanine
-
-
-
?
Subunits
Subunits
Commentary
Organism
monomer
-
Bacillus subtilis
Synonyms
Synonyms
Commentary
Organism
BacD
-
Bacillus subtilis
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
37
-
assay at
Bacillus subtilis
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
7.2
-
L-phenylalanine
pH 7.1, 37°C, mutant enzyme
Bacillus subtilis
7.2
-
L-alanine
pH 7.1, 37°C, mutant enzyme Y75F
Bacillus subtilis
7.7
-
L-alanine
pH 7.1, 37°C, wild-type enzyme
Bacillus subtilis
7.7
-
L-phenylalanine
pH 7.1, 37°C, wild-type enzyme
Bacillus subtilis
7.8
-
L-alanine
pH 7.1, 37°C, mutant enzyme S184F
Bacillus subtilis
7.8
-
L-phenylalanine
pH 7.1, 37°C, mutant enzyme S184F
Bacillus subtilis
9.7
-
L-phenylalanine
pH 7.7, 37°C, mutant enzyme
Bacillus subtilis
9.7
-
L-alanine
pH 7.7, 37°C, mutant enzyme Y75F
Bacillus subtilis
9.7
-
L-alanine
pH 7.7, 37°C, wild-type enzyme
Bacillus subtilis
9.7
-
L-phenylalanine
pH 7.7, 37°C, wild-type enzyme
Bacillus subtilis
10.8
-
L-alanine
pH 7.7, 37°C, mutant enzyme S184A
Bacillus subtilis
10.8
-
L-phenylalanine
pH 7.7, 37°C, mutant enzyme S184A
Bacillus subtilis
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.7
-
assay at
Bacillus subtilis
Ki Value [mM]
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
0.0154
-
(2S)-3-[[(1R)-1-aminoethyl(hydroxy)]phosphoryl]-2-benzylpropionic acid
pH 7.7, 37°C
Bacillus subtilis
Application (protein specific)
Application
Commentary
Organism
pharmacology
potential application in industrial protein engineering for the environmentally friendly biological production of useful peptide compounds, such as physiologically active peptides, artificial sweeteners and antibiotics
Bacillus subtilis
Cloned(Commentary) (protein specific)
Commentary
Organism
-
Bacillus subtilis
Crystallization (Commentary) (protein specific)
Crystallization
Organism
crystal structure of the enzyme in complex with ADP and an intermediate analog, phosphorylated phosphinate L-alanyl-L-phenylalanine, refined to 2.5 A resolution, sitting-drop vapor-diffusion method at 20°C
Bacillus subtilis
Engineering (protein specific)
Protein Variants
Commentary
Organism
S1845A
no significant difference in kcat value between the wild type and the mutant enzyme. 2fold increase in Km-value for L-alanine
Bacillus subtilis
Y75F
no significant difference in kcat value between the wild type and the mutant enzyme, 2fold increase in KM-value for L-phenylalanine
Bacillus subtilis
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
(2S)-3-[[(1R)-1-aminoethyl(hydroxy)]phosphoryl]-2-benzylpropionic acid
competitive inhibition for L-alanine but not for L-phenylalanine
Bacillus subtilis
Ki Value [mM] (protein specific)
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
0.0154
-
(2S)-3-[[(1R)-1-aminoethyl(hydroxy)]phosphoryl]-2-benzylpropionic acid
pH 7.7, 37°C
Bacillus subtilis
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
1.5
-
L-alanine
pH 7.1, 37°C, mutant enzyme Y75F
Bacillus subtilis
1.7
-
L-alanine
pH 7.7, 37°C, mutant enzyme Y75F
Bacillus subtilis
2
-
L-alanine
pH 7.7, 37°C, wild-type enzyme
Bacillus subtilis
2.6
-
L-alanine
pH 7.1, 37°C, wild-type enzyme
Bacillus subtilis
4.6
-
L-alanine
pH 7.7, 37°C, mutant enzyme S184A
Bacillus subtilis
4.9
-
L-alanine
pH 7.1, 37°C, mutant enzyme S184F
Bacillus subtilis
16
-
L-phenylalanine
pH 7.7, 37°C, mutant enzyme S184A
Bacillus subtilis
18
-
L-phenylalanine
pH 7.7, 37°C, wild-type enzyme
Bacillus subtilis
38
-
L-phenylalanine
pH 7.1, 37°C, mutant enzyme S184F
Bacillus subtilis
44
-
L-phenylalanine
pH 7.1, 37°C, wild-type enzyme
Bacillus subtilis
45
-
L-phenylalanine
pH 7.7, 37°C, mutant enzyme
Bacillus subtilis
92
-
L-phenylalanine
pH 7.1, 37°C, mutant 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
ATP + L-alanine + (1R,2S,6R)-anticapsin
Bacillus subtilis
-
ADP + phosphate + bacilysin
bacilysin i.e. L-alanyl-3-[(1R,2S,6R)-5-oxo-7-oxabicyclo[4.1.0]hept-2-yl]-L-alanine
-
?
