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Literature summary for 6.3.2.49 extracted from

  • Kino, K.; Noguchi, A.; Nakazawa, Y.; Yagasaki, M.
    A novel L-amino acid ligase from Bacillus licheniformis (2008), J. Biosci. Bioeng., 106, 313-315.
    View publication on PubMed
Search for more literature for 6.3.2.49

Cloned(Commentary)

Cloned (Comment) Organism
expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3) Bacillus licheniformis

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+
-
 Bacillus licheniformis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + L-leucine + an L-amino acid Bacillus licheniformis the enzyme catalyzes the formation of an alpha-peptide bond in unprotected L-amino acids in an ATP-dependent manner, the substrate specificity of BL00235 is strict, only methionine or leucine are accepted as dipeptide N-terminal residues, overview ADP + phosphate + L-leucyl-L-amino acid
-
 ?
ATP + L-leucine + an L-amino acid Bacillus licheniformis NBRC12200 the enzyme catalyzes the formation of an alpha-peptide bond in unprotected L-amino acids in an ATP-dependent manner, the substrate specificity of BL00235 is strict, only methionine or leucine are accepted as dipeptide N-terminal residues, overview ADP + phosphate + L-leucyl-L-amino acid
-
 ?
ATP + L-methionine + an L-amino acid Bacillus licheniformis the enzyme catalyzes the formation of an alpha-peptide bond in unprotected L-amino acids in an ATP-dependent manner, the substrate specificity of BL00235 is strict, only methionine or leucine are accepted as dipeptide N-terminal residues, overview ADP + phosphate + L-methionyl-L-amino acid
-
 ?
ATP + L-methionine + an L-amino acid Bacillus licheniformis NBRC12200 the enzyme catalyzes the formation of an alpha-peptide bond in unprotected L-amino acids in an ATP-dependent manner, the substrate specificity of BL00235 is strict, only methionine or leucine are accepted as dipeptide N-terminal residues, overview ADP + phosphate + L-methionyl-L-amino acid
-
 ?

Organism

Organism UniProt Comment Textmining
Bacillus licheniformis
-
 gene BL00235
-
Bacillus licheniformis NBRC12200
-
 gene BL00235
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration Bacillus licheniformis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-asparagine + L-methionine
-
 Bacillus licheniformis ADP + phosphate + L-asparaginyl-L-methionine
-
 ?
ATP + L-asparagine + L-methionine
-
 Bacillus licheniformis NBRC12200 ADP + phosphate + L-asparaginyl-L-methionine
-
 ?
ATP + L-leucine + an L-amino acid the enzyme catalyzes the formation of an alpha-peptide bond in unprotected L-amino acids in an ATP-dependent manner, the substrate specificity of BL00235 is strict, only methionine or leucine are accepted as dipeptide N-terminal residues, overview Bacillus licheniformis ADP + phosphate + L-leucyl-L-amino acid
-
 ?
ATP + L-leucine + an L-amino acid the enzyme catalyzes the formation of an alpha-peptide bond in unprotected L-amino acids in an ATP-dependent manner, the substrate specificity of BL00235 is strict, only methionine or leucine are accepted as dipeptide N-terminal residues, overview Bacillus licheniformis NBRC12200 ADP + phosphate + L-leucyl-L-amino acid
-
 ?
ATP + L-leucine + L-alanine
-
 Bacillus licheniformis ADP + phosphate + L-leucyl-L-alanine
-
 ?
ATP + L-leucine + L-alanine
-
 Bacillus licheniformis NBRC12200 ADP + phosphate + L-leucyl-L-alanine
-
 ?
ATP + L-methionine + an L-amino acid the enzyme catalyzes the formation of an alpha-peptide bond in unprotected L-amino acids in an ATP-dependent manner, the substrate specificity of BL00235 is strict, only methionine or leucine are accepted as dipeptide N-terminal residues, overview Bacillus licheniformis ADP + phosphate + L-methionyl-L-amino acid
-
 ?
ATP + L-methionine + an L-amino acid the enzyme catalyzes the formation of an alpha-peptide bond in unprotected L-amino acids in an ATP-dependent manner, the substrate specificity of BL00235 is strict, only methionine or leucine are accepted as dipeptide N-terminal residues, overview Bacillus licheniformis NBRC12200 ADP + phosphate + L-methionyl-L-amino acid
-
 ?
ATP + L-methionine + glycine
-
 Bacillus licheniformis ADP + phosphate + L-methionyl-glycine
-
 ?
ATP + L-methionine + L-alanine best substrate combination Bacillus licheniformis ADP + phosphate + L-methionyl-L-alanine
-
 ?
ATP + L-methionine + L-cysteine
-
 Bacillus licheniformis ADP + phosphate + L-methionyl-L-cysteine
-
 ?
ATP + L-methionine + L-leucine
-
 Bacillus licheniformis ADP + phosphate + L-methionyl-L-leucine
-
 ?
ATP + L-methionine + L-methionine
-
 Bacillus licheniformis ADP + phosphate + L-methionyl-L-methionine
-
 ?
ATP + L-serine + L-methionine
-
 Bacillus licheniformis ADP + phosphate + L-seryl-L-methionine
-
 ?
ATP + L-threonine + L-methionine
-
 Bacillus licheniformis ADP + phosphate + L-threonyl-L-methionine
-
 ?
additional information the enzyme catalyzes the formation of an alpha-peptide bond in unprotected L-amino acids in an ATP-dependent manner, the substrate specificity of BL00235 is very strict, overview Bacillus licheniformis ?
-
 ?
additional information the enzyme catalyzes the formation of an alpha-peptide bond in unprotected L-amino acids in an ATP-dependent manner, the substrate specificity of BL00235 is very strict, overview Bacillus licheniformis NBRC12200 ?
-
 ?

Synonyms

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

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
-
 Bacillus licheniformis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
9
-
-
 Bacillus licheniformis

Cofactor

Cofactor Comment Organism Structure
ATP
-
 Bacillus licheniformis