BRENDA - Enzyme Database
show all sequences of 6.3.2.49

The structure of L-amino-acid ligase from Bacillus licheniformis

Suzuki, M.; Takahashi, Y.; Noguchi, A.; Arai, T.; Yagasaki, M.; Kino, K.; Saito, J.; Acta Crystallogr. Sect. D 68, 1535-1540 (2012)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
gene BL00235, expression of wild-type enzyme in Escherichia coli strain BL21(DE3) and of selenomethionine-labeled enzyme in Escherichia coli strain B834(DE3)
Bacillus licheniformis
Crystallization (Commentary)
Crystallization
Organism
purified recombinant wild-type and selenomethionine-labeled LAL BL00235s, sitting drop vapour diffusion method, mixing of 00.001 ml of protein solution consisting of 8 mg/ml protein, 1.6 mM ADP, 1.6 mM Met-Ala dipeptide, with 0.001 ml of reservoir solution containing 100 mM CaCl2, 24-27% w/v PEG MME 550, 4% v/v 2-propanol, and 100 mM imidazole, pH 6.5, and equilibration against 0.3 ml of reservoir solution, at room temperature, X-ray diffraction structure determination and analysis at 1.9 A and 1.6 A resolution, respectively, multi-wavelength anomalous dispersion method
Bacillus licheniformis
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Mg2+
required
Bacillus licheniformis
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ATP + an L-amino acid + an L-amino acid
Bacillus licheniformis
-
ADP + phosphate + L-aminoacyl-L-amino acid
-
-
?
ATP + an L-amino acid + an L-amino acid
Bacillus licheniformis NBRC 12200
-
ADP + phosphate + L-aminoacyl-L-amino acid
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Bacillus licheniformis
Q65D11
gene BL00235
-
Bacillus licheniformis NBRC 12200
Q65D11
gene BL00235
-
Purification (Commentary)
Commentary
Organism
recombinant wild-type enzyme and selenomethionine-labeled enzyme from Escherichia coli by anion exchange and hydrophobic interaction chromatography, followed by another step of anion exchange chromatography and gel filtration
Bacillus licheniformis
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ATP + an L-amino acid + an L-amino acid
-
726581
Bacillus licheniformis
ADP + phosphate + L-aminoacyl-L-amino acid
-
-
-
?
ATP + an L-amino acid + an L-amino acid
the enzyme catalyzes the formation of an alpha-peptide bond between two L-amino acids in an ATP-dependent manner
726581
Bacillus licheniformis
ADP + phosphate + L-aminoacyl-L-amino acid
-
-
-
?
ATP + an L-amino acid + an L-amino acid
-
726581
Bacillus licheniformis NBRC 12200
ADP + phosphate + L-aminoacyl-L-amino acid
-
-
-
?
ATP + an L-amino acid + an L-amino acid
the enzyme catalyzes the formation of an alpha-peptide bond between two L-amino acids in an ATP-dependent manner
726581
Bacillus licheniformis NBRC 12200
ADP + phosphate + L-aminoacyl-L-amino acid
-
-
-
?
Cofactor
Cofactor
Commentary
Organism
Structure
ATP
ATP-binding site structure, overview
Bacillus licheniformis
Cloned(Commentary) (protein specific)
Commentary
Organism
gene BL00235, expression of wild-type enzyme in Escherichia coli strain BL21(DE3) and of selenomethionine-labeled enzyme in Escherichia coli strain B834(DE3)
Bacillus licheniformis
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
ATP
ATP-binding site structure, overview
Bacillus licheniformis
Crystallization (Commentary) (protein specific)
Crystallization
Organism
purified recombinant wild-type and selenomethionine-labeled LAL BL00235s, sitting drop vapour diffusion method, mixing of 00.001 ml of protein solution consisting of 8 mg/ml protein, 1.6 mM ADP, 1.6 mM Met-Ala dipeptide, with 0.001 ml of reservoir solution containing 100 mM CaCl2, 24-27% w/v PEG MME 550, 4% v/v 2-propanol, and 100 mM imidazole, pH 6.5, and equilibration against 0.3 ml of reservoir solution, at room temperature, X-ray diffraction structure determination and analysis at 1.9 A and 1.6 A resolution, respectively, multi-wavelength anomalous dispersion method
Bacillus licheniformis
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Mg2+
required
Bacillus licheniformis
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ATP + an L-amino acid + an L-amino acid
Bacillus licheniformis
-
ADP + phosphate + L-aminoacyl-L-amino acid
-
-
?
