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Literature summary extracted from

  • Tabata, K.; Ikeda, H.; Hashimoto, S.
    ywf in Bacillus subtilis codes for a novel enzyme, L-amino acid ligase (2005), J. Bacteriol., 187, 5195-5202.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
6.3.2.49 expression in Escherichia coli Bacillus subtilis

Inhibitors

EC Number Inhibitors Comment Organism Structure
6.3.2.49 CdSO4 2 mM, complete inhibition Bacillus subtilis
6.3.2.49 ZnSO4 2 mM, complete inhibition Bacillus subtilis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
6.3.2.49 0.07
-
 L-glutamine pH 9.0, 37°C Bacillus subtilis
6.3.2.49 0.42
-
 ATP pH 9.0, 37°C Bacillus subtilis
6.3.2.49 105
-
 L-alanine pH 9.0, 37°C Bacillus subtilis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
6.3.2.49 Mg2+ Mg2+ or Mn2+ is essential for activity Bacillus subtilis
6.3.2.49 Mn2+ Mg2+ or Mn2+ is essential for activity Bacillus subtilis

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
6.3.2.49 53000
-
 x * 53000, SDS-PAGE Bacillus subtilis

Organism

EC Number Organism UniProt Comment Textmining
6.3.2.49 Bacillus subtilis P39641
-
-
6.3.2.49 Bacillus subtilis 168 P39641
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
6.3.2.49
-
 Bacillus subtilis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.3.2.49 ATP + L-alanine + L-glutamine GTP does not substitute for ATP Bacillus subtilis ADP + phosphate + L-alanyl-L-glutamine
-
 ?
6.3.2.49 ATP + L-alanine + L-glutamine GTP does not substitute for ATP Bacillus subtilis 168 ADP + phosphate + L-alanyl-L-glutamine
-
 ?
6.3.2.49 additional information while the enzyme has extremely broad substrate specificity, some preferences are observed; the enzyme does not accept highly charged amino acids such as Lys, Arg, Glu, and Asp. The enzyme does not react with secondary amines such as Pro. The N-terminal residue of the dipeptide formed seems to be limited to Ala, Gly, Ser, Thr, and Met whereas the C-terminal residue seems to allow for a wider array of amino acids; and Ala and Ser seems to be most preferred for the N-terminal residue while Met and Phe seems to be preferred for the C-terminus. The enzyme does not react with D-Ala, D-serine, or D-phenylalanine Bacillus subtilis ?
-
 ?
6.3.2.49 additional information while the enzyme has extremely broad substrate specificity, some preferences are observed; the enzyme does not accept highly charged amino acids such as Lys, Arg, Glu, and Asp. The enzyme does not react with secondary amines such as Pro. The N-terminal residue of the dipeptide formed seems to be limited to Ala, Gly, Ser, Thr, and Met whereas the C-terminal residue seems to allow for a wider array of amino acids; and Ala and Ser seems to be most preferred for the N-terminal residue while Met and Phe seems to be preferred for the C-terminus. The enzyme does not react with D-Ala, D-serine, or D-phenylalanine Bacillus subtilis 168 ?
-
 ?

Subunits

EC Number Subunits Comment Organism
6.3.2.49 ? x * 53000, SDS-PAGE Bacillus subtilis

Synonyms

EC Number Synonyms Comment Organism
6.3.2.49 YwfE
-
 Bacillus subtilis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
6.3.2.49 37
-
-
 Bacillus subtilis

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
6.3.2.49 25 45 25°C: about 70% of maximal activity, 45°C: about 55% of maximal activity Bacillus subtilis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
6.3.2.49 9.5
-
-
 Bacillus subtilis

pH Range

EC Number pH Minimum pH Maximum Comment Organism
6.3.2.49 8.5 10.5 pH 8.5: about 70% of maximal activity, pH 10.5: about 35% of maximal activity Bacillus subtilis