L-tryptophan is the only protein amino acid (AA) containing an indole ring; through biotransformation in living things, it either aids in maintaining this chemical group in cells and tissues or degrades it by releasing a range of bioactive chemicals in both cases. Trp's small derivatives have a pleiotropic effect on homeostasis systems, according to studies on its biology. The pathways of Trp indole derivatives in humans are involved in protein turnover as well as the synthesis of the neurotransmitter and hormone serotonin (5-HT), the pineal gland hormone melatonin (MLT), and the trace amine tryptamine. Instead, the breakdown of the Trp indole ring is what defines the "kynurenine shunt," which produces cell-response adapters such L-kynurenine, kynurenic, and quinolinic acids, or the coenzyme nicotinamide adenine dinucleotide (NAD+). Bioremediation is one of the most promising methods for using potent, highly efficient microorganisms to clean up contaminated environments (Pavia CS et al., 2020).
Microbes may degrade the highly toxic heterocyclic compound nicotine and other tobacco alkaloids utilising specific enzymes and metabolic pathways. Following the metabolic conversion, these nicotinophilic bacteria utilise nicotine as their only source of carbon, nitrogen, and energy. Some of the known mechanisms for the breakdown of nicotine include the demethylation process in fungi, the pyridine pathway in Gram-positive bacteria, the pyrrolidine pathway, and variations of the pyridine and pyrrolidine pathways in Gram-negative bacteria. We discussed the enzymes and microorganisms that degrade nicotine as well as the biotechnological applications of nicotine intermediate metabolites (Gurusamy R et al., 2013).
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