Literature summary for 6.3.2.49 extracted from

Suzuki, M.; Takahashi, Y.; Noguchi, A.; Arai, T.; Yagasaki, M.; Kino, K.; Saito, J.
The structure of L-amino-acid ligase from Bacillus licheniformis (2012), Acta Crystallogr. Sect. D, 68, 1535-1540.

Cloned(Commentary)

Cloned (Comment)	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 (Comment)	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

Crystallization (Comment)

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	Comment	Organism	Structure
Mg2+	required	Bacillus licheniformis

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
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	UniProt	Comment	Textmining
Bacillus licheniformis	Q65D11	gene BL00235	-
Bacillus licheniformis NBRC 12200	Q65D11	gene BL00235	-

Purification (Commentary)

Purification (Comment)	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	Comment Substrates	Organism	Products	Comment (Products)	Rev.
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	the enzyme catalyzes the formation of an alpha-peptide bond between two L-amino acids in an ATP-dependent manner	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	-	?
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	Bacillus licheniformis NBRC 12200	ADP + phosphate + L-aminoacyl-L-amino acid	-	?

Synonyms

Synonyms	Comment	Organism
L-amino-acid ligase	-	Bacillus licheniformis
LAL	-	Bacillus licheniformis
LAL BL00235	-	Bacillus licheniformis

Cofactor

Cofactor	Comment	Organism	Structure
ATP	ATP-binding site structure, overview	Bacillus licheniformis

General Information

General Information	Comment	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