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Literature summary for 5.1.1.11 extracted from

  • Luo, L.; Walsh, C.T.
    Kinetic analysis of three activated phenylalanyl intermediates generated by the initiation module PheATE of gramicidin S synthetase (2001), Biochemistry, 40, 5329-5337.
    View publication on PubMed

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + L-phenylalanine + H2O Brevibacillus brevis the three-domain initiation module PheATE of gramicidin S synthetase catalyzes the activation, thiolation and epimerization of L-phenylalanine, the first amino acid incorporated into the decapeptide antibiotic gramicidin S AMP + diphosphate + D-phenylalanine
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Organism

Organism UniProt Comment Textmining
Brevibacillus brevis
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-phenylalanine + H2O there are three activated intermediates: L-phenylalanyl-adenosine-5'-monophosphate diester, L-Phe-S-4'-phosphopantetheine and D-Phe-S-4'-phosphopantetheine-acyl enzyme Brevibacillus brevis AMP + diphosphate + D-phenylalanine
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ATP + L-phenylalanine + H2O the three-domain initiation module PheATE of gramicidin S synthetase catalyzes the activation, thiolation and epimerization of L-phenylalanine, the first amino acid incorporated into the decapeptide antibiotic gramicidin S Brevibacillus brevis AMP + diphosphate + D-phenylalanine
-
?