The adenylation domain of the enzyme catalyses the activation of L-tryptophan to (L-tryptophyl)adenylate, followed by the transfer of the activated compound to the free thiol of a phosphopantetheine arm of a peptidyl-carrier protein domain. The peptidyl-carrier protein domain may be part of the same protein, or of a different protein. This activity is often found as part of a larger non-ribosomal peptide synthase.
The expected taxonomic range for this enzyme is: Streptomyces griseovariabilis subsp. bandungensis
The adenylation domain of the enzyme catalyses the activation of L-tryptophan to (L-tryptophyl)adenylate, followed by the transfer of the activated compound to the free thiol of a phosphopantetheine arm of a peptidyl-carrier protein domain. The peptidyl-carrier protein domain may be part of the same protein, or of a different protein. This activity is often found as part of a larger non-ribosomal peptide synthase.
during biosynthesis of echinomycin, the beginning precursor, L-tryptophan is loaded onto non-ribosomal peptide synthase protein Qui18, which contains both adenylation and PCP domains. The adenylation domain activates L-tryptophan by adenylation and subsequently catalyzes the formation of a thioester bond between the carbonyl group of adenylated tryptophan and the thiol group of phosphopantetheine on PCP domain and thereby loading tryptophan onto the PCP domain of Qui18 to form tryptophanyl-S-Qui18. Enzyme Qui18 interacts with MbtH-like protein Qui5. Two subunits of Qui5 and two subunits of Qui18 form a hetero-tetramer
In vitro characterization of echinomycin biosynthesis formation and hydroxylation of L-tryptophanyl-S-enzyme and oxidation of (2S,3S) beta-hydroxytryptophan
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