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Information on EC 1.1.1.405 - ribitol-5-phosphate 2-dehydrogenase (NADP+)
for references in articles please use BRENDA:EC1.1.1.405
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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
1.1.1.405 ribitol-5-phosphate 2-dehydrogenase (NADP+)
IUBMB Comments
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.
The enzyme appears in viruses and cellular organisms
showSynonyms
ACS1, Bcs1, bifunctional ribulose 5-phosphate reductase/CDP-ribitol pyrophosphorylase, ribulose-5-P reductase, ribulose-5-phosphate reductase, TarIJ, TarJ, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ACS1
Bcs1
bifunctional ribulose 5-phosphate reductase/CDP-ribitol pyrophosphorylase
ribulose-5-P reductase
-
-
-
-
ribulose-5-phosphate reductase
-
-
-
-
TarJ
ACS1
-
-
-
-
Bcs1
-
-
-
-
bifunctional ribulose 5-phosphate reductase/CDP-ribitol pyrophosphorylase
-
bifunctional ribulose 5-phosphate reductase/CDP-ribitol pyrophosphorylase
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TarJ
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
D-ribitol 5-phosphate + NADP+ = D-ribulose 5-phosphate + NADPH + H+
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
MetaCyc
poly(ribitol phosphate) wall teichoic acid biosynthesis I (B. subtilis), poly(ribitol phosphate) wall teichoic acid biosynthesis II (S. aureus), type IV lipoteichoic acid biosynthesis (S. pneumoniae)
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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.
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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
D-arabinose 5-phosphate + NADPH + H+
? + NADP+
Substrates: -
Products: -
Products: -
?
D-erythrose 4-phosphate + NADPH + H+
? + NADP+
Substrates: -
Products: -
Products: -
?
D-ribitol 5-phosphate + NADP+
D-ribulose 5-phosphate + NADPH + H+
Substrates: -
Products: -
Products: -
r
D-ribose 5-phosphate + NADPH + H+
? + NADP+
Substrates: -
Products: -
Products: -
?
D-ribulose + NADPH + H+
D-ribitol + NADP+
Substrates: -
Products: -
Products: -
?
D-xylulose 5-phosphate + NADH + H+
? + NAD+
Substrates: -
Products: -
Products: -
?
D-ribulose 5-phosphate + NADPH + H+
D-ribitol 5-phosphate + NADP+
-
Substrates: the data suggest that NADPH binds first and ribulose 5-phosphate binds second. Bifunction enzyme catalyzing the reactions of EC 1.1.1.137 and EC 2.7.7.40, ordered bi-bi mechanism
Products: -
Products: -
?
D-ribulose 5-phosphate + NADPH + H+
D-ribitol 5-phosphate + NADP+
Substrates: -
Products: -
Products: -
?
D-ribulose 5-phosphate + NADPH + H+
D-ribitol 5-phosphate + NADP+
Substrates: -
Products: -
Products: -
r
D-ribulose 5-phosphate + NADPH + H+
D-ribitol 5-phosphate + NADP+
-
Substrates: 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. Release and free diffusion of the intermediate ribitol 5-phosphate without channelling between active sites, ordered bi-bi mechanism
Products: -
Products: -
?
D-ribulose 5-phosphate + NADPH + H+
D-ribitol 5-phosphate + NADP+
Substrates: -
Products: -
Products: -
?
additional information
?
-
Substrates: the synthase first catalyzes the reduction of D-ribulose 5-phosphate followed by cytidylyl transfer to D-ribitol 5-phosphate, with a 650fold kinetic preference for cytidylyl transfer to D-ribitol 5-phosphate over D-ribulose 5-phosphate
Products: -
Products: -
?
additional information
?
-
Substrates: the dehydrogenase activity of Acs1 is specific for ribulose 5-phosphate and NADPH in one direction and for ribitol 5-phosphate and NADP+ in the other direction. The activity is about twofold higher with ribulose 5-phosphate as the substrate than with ribose 5-phosphate. No substrate: xylulose 5-phosphate
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
NADH is not consumed in the presence of Spr1148-His and ribulose 5-phosphate
-
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
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
additional information
not inhibitory: 0.5 mM ribitol 5-phosphate or 0.5 mM NADP+
-
2-[5-Amino-2-(4-fluoro-phenyl)-6-oxo-6H-pyrimidin-1-yl]-N-(1-benzyl-2-oxo-2-thiazol-2-yl-ethyl)-acetamide
-
-
2-[5-Amino-2-(4-fluoro-phenyl)-6-oxo-6H-pyrimidin-1-yl]-N-(1-benzyl-2-oxo-2-thiazol-2-yl-ethyl)-acetamide
-
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
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
LITERATURE
IMAGE
0.038
(2R,3R)-2,3-dihydroxy-4-oxobutyl-phosphate
wild-type, pH 7.2, 25°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.5
(2R,3R)-2,3-dihydroxy-4-oxobutyl-phosphate
wild-type, pH 7.2, 25°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0013
(2R,3R)-2,3-dihydroxy-4-oxobutyl-phosphate
wild-type, pH 7.2, 25°C
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
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
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
-
Ki(intercept) and Ki(slope)-values
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
-
Ki(intercept) and Ki(slope)-values
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2.87
substrate D-ribulose 5-phosphate, presence of CTP, pH 8.5, 30°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
additionally catalyzes reaction of ribitol-5-phosphate cytidylyltransferase, EC 2.7.7.40
UniProt
brenda
additionally catalyzes the reaction of ribitol-5-phosphate cytidylyltransferase, EC 2.7.7.40
UniProt
brenda
Highest Expressing Human Cell Lines
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
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
Show AA Sequence and Transmembrane Helices (466 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
129000
-
calculation from gel filtration and sedimentation velocity data
26000
-
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
-
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
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
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
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
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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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
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
overexpression of TarI and TarJ individually from their respective genes using the T7 expression system
-
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
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Follens, A.; Veiga-da-Cunha, M.; Merckx, R.; van Schaftingen, E.; van Eldere, J.
acs1 of Haemophilus influenzae type a capsulation locus region II encodes a bifunctional ribulose 5-phosphate reductase- CDP-ribitol pyrophosphorylase
J. Bacteriol.
181
2001-2007
1999
Haemophilus influenzae (Q48154)
brenda
Zolli, M.; Kobric, D.J.; Brown, E.D.
Reduction precedes cytidylyl transfer without substrate channeling in distinct active sites of the bifunctional CDP-ribitol synthase from Haemophilus influenzae
Biochemistry
40
5041-5048
2001
Haemophilus influenzae (Q48230)
brenda
Pereira, M.P.; Brown, E.D.
Bifunctional catalysis by CDP-ribitol synthase: convergent recruitment of the reductase and cytidylyltransferase activities in Haemophilus influenzae and Staphylococcus aureus
Biochemistry
43
11802-11812
2004
Haemophilus influenzae, Staphylococcus aureus
brenda
Baur, S.; Marles-Wright, J.; Buckenmaier, S.; Lewis, R.J.; Vollmer, W.
Synthesis of CDP-activated ribitol for teichoic acid precursors in Streptococcus pneumoniae
J. Bacteriol.
191
1200-1210
2009
Streptococcus pneumoniae (Q8DPI3)
brenda
EXTERNAL LINKS (specific for EC-Number 1.1.1.405)
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