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Information on EC 2.7.7.40 - D-ribitol-5-phosphate cytidylyltransferase for references in articles please use BRENDA:EC2.7.7.40
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EC Tree
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
Bcs1, CDP-ribitol (ribose) pyrophosphorylase, CDP-ribitol pyrophosphorylase, CDP-ribitol synthase, CDPribitol pyrophosphorylase, cytidine diphosphate ribitol pyrophosphorylase, Cytidine diphosphoribitol pyrophosphorylase, cytidylyltransferase, cytidylyltransferase, ribitol 5-phosphate, IspD,
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CDP-ribitol (ribose) pyrophosphorylase
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CDP-ribitol pyrophosphorylase
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CDPribitol pyrophosphorylase
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cytidine diphosphate ribitol pyrophosphorylase
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Cytidine diphosphoribitol pyrophosphorylase
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cytidylyltransferase, ribitol 5-phosphate
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ribitol 5-phosphate cytidylyltransferase
Bcs1
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Bcs1
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harbors both ribulose 5-phosphate reductase activity and ribitol 5-phosphate cytidylyltransferase activity
cytidylyltransferase
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ribitol 5-phosphate cytidylyltransferase
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ribitol 5-phosphate cytidylyltransferase
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CTP + D-ribitol 5-phosphate = diphosphate + CDP-ribitol
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nucleotidyl group transfer
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CTP:D-ribitol-5-phosphate cytidylyltransferase
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CTP + D-arabitol 5-phosphate
diphosphate + CDParabitol
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?
CTP + D-ribitol 5-phosphate
diphosphate + CDP-ribitol
CTP + D-ribitol 5-phosphate
diphosphate + CDPribitol
additional information
?
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CTP + D-ribitol 5-phosphate
diphosphate + CDP-ribitol
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?
CTP + D-ribitol 5-phosphate
diphosphate + CDP-ribitol
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ordered bi-bi mechanism
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?
CTP + D-ribitol 5-phosphate
diphosphate + CDP-ribitol
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?
CTP + D-ribitol 5-phosphate
diphosphate + CDP-ribitol
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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
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?
CTP + D-ribitol 5-phosphate
diphosphate + CDPribitol
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?
CTP + D-ribitol 5-phosphate
diphosphate + CDPribitol
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CTP + D-ribitol 5-phosphate
diphosphate + CDPribitol
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?
CTP + D-ribitol 5-phosphate
diphosphate + CDPribitol
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CTP + D-ribitol 5-phosphate
diphosphate + CDPribitol
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CTP + D-ribitol 5-phosphate
diphosphate + CDPribitol
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CTP + D-ribitol 5-phosphate
diphosphate + CDPribitol
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CTP + D-ribitol 5-phosphate
diphosphate + CDPribitol
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?
additional information
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enzyme functions possibly in synthesis of teichoic acids, repression of enzyme synthesis occurs at the onset of phosphate starvation
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additional information
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enzyme functions possibly in synthesis of teichoic acids, repression of enzyme synthesis occurs at the onset of phosphate starvation
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additional information
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enzyme has also ribitol 5-phosphate dehydrogenase activity
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additional information
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enzyme has also ribitol 5-phosphate dehydrogenase activity
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additional information
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no activity with erythritol 4-phosphate, sorbitol 6-phosphate and UTP
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additional information
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no activity with ATP, GTP, UTP, ADP or CDP
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additional information
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the enzyme is capable of generating CDP-ribitol or CDP-ribose using CTP and ribitol-5-phosphate or ribose-5-phosphate, respectively, but is not able to generate the sugar (alcohol) nucleotides with ribitol or ribose
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additional information
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the enzyme is capable of generating CDP-ribitol or CDP-ribose using CTP and ribitol-5-phosphate or ribose-5-phosphate, respectively, but is not able to generate the sugar (alcohol) nucleotides with ribitol or ribose
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CTP + D-ribitol 5-phosphate
diphosphate + CDP-ribitol
A4D126
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CTP + D-ribitol 5-phosphate
diphosphate + CDPribitol
additional information
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CTP + D-ribitol 5-phosphate
diphosphate + CDPribitol
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CTP + D-ribitol 5-phosphate
diphosphate + CDPribitol
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CTP + D-ribitol 5-phosphate
diphosphate + CDPribitol
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CTP + D-ribitol 5-phosphate
diphosphate + CDPribitol
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?
CTP + D-ribitol 5-phosphate
diphosphate + CDPribitol
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?
CTP + D-ribitol 5-phosphate
diphosphate + CDPribitol
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?
CTP + D-ribitol 5-phosphate
diphosphate + CDPribitol
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?
CTP + D-ribitol 5-phosphate
diphosphate + CDPribitol
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?
