Information on EC 1.1.1.405 - ribitol-5-phosphate 2-dehydrogenase (NADP+)

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.1.1.405
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RECOMMENDED NAME
GeneOntology No.
ribitol-5-phosphate 2-dehydrogenase (NADP+)
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
D-ribitol 5-phosphate + NADP+ = D-ribulose 5-phosphate + NADPH + H+
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
poly(ribitol phosphate) wall teichoic acid biosynthesis I (B. subtilis)
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poly(ribitol phosphate) wall teichoic acid biosynthesis II (S. aureus)
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type IV lipoteichoic acid biosynthesis (S. pneumoniae)
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SYSTEMATIC NAME
IUBMB Comments
D-ribitol-5-phosphate:NADP+ 2-oxidoreductase
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
D-ribulose 5-phosphate + NADPH + H+
D-ribitol 5-phosphate + NADP+
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
NADH is not consumed in the presence of Spr1148-His and ribulose 5-phosphate
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-[5-Amino-2-(4-fluoro-phenyl)-6-oxo-6H-pyrimidin-1-yl]-N-(1-benzyl-2-oxo-2-thiazol-2-yl-ethyl)-acetamide
D-ribitol 5-phosphate
NADP+
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.061
D-ribulose 5-phosphate
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0.00674 - 0.00706
NADPH
0.0285 - 0.106
ribulose 5-phosphate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.5
D-ribulose 5-phosphate
Streptococcus pneumoniae
Q8DPI3
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0.03 - 7.41
NADPH
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
2-[5-Amino-2-(4-fluoro-phenyl)-6-oxo-6H-pyrimidin-1-yl]-N-(1-benzyl-2-oxo-2-thiazol-2-yl-ethyl)-acetamide
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
26000
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2 * 26000 + 2 * 41000, tarI encodes an orthologue of the cytidylyltransferase domain of Bcs1 from Haemophilus influenzae and tarJ encodes an analogue of the reductase domain of Bcs1, TarI and TyrJ form a functional CDP-ribitol synthase complex, SDS-PAGE
41000
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2 * 26000 + 2 * 41000, tarI encodes an orthologue of the cytidylyltransferase domain of Bcs1 from Haemophilus influenzae and tarJ encodes an analogue of the reductase domain of Bcs1, TarI and TyrJ form a functional CDP-ribitol synthase complex, SDS-PAGE
53190
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2 * 53190, calculation from amino acid composition
106400
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amino acid composition
129000
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calculation from gel filtration and sedimentation velocity data
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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2 * 26000 + 2 * 41000, tarI encodes an orthologue of the cytidylyltransferase domain of Bcs1 from Haemophilus influenzae and tarJ encodes an analogue of the reductase domain of Bcs1, TarI and TyrJ form a functional CDP-ribitol synthase complex, SDS-PAGE
dimer
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2 * 53190, calculation from amino acid composition
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
overexpression of TarI and TarJ individually from their respective genes using the T7 expression system
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spr1148 gene amplified, inserted into plasmid pJFK118EH and transformed into competent cells of Escherichia coli DH5alpha. Plasmid pJFK118EH1148 isolated and insert with the spr1148 gene cut off by restriction enzymes NdeI and SacI. Fragment ligated into the overexpression plasmid pET28a(+) to generate plasmid pET1148. The plasmid transformed into Escherichia coli BL21(DE3) for overexpression of spr1148