Literature summary 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.

Inhibitors

EC Number	Inhibitors	Comment	Organism	Structure
5.1.1.11	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)

EC Number	Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
5.1.1.11	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	?	-	?

Organism

EC Number	Organism	UniProt	Comment	Textmining
5.1.1.11	Brevibacillus brevis	-	-	-

Substrates and Products (Substrate)

EC Number	Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
5.1.1.11	ATP + L-Phe + H2O	-	Brevibacillus brevis	AMP + diphosphate + D-Phe	-	?
5.1.1.11	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	?	-	?

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Release 2023.1 (January 2023)