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Literature summary for 6.3.2.49 extracted from

  • Kino, K.; Arai, T.; Tateiwa, D.
    A novel L-amino acid ligase from Bacillus subtilis NBRC3134 catalyzed oligopeptide synthesis (2010), Biosci. Biotechnol. Biochem., 74, 129-134.
    View publication on PubMed
Search for more literature for 6.3.2.49

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli BL21 Bacillus subtilis

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required for enzyme activity Bacillus subtilis

Organism

Organism UniProt Comment Textmining
Bacillus subtilis C0STU2 NBRC3134
-
Bacillus subtilis NBRC3134 C0STU2 NBRC3134
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + an L-amino acid + an L-amino acid assay at pH 8.0, 30°C Bacillus subtilis ADP + phosphate + L-aminoacyl-L-amino acid
-
 ?
ATP + an L-amino acid + an L-amino acid assay at pH 8.0, 30°C Bacillus subtilis NBRC3134 ADP + phosphate + L-aminoacyl-L-amino acid
-
 ?

Synonyms

Synonyms Comment Organism
L-amino acid ligase
-
 Bacillus subtilis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
40
-
-
 Bacillus subtilis

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
20 50 significant decrease in activity above 45°C Bacillus subtilis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
 assay at Bacillus subtilis

pH Range

pH Minimum pH Maximum Comment Organism
9 9.5 enzyme activity decreased sharply above pH 10.0 Bacillus subtilis

General Information

General Information Comment Organism
physiological function involved in rhizocticin biosynthesis Bacillus subtilis