ATP + an L-amino acid + an L-amino acid
Bacillus licheniformis NBRC 12200
-
ADP + phosphate + L-aminoacyl-L-amino acid
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant wild-type enzyme and selenomethionine-labeled enzyme from Escherichia coli by anion exchange and hydrophobic interaction chromatography, followed by another step of anion exchange chromatography and gel filtration
Bacillus licheniformis
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ATP + an L-amino acid + an L-amino acid
-
726581
Bacillus licheniformis
ADP + phosphate + L-aminoacyl-L-amino acid
-
-
-
?
ATP + an L-amino acid + an L-amino acid
the enzyme catalyzes the formation of an alpha-peptide bond between two L-amino acids in an ATP-dependent manner
726581
Bacillus licheniformis
ADP + phosphate + L-aminoacyl-L-amino acid
-
-
-
?
ATP + an L-amino acid + an L-amino acid
-
726581
Bacillus licheniformis NBRC 12200
ADP + phosphate + L-aminoacyl-L-amino acid
-
-
-
?
ATP + an L-amino acid + an L-amino acid
the enzyme catalyzes the formation of an alpha-peptide bond between two L-amino acids in an ATP-dependent manner
726581
Bacillus licheniformis NBRC 12200
ADP + phosphate + L-aminoacyl-L-amino acid
-
-
-
?
General Information
General Information
Commentary
Organism
evolution
the enzyme belongs to the ATP-grasp superfamily
Bacillus licheniformis
additional information
molecular basis of the substrate specificity, overview, ATP- and dipeptide-binding site structures, overview
Bacillus licheniformis
General Information (protein specific)
General Information
Commentary
Organism
evolution
the enzyme belongs to the ATP-grasp superfamily
Bacillus licheniformis
additional information
molecular basis of the substrate specificity, overview, ATP- and dipeptide-binding site structures, overview
Bacillus licheniformis
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
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
-
-
-
-
-
-
-
-
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
-
4
-
-
-
-
-
-
-
-
100
-
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 168, Bacillus subtilis
Biochemistry
52
889-901
2013
-
-
1
-
-
-
-
-
-
-
-
2
-
6
-
-
1
-
-
-
-
-
8
-
-
-
-
-
-
-
-
-
-
-
-
-
-
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
-
4
-
-
1
-
-
-
-
-
4
-
-
-
-
-
-
-
-
1
-
-
-
-
-
1
1
1
-
-
-
-
-
-
-
1
-
2
-
-
-
1
-
-
-
-
4
-
-
-
-
-
-
-
-
-
-
2
2
-
-
-
726615
Tsuda
Crystallization and preliminar ...
Bacillus subtilis 168, Bacillus subtilis
Acta Crystallogr. Sect. F
68
203-206
2012
-
-
-
1
1
-
-
-
-
-
2
-
-
7
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
-
-
-
-
2
-
-
-
-
1
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
730896
Shomura
Structural and enzymatic chara ...
Bacillus subtilis 168, Bacillus subtilis
Protein Sci.
21
707-716
2012
-
1
1
1
2
-
1
12
-
-
-
2
-
6
-
-
1
-
-
-
-
-
6
1
1
-
-
10
1
-
-
-
1
-
-
-
1
1
-
1
2
-
-
1
1
12
-
-
-
2
-
-
-
1
-
-
-
-
6
1
1
-
-
10
1
-
-
-
-
-
-
-
-
-
702768
Kino
A novel L-amino acid ligase fr ...
