| This synthetic peptide corresponds to a segment of GMC oxidoreductase (a flavin-dependent enzyme) derived from Streptomyces exfoliatus, a soil-dwelling actinomycete known for its metabolic versatility. GMC (glucose–methanol–choline) oxidoreductases are a large enzyme superfamily that shares structural features and catalyze diverse oxidation-reduction reactions via a bound FAD cofactor. Multiple GMC oxidoreductase-like genes have been identified in the genome of S. exfoliatus, including N-terminal-domain–containing variants associated with secondary metabolite gene clusters. While the precise functional role of this specific peptide is not yet characterized in the literature, its design suggests it may represent a bioactive fragment of the larger GMC oxidoreductase. Peptides like this are often used to mimic protein domains—particularly for antibody development, epitope mapping, or functional assays. Given its origin from the N-terminal domain of a GMC enzyme, the peptide may correspond to a structural motif involved in FAD binding or substrate recognition—both critical for enzymatic activity.
Peptide KTYLAQAAATG is part of GMC oxidoreductase.
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