ATP + L-alanine + (1R,2S,6R)-anticapsin
Bacillus subtilis 168
-
ADP + phosphate + bacilysin
bacilysin i.e. L-alanyl-3-[(1R,2S,6R)-5-oxo-7-oxabicyclo[4.1.0]hept-2-yl]-L-alanine
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
-
Bacillus subtilis
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
(2S)-3-[[(1R)-1-aminoethyl(hydroxy)]phosphoryl]-2-benzylpropionic acid + ATP
the phosphinate L-alanyl-L-phenylalanine analog binds the active site of the enzyme, and accepts a phosphate group from ATP to form the phosphorylated phosphinate L-alanyl-L-phenylalanine analog
730896
Bacillus subtilis
(2S)-3-[(3)-[(1R)-1-aminoethyl(phosphonooxy)]phosphoryl]-2-benzylpropanoic acid + ADP
-
-
-
?
(2S)-3-[[(1R)-1-aminoethyl(hydroxy)]phosphoryl]-2-benzylpropionic acid + ATP
the phosphinate L-alanyl-L-phenylalanine analog binds the active site of the enzyme, and accepts a phosphate group from ATP to form the phosphorylated phosphinate L-alanyl-L-phenylalanine analog
730896
Bacillus subtilis 168
(2S)-3-[(3)-[(1R)-1-aminoethyl(phosphonooxy)]phosphoryl]-2-benzylpropanoic acid + ADP
-
-
-
?
ATP + L-alanine + (1R,2S,6R)-anticapsin
-
730896
Bacillus subtilis
ADP + phosphate + bacilysin
bacilysin i.e. L-alanyl-3-[(1R,2S,6R)-5-oxo-7-oxabicyclo[4.1.0]hept-2-yl]-L-alanine
-
-
?
ATP + L-alanine + (1R,2S,6R)-anticapsin
-
730896
Bacillus subtilis 168
ADP + phosphate + bacilysin
bacilysin i.e. L-alanyl-3-[(1R,2S,6R)-5-oxo-7-oxabicyclo[4.1.0]hept-2-yl]-L-alanine
-
-
?
ATP + L-alanine + L-phenylalanine
the substrate pair L-alanine and L-phenylalanine shows the highest activity among the combinations of less bulky amino acids (glycine, L-alanine, and L-serine) and uncharged bulky amino acids (L-leucine, L-isolucine, L-methionine, L-phenylalanine, L-tyrosine, L-tryptophane, and L-glutamine). Some D-amino acids (D-alanine, D-serine, D-phenylalanine, and D-glutamine) are tested but show no activity
730896
Bacillus subtilis
ADP + phosphate + L-alanyl-L-phenylalanine
-
-
-
?
