Research Compound

5-Amino-1MQ

NNMT Inhibitor · MW 174.2 g/mol

5-Amino-1MQ is a small-molecule inhibitor of nicotinamide N-methyltransferase (NNMT), an enzyme involved in cellular metabolism and energy regulation. Research has examined its role in adipogenesis, metabolic function, and NAD+ biosynthesis pathways. The compound has been studied in cell culture and rodent models for its effects on fat cell differentiation and metabolic signaling.

≥99% HPLC MS Confirmed 3rd Party Tested San Diego
Overview

What is 5-Amino-1MQ?

5-Amino-1MQ is a small-molecule inhibitor of nicotinamide N-methyltransferase (NNMT), an enzyme involved in cellular metabolism and energy regulation. Research has examined its role in adipogenesis, metabolic function, and NAD+ biosynthesis pathways. The compound has been studied in cell culture and rodent models for its effects on fat cell differentiation and metabolic signaling.

5-Amino-1MQ (5-Amino-1-Methylquinolinium) is supplied strictly as a reference material for in vitro and preclinical investigation. All characterization data described here is drawn from peer-reviewed literature and laboratory analysis; nothing herein constitutes a claim of clinical effect in humans.

Investigational Scope

Documented Research Areas

The following domains summarize directions explored across published studies and laboratory models. Each reflects observations reported in rodent models, in vitro systems, or the peer-reviewed record.

Metabolic

NNMT Inhibition & Adipogenesis

Studies in rodent models have documented 5-Amino-1MQ's inhibitory effect on NNMT, an enzyme upregulated in adipose tissue. Research observed reductions in fat cell size and adipogenesis markers in treated subjects.

NAD+ Biology

NAD+ Precursor Pathway

By inhibiting NNMT, 5-Amino-1MQ may preserve methyl groups and support NAD+ biosynthesis. Research has examined downstream effects on sirtuin activity and cellular energy metabolism.

Cellular

Energy Expenditure Models

In vitro studies have examined 5-Amino-1MQ's effects on mitochondrial function and energy expenditure markers in adipocyte cell lines, with observed changes in oxygen consumption rates.

Epigenetic

Methylation & Gene Expression

NNMT inhibition alters cellular methylation balance. Researchers have studied downstream effects on epigenetic regulation and gene expression patterns in metabolic disease models.

Proposed Mechanism

Mechanistic Pathway

Mechanistic steps below are hypothesized from in vitro assays and animal-model data reported in the literature. They describe biochemical interactions observed under controlled experimental conditions.

  1. 1

    NNMT Enzyme Inhibition

    5-Amino-1MQ competitively inhibits NNMT, which catalyzes the methylation of nicotinamide using S-adenosylmethionine (SAM). Inhibition preserves SAM availability and alters downstream methylation reactions.

  2. 2

    NAD+ Pathway Support

    Reduced NNMT activity decreases consumption of the NAD+ precursor nicotinamide, potentially increasing flux through the NAD+ biosynthesis pathway and supporting sirtuin-dependent metabolic processes.

  3. 3

    Adipocyte Differentiation Modulation

    Research has documented changes in adipocyte differentiation markers including PPAR-γ and C/EBPα expression following NNMT inhibition, suggesting a role in regulating fat cell formation.

  4. 4

    Mitochondrial Function

    In vitro studies have observed changes in mitochondrial respiration and energy expenditure in cells treated with 5-Amino-1MQ, consistent with altered metabolic enzyme activity.

Technical Data

Molecular Specifications

Amino Acid SequenceN/A
Molecular Weight174.2 g/mol
Molecular FormulaC₁₀H₁₀N₂
CAS Number1380437-86-4
Storage−20°C long-term, 4°C short-term up to 4 weeks
References

Selected Literature

The following peer-reviewed references informed the research summaries on this page. Citations are provided for scientific context only.

  1. Neelakantan H, et al. (2018). Selective and membrane-permeable small molecule inhibitors of nicotinamide N-methyltransferase reverse high fat diet-induced obesity in mice. Biochemical Pharmacology, 147, 141–152.
  2. Hong S, et al. (2015). Nicotinamide N-methyltransferase regulates hepatic nutrient metabolism through Sirt1 protein stabilization. Nature Medicine, 21(8), 887–894.
  3. Roberti A, et al. (2021). Epigenetics in cancer therapy and nanomedicine. Clinical Epigenetics, 11, 81.
  4. Campagna R, et al. (2021). NAD+ metabolism in aging and cancer. International Journal of Molecular Sciences, 22(13), 6829.
  5. Aksoy S, et al. (1994). Characterization of human liver nicotinamide N-methyltransferase. Biochemical Pharmacology, 47(7), 1023–1034.

Research Disclaimer

This product is intended strictly for laboratory research purposes only. It is not a drug, food, cosmetic, or dietary supplement and is not intended to diagnose, treat, cure, or prevent any disease. It is not for human or animal consumption. All information presented is derived from published scientific literature and is provided for educational reference only. By purchasing, the buyer affirms they are a qualified researcher or institution and assume full responsibility for the safe and lawful handling of this material.