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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Pentose and glucuronate interconversions
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Metabolic pathways
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SYSTEMATIC NAME
IUBMB Comments
D-ribitol-5-phosphate:NADP+ 2-oxidoreductase
Requires Zn2+. The enzyme, characterized in bacteria, is specific for NADP. It is part of the synthesis pathway of CDP-ribitol. In Haemophilus influenzae it is part of a multifunctional enzyme also catalysing EC 2.7.7.40, D-ribitol-5-phosphate cytidylyltransferase. cf. EC 1.1.1.137, ribitol-5-phosphate 2-dehydrogenase.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
Acs1 encodes a bifunctional enzyme that converts ribulose 5-phosphate into ribitol 5-phosphate and further into CDP-ribitol, the activated precursor form for incorporation of ribitol 5-phosphate into the Haemophilus influenzae type a capsular polysaccharide
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
D-arabinose 5-phosphate + NADPH + H+
? + NADP+
show the reaction diagram
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?
D-erythrose 5-phosphate + NADPH + H+
? + NADP+
show the reaction diagram
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?
D-ribitol 5-phosphate + NADP+
D-ribulose 5-phosphate + NADPH + H+
show the reaction diagram
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r
D-ribose 5-phosphate + NADPH + H+
? + NADP+
show the reaction diagram
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?
D-ribulose + NADPH + H+
D-ribitol + NADP+
show the reaction diagram
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?
D-ribulose 5-phosphate + NADPH + H+
D-ribitol 5-phosphate + NADP+
show the reaction diagram
D-xylulose 5-phosphate + NADH + H+
? + NAD+
show the reaction diagram
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?
additional information
?
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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+
additional information
not inhibitory: 0.5 mM ribitol 5-phosphate or 0.5 mM NADP+
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
CTP
marked stimulation, presence of 50 mM CTP decreases the Km value for ribulose 5-phosphate from 400 to 50 microM
additional information
not stimulated by UTP, ATP, GTP, ADP, or dCTP
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3
D-arabinose 5-phosphate
wild-type, pH 7.2, 25°C
0.038
D-erythrose 5-phosphate
wild-type, pH 7.2, 25°C
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0.05 - 0.4
D-ribitol 5-phosphate
2.2
D-ribose 5-phosphate
wild-type, pH 7.2, 25°C
1.1
D-ribulose
wild-type, pH 7.2, 25°C
0.061 - 0.27
D-ribulose 5-phosphate
3.5
D-xylulose 5-phosphate
wild-type, pH 7.2, 25°C
0.6
NADH
wild-type, pH 7.2, 25°C
0.00674 - 0.044
NADPH
0.0285 - 0.106
ribulose 5-phosphate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.3
D-arabinose 5-phosphate
wild-type, pH 7.2, 25°C
0.5
D-erythrose 5-phosphate
wild-type, pH 7.2, 25°C
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4.1
D-ribose 5-phosphate
wild-type, pH 7.2, 25°C
3.6
D-ribulose
wild-type, pH 7.2, 25°C
0.32 - 22
D-ribulose 5-phosphate
3.6
D-xylulose 5-phosphate
wild-type, pH 7.2, 25°C
0.03 - 22
NADPH
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00008
D-arabinose 5-phosphate
wild-type, pH 7.2, 25°C
0.0013
D-erythrose 5-phosphate
wild-type, pH 7.2, 25°C
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0.0002
D-ribose 5-phosphate
wild-type, pH 7.2, 25°C
0.0003
D-ribulose
wild-type, pH 7.2, 25°C
0.0002 - 0.029
D-ribulose 5-phosphate
0.0001
D-xylulose 5-phosphate
wild-type, pH 7.2, 25°C
0.0008 - 0.05
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
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.73
substrate D-ribulose 5-phosphate, pH 8.5, 30°C
2.87
substrate D-ribulose 5-phosphate, presence of CTP, pH 8.5, 30°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
53000
x * 53000, 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
dimer
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2 * 53190, calculation from amino acid composition
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
23°C, at 0.3 mg/ml in the presence of 20 mM HEPES, pH 7.1, 1 mM DTT, and 0.5 mg of BSA/ml, ribitol 5-phosphate dehydrogenase activity decreases to about 50% of the initial activity after 2 h
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in ERscherichia coli
expression in Escherichia coli
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
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K386A
mutant impaired for reduction of D-ribulose. Equimolar mixtures of mutants K386A and R18A are efficient for bifunctional catalysis
R18A
mutant impaired for cytidylyl transfer. Equimolar mixtures of mutants K386A and R18A are efficient for bifunctional catalysis
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