ATP + L-alanine + L-phenylalanine
the substrate pair L-alanine and L-phenylalanine shows the highest activity among the combinations of less bulky amino acids (glycine, L-alanine, and L-serine) and uncharged bulky amino acids (L-leucine, L-isolucine, L-methionine, L-phenylalanine, L-tyrosine, L-tryptophane, and L-glutamine). Some D-amino acids (D-alanine, D-serine, D-phenylalanine, and D-glutamine) are tested but show no activity
730896
Bacillus subtilis 168
ADP + phosphate + L-alanyl-L-phenylalanine
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
monomer
-
Bacillus subtilis
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
37
-
assay at
Bacillus subtilis
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
7.2
-
L-phenylalanine
pH 7.1, 37°C, mutant enzyme
Bacillus subtilis
7.2
-
L-alanine
pH 7.1, 37°C, mutant enzyme Y75F
Bacillus subtilis
7.7
-
L-alanine
pH 7.1, 37°C, wild-type enzyme
Bacillus subtilis
7.7
-
L-phenylalanine
pH 7.1, 37°C, wild-type enzyme
Bacillus subtilis
7.8
-
L-alanine
pH 7.1, 37°C, mutant enzyme S184F
Bacillus subtilis
7.8
-
L-phenylalanine
pH 7.1, 37°C, mutant enzyme S184F
Bacillus subtilis
9.7
-
L-phenylalanine
pH 7.7, 37°C, mutant enzyme
Bacillus subtilis
9.7
-
L-alanine
pH 7.7, 37°C, mutant enzyme Y75F
Bacillus subtilis
9.7
-
L-alanine
pH 7.7, 37°C, wild-type enzyme
Bacillus subtilis
9.7
-
L-phenylalanine
pH 7.7, 37°C, wild-type enzyme
Bacillus subtilis
10.8
-
L-alanine
pH 7.7, 37°C, mutant enzyme S184A
Bacillus subtilis
10.8
-
L-phenylalanine
pH 7.7, 37°C, mutant enzyme S184A
Bacillus subtilis
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.7
-
assay at
Bacillus subtilis
Other publictions for EC 6.3.2.49
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)
733347
Tsuda
Single mutation alters the sub ...
Bacillus subtilis
Biochemistry
53
2650-2660
2014
-
1
-
1
1
-
-
-
-
-
-
1
-
2
-
-
-
-
-
-
-
-
3
-
3
-
-
-
-
-
-
-
1
-
-
-
-
1
-
1
1
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
2
2
-
-
-
726743
Arai
L-amino acid ligase from Pseud ...
Pseudomonas syringae, Pseudomonas syringae NBRC 14081
Appl. Environ. Microbiol.
79
5023-5029
2013
-
1
1
-
-
-
-
-
-
1
-
4
-
5
-
-
-
-
-
-
-
-
100
-
3
1
1
-
-
1
1
-
1
-
-
-
-
1
1
1
-
-
-
-
-
-
-
-
1
-
4
-
-
-
-
-
-
-
-
100
-
1
1
-
-
1
1
-
-
-
-
-
-
-
-
729244
Parker
Action and timing of BacC and ...
Bacillus subtilis, Bacillus subtilis 168
Biochemistry
52
889-901
2013
-
-
1
-
-
-
-
-
-
-
-
2
-
6
-
-
1
-
-
-
-
-
8
-
6
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
1
-
-
-
-
8
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
726581
Suzuki
The structure of L-amino-acid ...
Bacillus licheniformis, Bacillus licheniformis NBRC 12200
Acta Crystallogr. Sect. D
68
1535-1540
2012
-
-
1
1
-
-
-
-
-
1
-
2
-
6
-
-
1
-
-
-
-
-
4
-
3
-
-
-
-
-
-
-
1
-
-
-
-
-
1
1
1
-
-
-
-
-
-
-
1
-
2
-
-
-
1
-
-
-
-
4
-
-
-
-
-
-
-
-
-
-
2
2
-
-
-
726615
Tsuda
Crystallization and preliminar ...
