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Literature summary for 5.1.1.11 extracted from

  • Kanda, M.; Hori, K.; Kurotsu, T.; Yamada, Y.; Miura, S.; Saito, Y.
    Essential arginine residue in gramicidin S synthetase I of Bacillus brevis (1982), J. Biochem., 91, 939-943.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
Phenylglyoxal inhibition of Phe activation. Both ATP and Phe prevent the inactivation. ATP is competitive with phenylglyoxal, whereas Phe is not. A single arginine residue of GS 1 is essential for Phe activation in binding the phosphate moiety of ATP Brevibacillus brevis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + L-phenylalanine + H2O Brevibacillus brevis phenylalanine racemase, i.e. gramicidin-S synthetase 1, activates and transfers D-Phe to the heavy enzyme, gramicidin S-synthetase 2, which activates the other constituent amino acids on the thioester template ?
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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-Phe + H2O
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Brevibacillus brevis AMP + diphosphate + D-Phe
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?
ATP + L-phenylalanine + H2O phenylalanine racemase, i.e. gramicidin-S synthetase 1, activates and transfers D-Phe to the heavy enzyme, gramicidin S-synthetase 2, which activates the other constituent amino acids on the thioester template Brevibacillus brevis ?
-
?