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Information on EC 1.1.1.333 - decaprenylphospho-beta-D-erythro-pentofuranosid-2-ulose 2-reductase
for references in articles please use BRENDA:EC1.1.1.333
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EC Tree 1 Oxidoreductases
1.1 Acting on the CH-OH group of donors
1.1.1 With NAD+ or NADP+ as acceptor
1.1.1.333 decaprenylphospho-beta-D-erythro-pentofuranosid-2-ulose 2-reductase
IUBMB Comments
The reaction is catalysed in the reverse direction. The enzyme, isolated from the bacterium Mycobacterium smegmatis, is involved, along with EC 1.1.98.3, decaprenylphospho-β-D-ribofuranose 2-oxidase, in the epimerization of trans,octacis-decaprenylphospho-β-D-ribofuranose to trans,octacis-decaprenylphospho-β-D-arabinoofuranose, the arabinosyl donor for the biosynthesis of mycobacterial cell wall arabinan polymers.
The expected taxonomic range for this enzyme is: Mycobacteriaceae
- 1.1.1.333
- tuberculosis
- mycobacterium
-
benzothiazinones
- arabinogalactan
- arabinans
- smegmatis
- d-arabinose
-
mycolate
-
dinitrobenzamide
-
corynebacterium
- glutamicum
-
arabinosylated
-
multidrug-resistant
- corynebacterineae
-
heteromeric
-
xdr-tb
-
antituberculosis
-
antitubercular
-
drug-resistant
- analysis
Reaction Schemes
showSynonyms
dpre2, rv3791, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
decaprenylphospho-beta-D-ribofuranose 2'-epimerase
-
-
-
-
DprE2
Rv3791
DprE2
-
-
-
-
Rv3791
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
trans,octacis-decaprenylphospho-beta-D-arabinofuranose + NAD+ = trans,octacis-decaprenylphospho-beta-D-erythro-pentofuranosid-2-ulose + NADH + H+
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-
-
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PATHWAY SOURCE
PATHWAYS
MetaCyc
mycolyl-arabinogalactan-peptidoglycan complex biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
trans,octacis-decaprenylphospho-beta-D-arabinofuranose:NAD+ 2-oxidoreductase
The reaction is catalysed in the reverse direction. The enzyme, isolated from the bacterium Mycobacterium smegmatis, is involved, along with EC 1.1.98.3, decaprenylphospho-beta-D-ribofuranose 2-oxidase, in the epimerization of trans,octacis-decaprenylphospho-beta-D-ribofuranose to trans,octacis-decaprenylphospho-beta-D-arabinoofuranose, the arabinosyl donor for the biosynthesis of mycobacterial cell wall arabinan polymers.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
trans,octacis-decaprenylphospho-beta-D-erythro-pentafuranosid-2-ulose + NADH
trans,octacis-decaprenylphospho-beta-D-arabinofuranose + NAD+
Substrates: reaction catalyzed by decaprenylphospho-beta-D-erythro-pentofuranosid-2-ulose 2-reductase DprE2
Products: -
Products: -
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additional information
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Substrates: decaprenylphospho-beta-D-ribofuranose 2-oxidase DprE1 and decaprenylphospho-beta-D-erythro-pentofuranosid-2-ulose 2-reductase DprE2 together catalyze the epimerization of decaprenylphosphoryl-beta-D-ribofuranose to decaprenylphosphoryl-beta-D-arabinofuranose. Neither protein individually is sufficient to support the activity
Products: -
Products: -
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additional information
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Substrates: decaprenylphospho-beta-D-ribofuranose 2-oxidase DprE1 and decaprenylphospho-beta-D-erythro-pentofuranosid-2-ulose 2-reductase DprE2 together catalyze the epimerization of decaprenylphosphoryl-beta-D-ribofuranose to decaprenylphosphoryl-beta-D-arabinofuranose. Neither protein individually is sufficient to support the activity
Products: -
Products: -
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additional information
