Bacterial Substrate

Gly-Ala-Tyr (H-Gly-Ala-Tyr-OH) is a tripeptide substrate composed of L-glycine, alanine, and L-tyrosine joined in sequence by peptide linkages. Gly-Ala-Tyr can be hydrolyzed at both extracellular and intracellular levels by Streptococcus thermophilus, Lactobacillus delbrueckii ssp. bulgaricus, Lactobacillus acidophilus, and Bifidobacterium spp. Ala-Gly-Tyr is functionally related to L-alanine, glycine and L-tyrosine..

RMR-Tre is a fluorescent probe targeting the mycobacterial acyltransferase Ag85. Under the catalysis of Ag85, RMR-Tre undergoes 6-position mycoloylation and anchors to the mycobacterial membrane, while achieving fluorescence activation by inhibiting the intramolecular twisted charge transfer state transition. RMR-Tre can distinguish live mycobacteria from dead ones through metabolism-driven labeling, enabling rapid, wash-free, low-background detection of viable bacteria. RMR-Tre reports the drug resistance of Mycobacterium tuberculosis via the trehalose catalytic shift activity readout associated with TreS. In addition, RMR-Tre can be combined with flow cytometry or high-content imaging techniques to visualize and quantitatively analyze the metabolic heterogeneity of Mycobacterium tuberculosis related to persistence and drug resistance. RMR-Tre is widely used in tuberculosis-related research.