Application | Comment | Organism |
---|---|---|
synthesis | enzyme Trp332 mutants can alter the substrate specificity and activity depending on the size and shape of substituted amino acids, scope for the rational design of the enzyme to produce desirable dipeptides, the positioning of the conserved Arg residue in L-aminoa cid ligase is important for enantioselective recognition of L-amino acids | Bacillus subtilis |
Crystallization (Comment) | Organism |
---|---|
YwfE with bound ADP-Mg2+-phosphate and ADP-Mg2+-L-Ala, X-ray diffraction structure determination and analysis at 1.9 and 2.0 A resolution, respectively | Bacillus subtilis |
Protein Variants | Comment | Organism |
---|---|---|
Y332A | site-directed mutagenesis, mutation of Trp332 to Ala causes the enzyme to hydrolyze ATP, even in the absence of L-Ala, and the structure of this mutant protein show a cavity in the N-terminal substrate-binding pocket | Bacillus subtilis |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | Bacillus subtilis | L-amino acid ligase catalyzes the formation of a dipeptide from two L-amino acids in an ATP-dependent manner, it produces the dipeptide antibiotic bacilysin, which consists of L-Ala and L-anticapsin | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Bacillus subtilis | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + L-alanine + L-anticapsin | - |
Bacillus subtilis | ADP + phosphate + bacilysin | - |
? | |
additional information | L-amino acid ligase catalyzes the formation of a dipeptide from two L-amino acids in an ATP-dependent manner, it produces the dipeptide antibiotic bacilysin, which consists of L-Ala and L-anticapsin | Bacillus subtilis | ? | - |
? | |
additional information | the substrate specificity is restricted to smaller amino acids such as L-Ala for the N-terminal end of the dipeptide, whereas a wide range of hydrophobic amino acids including L-Phe and L-Met are recognized for the C-terminal end in vitro | Bacillus subtilis | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
L-amino acid ligase | - |
Bacillus subtilis |
LAL | - |
Bacillus subtilis |
YwfE | - |
Bacillus subtilis |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
ATP | - |
Bacillus subtilis |
General Information | Comment | Organism |
---|---|---|
evolution | the enzyme belongs to the ATP-grasp superfamily | Bacillus subtilis |
additional information | conserved residue Arg328 is suggested to be a crucial residue for L-Ala recognition and catalysis. Residue Trp332 plays a key role in restricting the substrate specificity to smaller amino acids such as L-Ala. Trp332 mutants can alter the substrate specificity and activity depending on the size and shape of substituted amino acids, the positioning of the conserved Arg residue is important for enantioselective recognition of L-amino acids | Bacillus subtilis |