Product Description | 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. |
Scientific Background | KTYLAQAAATG is a 11-residue synthetic peptide with the sequence Lys-Thr-Tyr-Leu-Ala-Gln-Ala-Ala-Ala-Thr-Gly. C-terminal amidation removes the terminal carboxylate charge. The sequence has a relatively high hydrophobic-residue fraction that can influence aqueous solubility and surface adsorption. These sequence-derived properties describe the reagent chemically; no specific receptor, enzyme, pathway, disease association, or biological activity is assigned without product-specific experimental evidence. |
Experimental Notes | Sequence-derived chemical properties support reagent selection and experimental planning but do not establish biological function. Solubility, aggregation, adsorption, conjugation efficiency, and assay performance should be validated under the intended experimental conditions. |