additional information
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enzyme functions possibly in synthesis of teichoic acids, repression of enzyme synthesis occurs at the onset of phosphate starvation
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additional information
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enzyme functions possibly in synthesis of teichoic acids, repression of enzyme synthesis occurs at the onset of phosphate starvation
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CDP-ribitol
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competitive versus CTP
CDP-ribitol
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competitive versus CTP
diphosphate
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0.0147 - 1.28
D-ribitol 5-phosphate
0.00851
CTP
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pH 7.2
0.092
CTP
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pH 7.2, 25°C, K386A mutant
0.39
CTP
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pH 7.2, 25°C, R18A mutant
0.0147
D-ribitol 5-phosphate
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pH 7.2
0.037
D-ribitol 5-phosphate
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pH 7.1, 30°C
0.12
D-ribitol 5-phosphate
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pH 7.2, 25°C, K386A mutant
0.13
D-ribitol 5-phosphate
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pH 7.2, 25°C
1
D-ribitol 5-phosphate
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pH 7.2, 25°C, R18A mutant
1.28
D-ribitol 5-phosphate
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pH 7.2
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0.14 - 13
D-ribitol 5-phosphate
2.8
CTP
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pH 7.2
0.14
D-ribitol 5-phosphate
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pH 7.2, 25°C, R18A mutant
9.7
D-ribitol 5-phosphate
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pH 7.2, 25°C, K386A mutant
13
D-ribitol 5-phosphate
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pH 7.2, 25°C, wild-type enzyme
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additional information
additional information
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additional information
additional information
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Ki(intercept) and Ki(slope)-values
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additional information
additional information
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Ki(intercept) and Ki(slope)-values
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15.7
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CDP-ribitol pyrophosphorylase activity
37.5
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ribitol 5-phosphate dehydrogenase activity
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7.1
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same enzyme activity at pH 7.1 and pH 8
8
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same enzyme activity at pH 7.1 and pH 8
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W23
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UniProt
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UniProt
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W23
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malfunction
defects in DPM1/2/3 and ISPD are considered tertiary dystroglycanopathies since they synthesize the sugar donors Dol-P-Man (POMT1/2) and CDP-ribitol (presumably Fukutin and/or FKRP) for subsequent glycosyltransferases
metabolism
ISPD, similar to the DPM1/2/3 enzyme complex that generates dolichol-phosphomannose for initial mannosylation, generates CDP-ribitol for ribosylation of the phosphotrisaccharide. Both of these processes are involved in the generation of donors for the enzymes involved in functional glycosylation of alpha-dystroglycan and as such congenital muscular dystrophy (CMD) resulting from these enzymes can then be referred to as tertiary dystroglycanopathies
physiological function
ISPD is a CDP-ribitol (ribose) diphosphorylase that generates the reduced sugar nucleotide for the insertion of ribitol in a phosphodiester linkage to the glycoprotein, the enzyme is employed for the synthesis of the required sugar (alcohol) nucleotide needed for ribitol insertion into the M3 glycan
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Bacillus subtilis subsp. spizizenii (strain ATCC 23059 / NRRL B-14472 / W23)
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25000
x * 25000, SDS-PAGE
26000
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2 * 26000 + 2 * 41000, TarI2J2, 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, TarI2J2, 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
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?
x * 25000, SDS-PAGE
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2 * 53190, calculation from amino acid composition
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2 * 26000 + 2 * 41000, TarI2J2, 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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to 1.78 A resolution. Space group C2, dimer in the asymmetric unit
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K368A
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kinetic values similar to wild-type enzyme
R18A
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reduced enzyme activity
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23
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50% loss of activity after 2 h in 20 mM HEPES, 1 mM DTT and 0.5mg/ml bovine serum albumin, decrease of activity can be prevented by addition of 0.005 mM CTP
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unstable, 50% loss of activity after 2 h at 23°C in 20 mM HEPES, 1 mM DTT and 0.5mg/ml bovine serum albumin, decrease of activity can be prevented by addition of 0.05 mM CTP
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enzyme copurifies with ribitol 5-phosphate dehydrogenase activity
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Hi Trap affinity nickel column chromatography and Superdex S200 gel filtration
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recombinant His-tagged enzyme from HEK-293F cells
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expressed in Escherichia coli
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overexpression of TarI and TarJ individually from their respective genes using the T7 expression system
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recombinant expression of His-tagged enzyme in HEK-293F cells
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Shaw, D.R.D.
Phosphorolysis and enzymic synthesis of cytidine diphosphate glycerol and cytidine diphosphate ribitol
Biochem. J.
82
297-312
1962
Bacillus subtilis, Chlorella vulgaris, Lactobacillus plantarum, Lactococcus lactis, Propionibacterium freudenreichii subsp. shermanii, Saccharomyces cerevisiae, Staphylococcus aureus
brenda
Cheah, S.C.; Hussey, H.; Baddiley, J.
Control of synthesis of wall teichoic acid in phosphate-starved cultures of Bacillus subtilis W23
Eur. J. Biochem.
118
497-500
1981
Bacillus subtilis, Bacillus subtilis W23
brenda
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
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
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
Allali-Hassani, A.; Pereira, M.P.; Navani, N.K.; Brown, E.D.; Li, Y.
Isolation of DNA aptamers for CDP-ribitol synthase, and characterization of their inhibitory and structural properties
Chembiochem
8
2052-2057
2007
Haemophilus influenzae
brenda
Chen, S.C.; Yang, C.S.; Lin, C.T.; Chan, N.L.; Chang, M.C.; Chen, Y.
Expression, purification, crystallization and preliminary X-ray analysis of ribitol-5-phosphate cytidylyltransferase from Bacillus subtilis
Acta Crystallogr. Sect. F
68
1195-1197
2012
Bacillus subtilis (Q8RKI9)
brenda
Praissman, J.L.; Willer, T.; Sheikh, M.O.; Toi, A.; Chitayat, D.; Lin, Y.Y.; Lee, H.; Stalnaker, S.H.; Wang, S.; Prabhakar, P.K.; Nelson, S.F.; Stemple, D.L.; Moore, S.A.; Moremen, K.W.; Campbell, K.P.; Wells, L.
The functional O-mannose glycan on alpha-dystroglycan contains a phospho-ribitol primed for matriglycan addition
eLife
5
0000
2016
Homo sapiens (A4D126), Homo sapiens
brenda
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2.7.7.40 D-ribitol-5-phosphate cytidylyltransferase
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