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Literature summary for 6.3.2.49 extracted from

  • Tsuda, T.; Asami, M.; Koguchi, Y.; Kojima, S.
    Single mutation alters the substrate specificity of L-amino acid ligase (2014), Biochemistry, 53, 2650-2660.
    View publication on PubMed

Application

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 (Commentary)

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

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/ Products (Substrates)

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 ?
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?

Organism

Organism UniProt Comment Textmining
Bacillus subtilis
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-alanine + L-anticapsin
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Bacillus subtilis ADP + phosphate + bacilysin
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?
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 ?
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?
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 ?
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?

Synonyms

Synonyms Comment Organism
L-amino acid ligase
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Bacillus subtilis
LAL
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Bacillus subtilis
YwfE
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Bacillus subtilis

Cofactor

Cofactor Comment Organism Structure
ATP
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Bacillus subtilis

General Information

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