Bacillus subtilis, Bacillus subtilis 168
Acta Crystallogr. Sect. F
68
203-206
2012
-
-
-
1
1
-
-
-
-
-
2
-
-
9
-
-
1
-
-
-
-
-
-
1
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
-
-
-
-
2
-
-
-
-
1
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
730896
Shomura
Structural and enzymatic chara ...
Bacillus subtilis, Bacillus subtilis 168
Protein Sci.
21
707-716
2012
-
1
1
1
2
-
1
12
-
-
-
2
-
6
-
-
1
-
-
-
-
-
6
1
1
1
-
-
12
1
-
-
-
1
-
-
-
1
1
-
1
2
-
-
1
1
12
-
-
-
2
-
-
-
1
-
-
-
-
6
1
1
-
-
12
1
-
-
-
-
-
-
-
-
-
702768
Kino
A novel L-amino acid ligase fr ...
Bacillus subtilis, Bacillus subtilis NBRC3134
Biosci. Biotechnol. Biochem.
74
129-134
2010
-
-
1
-
-
-
-
-
-
1
-
-
-
6
-
-
-
-
-
-
-
-
2
-
1
1
1
-
-
1
1
-
-
-
-
-
-
-
1
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1
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2
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1
1
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1
1
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1
1
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-
702771
Senoo
Identification of novel L-amin ...
Actinobacillus pleuropneumoniae, Streptococcus mutans, Streptococcus pneumoniae, Treponema denticola, Photorhabdus laumondii subsp. laumondii
Biosci. Biotechnol. Biochem.
74
415-418
2010
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5
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5
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5
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115
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10
5
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5
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5
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5
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115
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5
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5
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690733
Kino
Dipeptide synthesis by L-amino ...
Ralstonia solanacearum, Ralstonia solanacearum JCM 10489
Biochem. Biophys. Res. Commun.
371
536-540
2008
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1
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1
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1
1
2
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6
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1
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4
1
2
1
-
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1
1
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1
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-
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1
1
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-
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1
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1
1
2
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1
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4
1
1
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1
1
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-
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693286
Kino
A novel L-amino acid ligase fr ...
Bacillus licheniformis, Bacillus licheniformis NBRC12200
J. Biosci. Bioeng.
106
313-315
2008
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1
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1
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4
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8
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1
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17
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2
1
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1
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1
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1
1
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1
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4
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1
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17
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1
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1
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671498
Tabata
Fermentative production of L-a ...
Bacillus subtilis
Appl. Environ. Microbiol.
73
6378-6385
2007
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1
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4
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1
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662037
Tabata
ywf in Bacillus subtilis codes ...
Bacillus subtilis, Bacillus subtilis 168
J. Bacteriol.
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5195-5202
2005
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1
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2
3
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2
1
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8
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1
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4
1
1
1
1
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1
1
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1
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2
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3
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2
1
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1
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4
1
1
1
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1
1
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733219
Steinborn
bac genes for recombinant baci ...
Bacillus pumilus, no activity in Bacillus licheniformis, no activity in Bacillus megaterium, no activity in Bacillus coagulans, no activity in Bacillus pumilus, no activity in Bacillus amyloliquefaciens, Bacillus subtilis, Bacillus amyloliquefaciens, Bacillus subtilis 168, Bacillus pumilus ATCC 7065, Bacillus amyloliquefaciens ATCC 15841, no activity in Bacillus amyloliquefaciens GSB272, Bacillus subtilis A1/3, no activity in Bacillus licheniformis ATCC 9789, no activity in Bacillus megaterium PV361, no activity in Bacillus pumilus ATCC 12140
Arch. Microbiol.
183
71-79
2005
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4
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1
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4
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8
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21
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8
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4
-
-
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4
4
-
1
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4
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8
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8
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7
7
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