Decaprenylphospho-beta-D-ribofuranose 2-oxidase

Search
PMC	articles
PubMed	articles
NCBI	proteins

Decaprenylphospho-beta-D-ribofuranose 2-oxidase
Decaprenylphospho-beta-D-ribofuranose 2-oxidase
Identifiers
EC no.	1.1.98.3
Databases
BRENDA	enzyme data
ExPASy	NiceZyme view
KEGG	enzyme entry
MetaCyc	metabolic pathway
Rhea	reactions
PDB structures	RCSB PDB PDBe PDBsum
PMC
Search
PMC	articles
PubMed	articles
NCBI	proteins

Decaprenylphospho-beta-D-ribofuranose 2-oxidase (EC 1.1.98.3, decaprenylphosphoryl-beta-D-ribofuranose 2'-epimerase, Rv3790, DprE1) is an enzyme with systematic name trans,octacis-decaprenylphospho-beta-D-ribofuranose:FAD 2-oxidoreductase.^[1]^[2] This enzyme catalyses the following chemical reaction

trans,octacis-decaprenylphospho-beta-D-ribofuranose + FAD

\rightleftharpoons

trans,octacis-decaprenylphospho-beta-D-erythro-pentofuranosid-2-ulose + FADH₂

This enzyme from the bacterium Mycobacterium smegmatis participates in epimerization of trans,octacis-decaprenylphospho-beta-D-ribofuranose to trans,octacis-decaprenylphospho-beta-D-arabinoofuranose.

Macozinone and quabodepistat are two investigational drugs that target DprE1.^[3]

References

↑ Ribeiro AL, Degiacomi G, Ewann F, Buroni S, Incandela ML, Chiarelli LR, et al. (2011). "Analogous mechanisms of resistance to benzothiazinones and dinitrobenzamides in Mycobacterium smegmatis". PLOS ONE. 6 (11) e26675. Bibcode:2011PLoSO...626675D. doi:10.1371/journal.pone.0026675. PMC 3206020. PMID 22069462.
↑ Trefzer C, Škovierová H, Buroni S, Bobovská A, Nenci S, Molteni E, et al. (January 2012). "Benzothiazinones are suicide inhibitors of mycobacterial decaprenylphosphoryl-β-D-ribofuranose 2'-oxidase DprE1". Journal of the American Chemical Society. 134 (2): 912–915. doi:10.1021/ja211042r. PMID 22188377.
↑ Jaorawala Z, Samaiya PK, Parida KK, Kalia NP, Tanwar O (January 2026). "Preclinical and Clinical Efficacy of Promising DprE1 Inhibitors: A Critical Review". ChemistrySelect. 11 (1). doi:10.1002/slct.202505382.

External links

Decaprenylphospho-beta-D-ribofuranose+2-oxidase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)

[1] Ribeiro AL, Degiacomi G, Ewann F, Buroni S, Incandela ML, Chiarelli LR, et al. (2011). "Analogous mechanisms of resistance to benzothiazinones and dinitrobenzamides in Mycobacterium smegmatis". PLOS ONE. 6 (11) e26675. Bibcode:2011PLoSO...626675D. doi:10.1371/journal.pone.0026675. PMC 3206020. PMID 22069462.

[2] Trefzer C, Škovierová H, Buroni S, Bobovská A, Nenci S, Molteni E, et al. (January 2012). "Benzothiazinones are suicide inhibitors of mycobacterial decaprenylphosphoryl-β-D-ribofuranose 2'-oxidase DprE1". Journal of the American Chemical Society. 134 (2): 912–915. doi:10.1021/ja211042r. PMID 22188377.

[3] Jaorawala Z, Samaiya PK, Parida KK, Kalia NP, Tanwar O (January 2026). "Preclinical and Clinical Efficacy of Promising DprE1 Inhibitors: A Critical Review". ChemistrySelect. 11 (1). doi:10.1002/slct.202505382.

[1]

[2]

[3]

Oxidoreductases: alcohol oxidoreductases (EC 1.1)
1.1.1: NAD/NADP acceptor	3-hydroxyacyl-CoA dehydrogenase 3-hydroxybutyryl-CoA dehydrogenase 6-Phosphogluconate dehydrogenase Alcohol dehydrogenase Aldo-keto reductase 1A1 1B1 1B10 1C1 1C3 1C4 7A2 Aldose reductase Beta-Ketoacyl ACP reductase Carbohydrate dehydrogenases Carnitine dehydrogenase D-malate dehydrogenase (decarboxylating) DXP reductoisomerase Glucose-6-phosphate dehydrogenase Glycerol-3-phosphate dehydrogenase HMG-CoA reductase IMP dehydrogenase Isocitrate dehydrogenase Lactate dehydrogenase L-threonine dehydrogenase L-xylulose reductase Malate dehydrogenase Malate dehydrogenase (decarboxylating) Malate dehydrogenase (NADP+) Malate dehydrogenase (oxaloacetate-decarboxylating) Malate dehydrogenase (oxaloacetate-decarboxylating) (NADP+) Sorbitol dehydrogenase Hydroxysteroid dehydrogenase: 3β 3β-HSD NSDHL 11β 11β-HSD1 11β-HSD2 17β
1.1.2: cytochrome acceptor	D-lactate dehydrogenase (cytochrome) D-lactate dehydrogenase (cytochrome c-553) Mannitol dehydrogenase (cytochrome)
1.1.3: oxygen acceptor	Alcohol oxidase Glucose oxidase L-gulonolactone oxidase L-lactate oxidase Xanthine oxidase
1.1.4: disulfide as acceptor	Vitamin K epoxide reductase Vitamin-K-epoxide reductase (warfarin-insensitive)
1.1.5: quinone/similar acceptor	Malate dehydrogenase (quinone) Quinoprotein glucose dehydrogenase
1.1.99: other acceptors	Choline dehydrogenase L2HGDH

Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)