6.3.2.49: L-alanine-L-anticapsin ligase
This is an abbreviated version!
For detailed information about L-alanine-L-anticapsin ligase, go to the full flat file.
Word Map on EC 6.3.2.49
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6.3.2.49
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dipeptide
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unprotected
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l-alanyl-l-glutamine
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oligopeptide
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atp-grasp
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rhizocticins
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ligases
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licheniformis
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bacilysin
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synthesis
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branched-chain
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syringae
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alpha-peptide
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taste
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d-amino
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homo-oligomers
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l-glutamine
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adolescentis
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met-gly
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l-asparagine
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ala-gln
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pharmacology
- 6.3.2.49
- dipeptide
-
unprotected
- l-alanyl-l-glutamine
- oligopeptide
-
atp-grasp
-
rhizocticins
- ligases
- licheniformis
- bacilysin
- synthesis
-
branched-chain
- syringae
- alpha-peptide
-
taste
-
d-amino
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homo-oligomers
- l-glutamine
- adolescentis
- met-gly
- l-asparagine
- ala-gln
- pharmacology
Reaction
Synonyms
alanine-anticapsin ligase, BacD, BL00235, BSU37710, EC 6.3.2.28, L-Ala-L-aniticapsin ligase, L-alanine-L-aniticapsin ligase, L-amino acid alpha-ligase, L-amino acid ligase, L-amino-acid ligase, LAL, LAL BL00235, RSp1486a, TabS, YwfE
ECTree
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General Information
General Information on EC 6.3.2.49 - L-alanine-L-anticapsin ligase
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evolution
malfunction
physiological function
additional information
mutation of the bacD gene or transformation of the bacABC genes into a Bacillus subtilis D (ywfAbacABCDE) deletion mutant leads to the accumulation of anticapsin, which is 4fold higher after transformation of the bacABC genes into a bacD mutant
malfunction
mutation of the bacD gene or transformation of the bacABC genes into a Bacillus subtilis D (ywfAbacABCDE) deletion mutant leads to the accumulation of anticapsin, which is 4fold higher after transformation of the bacABC genes into a bacD mutant
malfunction
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mutation of the bacD gene or transformation of the bacABC genes into a Bacillus subtilis D (ywfAbacABCDE) deletion mutant leads to the accumulation of anticapsin, which is 4fold higher after transformation of the bacABC genes into a bacD mutant
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malfunction
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mutation of the bacD gene or transformation of the bacABC genes into a Bacillus subtilis D (ywfAbacABCDE) deletion mutant leads to the accumulation of anticapsin, which is 4fold higher after transformation of the bacABC genes into a bacD mutant
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physiological function
the enzyme shows antibiotic activity against various indicator strains as Candida albicans CAP1-312, Escherica coli B, Escherichia coli K12, Proteus mirabilis, Proteus vulgaris, Sthapylococcus aureus, Streptomyces typhimurium, or Saccharomces cerevisiae
physiological function
the enzyme shows antibiotic activity against various indicator strains as Escherica coli B, Escherichia coli K12, Proteus mirabilis, Proteus vulgaris, Staphylococcus aureus, Salmonella typhimurium, or Saccharomyces cerevisiae
physiological function
the enzyme shows antibiotic activity against various indicator strains as Escherica coli B, Escherichia coli K12, Proteus mirabilis, Proteus vulgaris, Staphylococcus aureus, Salmonella typhimurium, or Saccharomyces cerevisiae
physiological function
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the enzyme shows antibiotic activity against various indicator strains as Escherica coli B, Escherichia coli K12, Proteus mirabilis, Proteus vulgaris, Sthapylococcus aureus, Streptomyces typhimurium, or Saccharomces cerevisiae
physiological function
-
the enzyme shows antibiotic activity against various indicator strains as Candida albicans CAP1-312, Escherica coli B, Escherichia coli K12, Proteus mirabilis, Proteus vulgaris, Sthapylococcus aureus, Streptomyces typhimurium, or Saccharomces cerevisiae
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physiological function
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the enzyme shows antibiotic activity against various indicator strains as Escherica coli B, Escherichia coli K12, Proteus mirabilis, Proteus vulgaris, Sthapylococcus aureus, Streptomyces typhimurium, or Saccharomces cerevisiae
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physiological function
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the enzyme shows antibiotic activity against various indicator strains as Escherica coli B, Escherichia coli K12, Proteus mirabilis, Proteus vulgaris, Staphylococcus aureus, Salmonella typhimurium, or Saccharomyces cerevisiae
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physiological function
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the enzyme shows antibiotic activity against various indicator strains as Escherica coli B, Escherichia coli K12, Proteus mirabilis, Proteus vulgaris, Staphylococcus aureus, Salmonella typhimurium, or Saccharomyces cerevisiae
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molecular basis of the substrate specificity, overview, ATP- and dipeptide-binding site structures, overview
additional information
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molecular basis of the substrate specificity, overview, ATP- and dipeptide-binding site structures, overview
additional information
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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
additional information
physiological prevention of suicidal antibiotic effects, e.g. for enzyme-deficient strain GSB322 with plasmid pSB674(bacABCD), overview
additional information
physiological prevention of suicidal antibiotic effects, e.g. for enzyme-deficient strain GSB322 with plasmid pSB674(bacABCD), overview
additional information
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physiological prevention of suicidal antibiotic effects, e.g. for enzyme-deficient strain GSB322 with plasmid pSB674(bacABCD), overview
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additional information
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molecular basis of the substrate specificity, overview, ATP- and dipeptide-binding site structures, overview
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