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Substrates: decaprenylphosphoryl-beta-D-ribofuranose 2'-epimerase is constituted of decaprenylphospho-beta-D-ribofuranose 2-oxidase DprE1 and decaprenylphospho-beta-D-erythro-pentofuranosid-2-ulose 2-reductase DprE2 that together catalyze the epimerization of decaprenylphosphoryl-beta-D-ribofuranose to decaprenylphosphoryl-beta-D-arabinofuranose
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
N-(2-(4-methoxyphenoxy)ethyl)-3,5-dinitrobenzamide
more than a ten-fold decrease in the number of colony-forming units is observed with both human and mouse primary cells at a N-(2-(4-methoxyphenoxy)ethyl)-3,5-dinitrobenzamide concentrations above 5 microM, compound is also highly active against multidrug-resistant and extensively drug-resistant clinical isolates. N-(2-(4-methoxyphenoxy)ethyl)-3,5-dinitrobenzamide shows a clear-cut effect on the synthesis of the arabinan domains of arabinogalactan and lipoarabinomannan, and inhibition of decaprenyl-phospho-arabinose formation in the treated extracts concurrent with the accumulation of decaprenylphospho-ribose. Target of the inhibitors is probably the heteromeric decaprenylphospho-ribose 29 epimerase encoded by the dprE1/dprE2 genes
N-(2-(benzyloxy)ethyl)-3,5-dinitrobenzamide
more than a ten-fold decrease in the number of colony-forming units is observed with both human and mouse primary cells at a N-(2-(benzyloxy)ethyl)-3,5-dinitrobenzamide concentrations above 5 microM, compound is also highly active against multidrug-resistant and extensively drug-resistant clinical isolates. N-(2-(benzyloxy)ethyl)-3,5-dinitrobenzamide shows a clear-cut effect on the synthesis of the arabinan domains of arabinogalactan and lipoarabinomannan, and inhibition of decaprenyl-phospho-arabinose formation in the treated extracts concurrent with the accumulation of decaprenylphospho-ribose. Target of the inhibitors is probably the heteromeric decaprenylphospho-ribose 29 epimerase encoded by the dprE1/dprE2 genes
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Tuberculosis
Pseudomonas aeruginosa D-Arabinofuranose Biosynthetic Pathway and Its Role in Type IV Pilus Assembly.
Tuberculosis
Structure, dynamics, and interaction of Mycobacterium tuberculosis (Mtb) DprE1 and DprE2 examined by molecular modeling, simulation, and electrostatic studies.
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
decaprenylphosphoryl-beta-D-ribofuranose 2'-epimerase is constituted of DprE1 and DprE2 that together catalyze the epimerization of decaprenylphosphoryl-beta-D-ribofuranose to decaprenylphosphoryl-beta-D-arabinofuranose
physiological function
decaprenylphosphoryl-D-arabinofuranose is synthesized by the following sequence of events: 5-phosphoribose 1-diphosphate is transferred to a decaprenyl-phosphate molecule to form decaprenylphosphoryl-beta-D-5-phosphoribose. Decaprenylphosphoryl-beta-D-5-phosphoribose is dephosphorylated to form decaprenylphosphoryl-beta-D-ribose. The hydroxyl group at the 2 position of the ribose is oxidized and is likely to form decaprenylphosphoryl-2-keto-beta-D-erythro-pentofuranose. Decaprenylphosphoryl-2-keto-beta-D-erythro-pentofuranose is reduced to form decaprenylphosphoryl-beta-D-arabinofuranose. Thus, the epimerization of the ribosyl to an arabinosyl residue occurs at the lipid-linked level
physiological function
-
decaprenylphosphoryl-D-arabinofuranose is synthesized by the following sequence of events: 5-phosphoribose 1-diphosphate is transferred to a decaprenyl-phosphate molecule to form decaprenylphosphoryl-beta-D-5-phosphoribose. Decaprenylphosphoryl-beta-D-5-phosphoribose is dephosphorylated to form decaprenylphosphoryl-beta-D-ribose. The hydroxyl group at the 2 position of the ribose is oxidized and is likely to form decaprenylphosphoryl-2-keto-beta-D-erythro-pentofuranose. Decaprenylphosphoryl-2-keto-beta-D-erythro-pentofuranose is reduced to form decaprenylphosphoryl-beta-D-arabinofuranose. Thus, the epimerization of the ribosyl to an arabinosyl residue occurs at the lipid-linked level
