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Literature summary for 6.2.1.54 extracted from

  • Yonus, H.; Neumann, P.; Zimmermann, S.; May, J.J.; Marahiel, M.A.; Stubbs, M.T.
    Crystal structure of DltA: implications for the reaction mechanism of non-ribosomal peptide synthetase (NRPS) adenylation domains (2008), J. Biol. Chem., 283, 32484-32491.
    View publication on PubMed
Search for more literature for 6.2.1.54

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli as a His-tagged fusion protein Bacillus subtilis

Crystallization (Commentary)

Crystallization (Comment) Organism
protein is crystallized in the presence of substrates D-Ala, ATP and MgCl2. The structures of the reported DltA reveal the determinants for D-Ala substrate specificity, and confirm that the PCP-activating domains are able to adopt multiple conformational states, in this case corresponding to the thiolation reaction Bacillus subtilis

Protein Variants

Protein Variants Comment Organism
C268A mutant shows strong preference for D-Ala as a substrate, a high activity is also observed towards D-amino butyric acid (56%). Most significantly, the variant accepts the L-amino acids LAla (9.7%), L-amino butyric acid (6%) and L-Ser (7%). Turnover of D-Ser is reduced to 3% Bacillus subtilis
C268D mutant demonstrates a similar specificity profile to wild-type DltA, although with significantly lower activity Bacillus subtilis

Organism

Organism UniProt Comment Textmining
Bacillus subtilis P39581
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + D-2-amino butyric acid + diphosphate activity and specificity of DltA is investigated using the ATP-pyrophosphate exchange assay. Enzyme shows only minor activity 13% with D-amino butyric acid Bacillus subtilis ?
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 ?
ATP + D-Ala + diphosphate activity and specificity of DltA is investigated using the ATP-pyrophosphate exchange assay. Enzyme is highly specific for cognate D-Ala substrate Bacillus subtilis ?
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 ?
ATP + D-Ser + diphosphate activity and specificity of DltA is investigated using the ATP-pyrophosphate exchange assay. Enzyme shows only minor activity 13% with D-Ser Bacillus subtilis ?
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 ?

Synonyms

Synonyms Comment Organism
D-alanine:D-alanyl carrier protein ligase
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 Bacillus subtilis
DltA
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 Bacillus subtilis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
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 assay at Bacillus subtilis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.8
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 assay at Bacillus subtilis