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Related Concept Videos

Amino Acid Biosynthetic Pathways01:29

Amino Acid Biosynthetic Pathways

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Amino acid biosynthesis is essential for cell growth, protein synthesis, and metabolic regulation. Cells generate essential and non-essential amino acids from metabolic intermediates to sustain vital biological functions. These intermediates originate from key metabolic pathways: glycolysis, the tricarboxylic acid (TCA) cycle, and the pentose phosphate pathway. Important precursors include α-ketoglutarate, pyruvate, oxaloacetate, phosphoenolpyruvate, and erythrose-4-phosphate, which...
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Drugs Affecting GI Tract Motility: Serotonin Receptor Agonists01:23

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Serotonin, a crucial neurotransmitter synthesized by enterochromaffin cells, plays a cardinal role in regulating gastrointestinal (GI) motility. With over 90% of the body's total serotonin in the GI tract, its influence on digestive processes is profound. Serotonin is swiftly released upon various stimuli, such as food boluses or certain drugs, triggering intrinsic sensory neurons in the myenteric plexus and extrinsic vagal and spinal sensory neurons. This leads to the activation of the...
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Repressible Operon: trp Operon01:21

Repressible Operon: trp Operon

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The trp operon in Escherichia coli exemplifies a repressible operon. It regulates the synthesis of tryptophan through repressor-mediated transcriptional control and attenuation. This dual regulatory mechanism ensures tryptophan biosynthesis occurs only when needed, conserving cellular resources.Structure of the trp OperonThe trp operon consists of five structural genes (trpE, trpD, trpC, trpB, and trpA) that encode enzymes for tryptophan biosynthesis. These genes are transcribed as a single...
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Amino Acid Catabolism01:18

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Microorganisms rely on proteins as an essential carbon and energy source, particularly in environments with limited polysaccharides or lipids. However, proteins are too large to cross the plasma membrane unaided, necessitating enzymatic degradation. Microbes secrete extracellular proteases and peptidases that hydrolyze proteins into peptides, which can then be transported across the membrane. Once inside the cell, intracellular proteases degrade these peptides into free amino acids, which...
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Transduction01:16

Transduction

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Among the three main modes of HGT—transformation, conjugation, and transduction—transduction is unique in that it is mediated by bacteriophages, or bacterial viruses.Transduction occurs in two ways. Generalized transduction occurs during the lytic cycle of a bacteriophage infection. In this process, bacteriophages infect bacterial cells, replicate within them, and ultimately cause cell lysis, releasing newly assembled virions. Occasionally, random fragments of the bacterial genome...
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Inorganic Nitrogen Assimilation

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Nitrogen is an essential element in biological systems, forming a crucial component of proteins, nucleic acids, and other cellular constituents. Many bacteria and archaea acquire nitrogen in the form of nitrate (NO₃⁻) or ammonia (NH₃), which are then assimilated into biomolecules through specific enzymatic pathways.Assimilatory Nitrate ReductionWhen nitrate enters the cell, it undergoes a two-step reduction process known as assimilatory nitrate reduction. Initially, the enzyme...
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Related Experiment Video

Updated: Sep 17, 2025

Radiosynthesis of 1-2-[18F]Fluoroethyl-L-Tryptophan using a One-pot, Two-step Protocol
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Tryptamine Metabolism and Functionalization in Gut Commensal Bacteria Expand Human Tryptamine Signaling Responses.

Hyun Bong Park1,2,3, Deguang Song4, Mytien Nguyen4

  • 1Department of Chemistry, Yale University, New Haven, Connecticut 06520, United States.

ACS Chemical Biology
|June 27, 2025
PubMed
Summary

Researchers discovered new molecules from gut bacteria that activate human melatonin receptors and other targets. One molecule, 1, also inhibits an inflammatory enzyme and impacts CD8 T cells in mice.

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Last Updated: Sep 17, 2025

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PCR Mutagenesis, Cloning, Expression, Fast Protein Purification Protocols and Crystallization of the Wild Type and Mutant Forms of Tryptophan Synthase
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Chemical Modification of the Tryptophan Residue in a Recombinant Ca2+-ATPase N-domain for Studying Tryptophan-ANS FRET
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Area of Science:

  • Microbiology
  • Pharmacology
  • Immunology

Background:

  • Gut microbes produce diverse small molecules influencing human physiology.
  • The repertoire of known gut-derived functional molecules remains limited.
  • G protein-coupled receptors (GPCRs) are key targets for microbial metabolites.

Purpose of the Study:

  • To screen human fecal-derived bacterial supernatants for agonists of melatonin receptors MTNR1A and MTNR1B.
  • To identify and characterize novel small molecules from *Clostridium sporogenes* with GPCR agonist activity.

Main Methods:

  • Screening of bacterial supernatants for GPCR activity.
  • Bioactivity-assisted isolation and chemical characterization of metabolites.
  • Synthesis of identified compounds for structural confirmation.
  • GPCR screening and enzyme inhibition assays.
  • Single-cell RNA sequencing analysis in a mouse model.

Main Results:

  • Three tryptamine-derived metabolites (1-3) were identified from *C. sporogenes*, including two novel compounds.
  • Compound 2 activated melatonin receptors and P2RY11.
  • Compound 1 activated GPR55 and inhibited soluble epoxide hydrolase (sEH) with an IC50 of 420 nM.
  • Oral administration of compound 1 reduced GPR55+ and granzyme K+ CD8 T cells in mouse gut intraepithelial lymphocytes.

Conclusions:

  • This study expands the known chemical diversity of gut microbial metabolites.
  • Identified compounds modulate key host receptors and enzymes, impacting immune cell populations.
  • Tryptamine metabolism in gut bacteria represents a significant source of bioactive signaling molecules.