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

D-glucuronate Drug Info

AEMOLEFTQBMNLQ-AQKNRBDQSA-N; D-GlcA; D-Glucopyranuronate; D-Glucopyranuronic Acid; D-Glucuronate; D-Glucuronic Acid; Glucopyranuronate; Glucopyranuronic Acid; Glucosiduronic acid; Glucuronate; Glucuronic Acid; Maybridge1_004154; O_FULL_00000000001000_GS_791; SR-01000639202-1; AC1L3SRL; AC1Q5R59; AKOS015955920; C00191; CCG-49770; CHEBI:47952; CHEMBL496672; DTXSID50894097; EINECS 208-429-7; Epitope ID:115136; GlcA; HMS553E20; SCHEMBL30411; WURCS=2.0/1,1,0/[a2122A-1x_1-5]/1/; bmse000140

Cross-matching ID

PubChem CID

94715

ChEBI ID

CHEBI:47952

CAS Number

CAS 528-16-5

TTD Drug ID

DM1YBTC

INTEDE Drug ID

DR1996

General Information of Drug (ID: DM1YBTC)

Molecule-Related Drug Atlas

Molecule Type:

DME

Drug Status:

Approved Drug(s)

Investigative Drug(s)

Download the Complete Related Drug List

Drug(s) Metabolized By Aldo-keto reductase 1A1 (AKR1A1)

Drug Name	Drug ID	Indication	ICD 11	Highest Status	REF
Doxorubicin	DMVP5YE	Acute myelogenous leukaemia	2A41	Approved	[2]
Ethanol	DMDRQZU	Chronic pain	MG30	Approved	[3]
NADH	DM5NM6E	Parkinson disease	8A00.0	Approved	[4]
2,3-dihydroxypropanal	DMOWNB4	Discovery agent	N.A.	Investigative	[1]
Nitrobenzaldehyde	DM4UHB5	N. A.	N. A.	Investigative	[1]
BRN-0471734	DMZMWVX	N. A.	N. A.	Investigative	[1]
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Molecular Interaction Atlas of This Drug

Molecular Interaction Atlas

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Drug-Metabolizing Enzyme (DME)

DME Name	DME ID	UniProt ID	MOA	REF
Aldo-keto reductase 1A1 (AKR1A1)^{Main DME}	DED2FW3	AK1A1_HUMAN	Substrate	[1]

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References

1	The C-terminal loop of aldehyde reductase determines the substrate and inhibitor specificity. Biochemistry. 1996 Nov 12;35(45):14276-80.
2	Carbonyl reductase 1 is a predominant doxorubicin reductase in the human liver. Drug Metab Dispos. 2008 Oct;36(10):2113-20.
3	Functional assessment of human alcohol dehydrogenase family in ethanol metabolism: significance of first-pass metabolism. Alcohol Clin Exp Res. 2006 Jul;30(7):1132-42.
4	Conformational changes and catalysis by alcohol dehydrogenase. Arch Biochem Biophys. 2010 Jan 1;493(1):3-12.