Details of the Drug-Related molecule(s) Interaction Atlas

General Information of Drug (ID: DM1EZ3N)

Drug Name

Namn Drug Info

Synonyms

NaMN; nicotinate mononucleotide; 321-02-8; nicotinic acid mononucleotide; Nicotinic acid mono nucleotide; AC1NRCHP; NCN; DB02382; 3-carboxy-1-[5-O-(hydroxyphosphinato)-beta-D-ribofuranosyl]pyridinium; [(2R,3S,4R,5R)-5-(3-carboxypyridin-1-ium-1-yl)-3,4-dihydroxyoxolan-2-yl]methyl hydrogen phosphate; [(2R,3S,4R,5R)-5-(3-carboxypyridin-1-ium-1-yl)-3,4-dihydroxy-tetrahydrofuran-2-yl]methyl hydrogen phosphate; ((2R,3S,4R,5R)-5-(3-carboxypyridinium-1-yl)-3,4-dihydroxytetrahydrofuran-2-yl)methyl hydrogen phosphate

Indication

Disease Entry	ICD 11	Status	REF
Discovery agent	N.A.	Investigative	[1]

Cross-matching ID

PubChem CID: 5288991
CAS Number: CAS 321-02-8
TTD Drug ID: DM1EZ3N
INTEDE Drug ID: DR2116

Molecule-Related Drug Atlas

Molecule Type:

DTT

DME

Drug Status:

Investigative Drug(s)

Download the Complete Related Drug List

Drug(s) Targeting Mycobacterium Nicotinate-nucleotide pyrophosphorylase (MycB nadC)

Drug Name	Drug ID	Indication	ICD 11	Highest Status	REF
5-Phosphoribosyl-1-(Beta-Methylene) Pyrophosphate	DMGK05W	Discovery agent	N.A.	Investigative	[1]
Quinolinic Acid	DM8YGOI	Discovery agent	N.A.	Investigative	[1]
Phthalic Acid	DMF9T64	Discovery agent	N.A.	Investigative	[1]
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Molecular Interaction Atlas of This Drug

Molecular Interaction Atlas

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Drug Therapeutic Target (DTT)

DTT Name	DTT ID	UniProt ID	MOA	REF
Mycobacterium Nicotinate-nucleotide pyrophosphorylase (MycB nadC)	TTH29K0	NADC_MYCTU	Inhibitor	[1]

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Drug-Metabolizing Enzyme (DME)

DME Name	DME ID	UniProt ID	MOA	REF
Nicotinate-nucleotide adenylyltransferase 3 (NMNAT3)	DERBKPU	NMNA3_HUMAN	Substrate	[2]
Nicotinate-nucleotide adenylyltransferase 2 (NMNAT2)	DE2HB58	NMNA2_HUMAN	Substrate	[3]
Nicotinate-nucleotide adenylyltransferase 1 (NMNAT1)	DE4D159	NMNA1_HUMAN	Substrate	[3]

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References

1	How many drug targets are there Nat Rev Drug Discov. 2006 Dec;5(12):993-6.
2	The NMN/NaMN adenylyltransferase (NMNAT) protein family. Front Biosci (Landmark Ed). 2009 Jan 1;14:410-31.
3	Initial-rate kinetics of human NMN-adenylyltransferases: substrate and metal ion specificity, inhibition by products and multisubstrate analogues, and isozyme contributions to NAD+ biosynthesis. Biochemistry. 2007 Apr 24;46(16):4912-22.