Bacillus subtilis, Bacillus subtilis NBRC3134
Biosci. Biotechnol. Biochem.
74
129-134
2010
-
-
1
-
-
-
-
-
-
1
-
-
-
4
-
-
-
-
-
-
-
-
2
-
1
1
-
-
1
1
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
2
-
1
1
-
-
1
1
-
-
-
1
1
-
-
-
702771
Senoo
Identification of novel L-amin ...
Actinobacillus pleuropneumoniae, Photorhabdus laumondii subsp. laumondii, Streptococcus mutans, Streptococcus pneumoniae, Treponema denticola
Biosci. Biotechnol. Biochem.
74
415-418
2010
-
-
5
-
-
-
-
-
-
-
-
-
-
5
-
-
5
-
-
-
-
-
115
-
5
-
-
-
5
-
-
-
-
-
-
-
-
5
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
5
-
-
-
-
115
-
5
-
-
-
5
-
-
-
-
-
-
-
-
-
690733
Kino
Dipeptide synthesis by L-amino ...
Ralstonia solanacearum, Ralstonia solanacearum JCM 10489
Biochem. Biophys. Res. Commun.
371
536-540
2008
-
-
1
-
-
-
-
1
-
1
1
2
-
4
-
-
1
-
-
-
-
-
4
1
1
-
-
-
1
1
-
1
-
-
-
-
-
1
1
-
-
-
-
-
-
1
-
1
1
2
-
-
-
1
-
-
-
-
4
1
1
-
-
-
1
1
-
-
-
-
-
-
-
-
693286
Kino
A novel L-amino acid ligase fr ...
Bacillus licheniformis, Bacillus licheniformis NBRC12200
J. Biosci. Bioeng.
106
313-315
2008
-
-
1
-
-
-
-
-
-
1
-
4
-
4
-
-
1
-
-
-
-
-
17
-
1
-
-
-
1
-
-
1
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
1
-
4
-
-
-
1
-
-
-
-
17
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
671498
Tabata
Fermentative production of L-a ...
Bacillus subtilis
Appl. Environ. Microbiol.
73
6378-6385
2007
-
1
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
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-
1
-
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-
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-
-
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-
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-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
662037
Tabata
ywf in Bacillus subtilis codes ...
Bacillus subtilis, Bacillus subtilis 168
J. Bacteriol.
187
5195-5202
2005
-
-
1
-
-
-
2
3
-
2
1
-
-
7
-
-
1
-
-
-
-
-
4
1
1
1
-
-
1
1
-
-
-
-
-
-
-
1
-
-
-
-
-
2
-
3
-
2
1
-
-
-
-
1
-
-
-
-
4
1
1
1
-
-
1
1
-
-
-
-
-
-
-
-
733219
Steinborn
bac genes for recombinant baci ...
Bacillus amyloliquefaciens, Bacillus amyloliquefaciens ATCC 15841, Bacillus pumilus, Bacillus pumilus ATCC 7065, Bacillus subtilis, Bacillus subtilis 168, Bacillus subtilis A1/3, no activity in Bacillus amyloliquefaciens, no activity in Bacillus amyloliquefaciens GSB272, no activity in Bacillus coagulans, no activity in Bacillus licheniformis, no activity in Bacillus licheniformis ATCC 9789, no activity in Bacillus megaterium, no activity in Bacillus megaterium PV361, no activity in Bacillus pumilus, no activity in Bacillus pumilus ATCC 12140
Arch. Microbiol.
183
71-79
2005
-
-
3
-
1
-
-
-
-
3
-
8
-
21
-
-
-
-
-
-
-
-
8
-
-
-
-
-
-
-
-
3
-
-
-
-
-
4
4
-
1
-
-
-
-
-
-
4
-
8
-
-
-
-
-
-
-
-
8
-
-
-
-
-
-
-
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6
7
-
-
-