RESEARCH MONOGRAPH · KDC-MN-014

5-Amino-1MQ

May 9, 2026 Kodiac biolabs Research Revised May 30, 2026 2 min read

Our opinion on this compound

68/100

Selective NNMT inhibitor with real biology and one of the most interesting metabolic mechanisms of the decade

5-amino-1-methylquinolinium (5-Amino-1MQ) is a designed selective inhibitor of nicotinamide N-methyltransferase (NNMT), an enzyme that's emerged over the last decade as a surprisingly central node in adipose-tissue metabolic signaling. The Nawrocki and Heinrich-Pinhas labs did much of the foundational target validation work, showing that NNMT inhibition shifts adipocyte metabolic state away from lipid storage and toward energy expenditure.

Mechanism is genuinely interesting. NNMT consumes SAM (S-adenosylmethionine) and produces methylnicotinamide (MNAM) plus SAH. By methylating nicotinamide, NNMT acts as a kind of NAD+ sink (since nicotinamide is normally salvaged back into NAD+), and elevated NNMT activity in adipocytes is associated with insulin resistance, lipid accumulation, and the metabolic syndrome phenotype. Inhibiting NNMT restores NAD+ flux, lifts SAM tone, and shifts adipocyte gene expression toward thermogenic programs.

5-Amino-1MQ is the most-characterized small-molecule inhibitor in this class. Selectivity over related methyltransferases is reasonable, oral bioavailability is documented in mouse studies, and the in-vivo metabolic effects (improved insulin sensitivity, reduced adipose mass, increased energy expenditure) are real and replicated across multiple research groups. The Kraus group and others have extended the mechanism work into skeletal muscle and senescence contexts.

Human data is essentially nonexistent at this point, which is the major caveat. All the metabolic readouts are from mouse and cell models. NNMT inhibitor programs are moving toward clinic at several biotechs (most notably a few startups in the metabolic-disease space), but 5-Amino-1MQ specifically isn't the clinical lead, it's the academic tool compound.

Sourcing in capsule format is moderately variable. The chemistry is straightforward (it's a substituted quinolinium salt), but the source material can have impurities from the quaternization step, and not every vendor characterizes the salt form clearly. HPLC purity should be easy to verify but COA quality varies. We've seen issues with hygroscopic packaging in some lots.

What we like is that this is a real mechanism with real preclinical validation, not vibes. What we don't like is the gap between preclinical promise and clinical evidence, which is wide.

Genuinely interesting research tool. Don't extrapolate to human outcomes yet.

Evidence: 50
Mechanism: 80
Reliability: 70
Safety: 65
Sourcing: 65
Value: 65
Signal: 75
Staying power: 75

Plain-language summary Intrigue 72 / 100

5-Amino-1MQ is a small molecule that selectively inhibits the NNMT enzyme. NNMT degrades NAD+ precursors and methyl donors; inhibiting it boosts cellular energy and fat metabolism, with research interest in obesity and metabolic disease. Capsule format here. Stocked in the Kodiac catalog as a research-only powder for laboratory work; not a medicine, not for human consumption.

Intrigue 0–100 blends mechanism novelty, evidence strength, and translational potential. Kodiac editorial, not peer-reviewed.

Small-molecule selective NNMT inhibitor (capsule format)

A 159 Da quinolinium small molecule that selectively inhibits nicotinamide N-methyltransferase, characterized for effects on adipose metabolism and skeletal muscle stem cell function. Supplied as 60 capsules x 50 mg.

Abstract

5-Amino-1-methylquinolinium iodide (5-Amino-1MQ; CAS 954126-98-8; molecular formula C11H12N2; molecular weight 159.20 for the cation; the iodide salt has additional mass) is a small-molecule selective inhibitor of nicotinamide N-methyltransferase (NNMT, EC 2.1.1.1), the enzyme that methylates nicotinamide to N1-methylnicotinamide using S-adenosylmethionine (SAM) as the methyl donor. NNMT activity diverts nicotinamide away from the NAD+ salvage pathway and consumes SAM, which connects NNMT activity to both the cellular NAD+ pool and the methylation potential of the cell. NNMT is overexpressed in many cancers (where it has been characterized as an "oncometabolic" enzyme) and in obesity-associated white adipose tissue, where it has been linked to insulin resistance and to the metabolic dysfunction phenotype. Selective NNMT inhibitors including 5-Amino-1MQ have been developed primarily by academic medicinal chemistry groups beginning in the late 2010s and have been characterized in cell culture, in vivo rodent obesity and aging models, and in skeletal muscle stem cell and aging models. The compound is supplied at Kodiac biolabs as a 60-capsule oral preparation, 50 milligrams per capsule, reflecting the small molecule's stability and oral bioavailability. There is no FDA-approved IND for 5-Amino-1MQ in any indication. The compound is not a regulated drug substance in the United States, the European Union, or Japan. The principal limitations on the strength of the evidence are the relatively short duration of the published research record and the limited human safety and efficacy data.

Read the full monograph

The full reference document covers compound identification, discovery and developmental history, mechanism of action, pharmacokinetics, reported research dose ranges, sourcing and quality verification, reconstitution and handling, stack interaction considerations, and a curated reference list. Available as a research-use-only PDF download.

KDC-MN-014

The full reference document is provided strictly for research use only. It reports research dose ranges from the published literature, not instructions for use in humans or animals.

Download PDF →

Acquire 5-Amino-1MQ from the catalog

View 5-Amino-1MQ →

FOR RESEARCH USE ONLY. Not for medical, diagnostic, or therapeutic purposes. Not for human consumption. All information is provided for research and educational purposes only.

Kodiac sells research compounds for investigative use only.

5-Amino-1MQ

Abstract

Read the full monograph

Quick actions

Categories

Help and policies

Abstract

Read the full monograph

Adjacent monographs