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). DPRE2_MYCS2
Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155)
254
0
27137
Swiss-Prot
-
DPRE2_MYCBO
Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97)
254
0
27469
Swiss-Prot
-
DPRE2_MYCTU
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
254
0
27469
Swiss-Prot
-
DPRE2_MYCTO
Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
254
0
27469
Swiss-Prot
other Location (Reliability: 3)
A0A0H3MJ74_MYCBP
Mycobacterium bovis (strain BCG / Pasteur 1173P2)
254
0
27469
TrEMBL
-
A0A100XJD3_MYCTH
254
0
27469
TrEMBL
-
A0A1A3NB41_MYCAS
254
0
27572
TrEMBL
Secretory Pathway (Reliability: 3)
A0A1B4Y9Q6_MYCUL
254
0
27309
TrEMBL
Secretory Pathway (Reliability: 2)
A0A1V3X2Q1_MYCKA
253
0
27384
TrEMBL
other Location (Reliability: 2)
A0A2G8B1C7_9MYCO
254
0
27314
TrEMBL
other Location (Reliability: 2)
A0A2Z5YPI1_MYCMR
254
0
27339
TrEMBL
Secretory Pathway (Reliability: 1)
A0A679LM26_MYCBO
Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97)
254
0
27469
TrEMBL
-
A0A7I7MTJ8_9MYCO
254
0
27385
TrEMBL
Mitochondrion (Reliability: 3)
A0A829C615_9MYCO
254
0
27469
TrEMBL
-
A0A9P2H4I8_MYCTX
254
0
27469
TrEMBL
-
A0AB72XR60_MYCCP
Mycobacterium canettii (strain CIPT 140010059)
254
0
27470
TrEMBL
-
A0AB74LKI0_MYCBI
254
0
27469
TrEMBL
other Location (Reliability: 1)
A0ABD6P5H3_9MYCO
254
0
27506
TrEMBL
other Location (Reliability: 3)
A0PWY3_MYCUA
Mycobacterium ulcerans (strain Agy99)
254
0
27339
TrEMBL
Mitochondrion (Reliability: 2)
A5U9C0_MYCTA
Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra)
254
0
27469
TrEMBL
-
B2HMI8_MYCMM
Mycobacterium marinum (strain ATCC BAA-535 / M)
254
0
27339
TrEMBL
-
G7CE97_MYCT3
Mycolicibacterium thermoresistibile (strain ATCC 19527 / DSM 44167 / CIP 105390 / JCM 6362 / NCTC 10409 / 316)
254
0
27469
TrEMBL
-
L7VB27_MYCL1
Mycobacterium liflandii (strain 128FXT)
254
0
27325
TrEMBL
-
R4MBM8_MYCTX
254
0
27384
TrEMBL
Secretory Pathway (Reliability: 5)
R4MC07_MYCTX
254
0
27469
TrEMBL
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
analysis
developed of an assay method based on the visualization of mycobacterium replication within host cells and application for the search of compounds that are able to chase the pathogen from its hideout
analysis
-
developed of an assay method based on the visualization of mycobacterium replication within host cells and application for the search of compounds that are able to chase the pathogen from its hideout
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Trefzer, C.; Skovierova, H.; Buroni, S.; Bobovska, A.; Nenci, S.; Molteni, E.; Pojer, F.; Pasca, M.; Makarov, V.; Cole, S.; Riccardi, G.; Mikusova, K.; Johnsson, K.
Benzothiazinones are suicide inhibitors of mycobacterial decaprenylphosphoryl-beta-D-ribofuranose 2'-oxidase DprE1
J. Am. Chem. Soc.
134
912-915
2012
Mycolicibacterium smegmatis (A0R610)
brenda
Mikusova, K.; Huang, H.; Yagi, T.; Holsters, M.; Vereecke, D.; DHaeze, W.; Scherman, M.S.; Brennan, P.J.; McNeil, M.R.; Crick, D.C.
Decaprenylphosphoryl arabinofuranose, the donor of the D-arabinofuranosyl residues of mycobacterial arabinan, is formed via a two-step epimerization of decaprenylphosphoryl ribose
J. Bacteriol.
187
8020-8025
2005
Mycobacterium tuberculosis (P9WGS9), Mycobacterium tuberculosis H37Rv (P9WGS9)
brenda
Christophe, T.; Jackson, M.; Hee, K.; Fenistein, D.; Contreras-Dominguez, M.; Kim, J.; Genovesio, A.; Carralot, J.; Ewann, F.; Kim, E.; Lee, S.; Kang, S.; Seo, M.; Eun, J.; Skovierova, H.; Pham, H.; Riccardi, G.; Youn, N.; Marsollier, L.; Kempf, M.; Jol
High content screening identifies decaprenyl-phosphoribose 2beta epimerase as a target for intracellular antimycobacterial inhibitors
PLoS Pathog.
5
e1000645
2009
Mycobacterium tuberculosis (P9WGS9), Mycobacterium tuberculosis H37Rv (P9WGS9)
-
brenda
EXTERNAL LINKS (specific for EC-Number 1.1.1.333)
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