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Information on EC 2.7.7.40 - D-ribitol-5-phosphate cytidylyltransferase
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EC Tree
2.7.7.40 D-ribitol-5-phosphate cytidylyltransferaseSpecify your search results
Word Map
- 2.7.7.40
- polysaccharide
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teichoic
- influenzae
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capsulation
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haemophilus
- aureus
- polymer
- capsular
-
dispensability
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polyribitol
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virulence-associated
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
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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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Bcs1
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
cytidylyltransferase, ribitol 5-phosphate
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ribitol 5-phosphate cytidylyltransferase
Bcs1
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harbors both ribulose 5-phosphate reductase activity and ribitol 5-phosphate cytidylyltransferase activity
ribitol 5-phosphate cytidylyltransferase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
CTP + D-ribitol 5-phosphate = diphosphate + CDP-ribitol
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
nucleotidyl group transfer
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
CTP:D-ribitol-5-phosphate cytidylyltransferase
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CAS REGISTRY NUMBER
COMMENTARY
9027-07-0
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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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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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-
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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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?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
CTP + D-ribitol 5-phosphate
diphosphate + CDPribitol
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-
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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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-
?
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
Show AA Sequence and Transmembrane Helices (1407 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
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calculation from gel filtration and sedimentation velocity data
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
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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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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
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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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Hi Trap affinity nickel column chromatography and Superdex S200 gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
overexpression of TarI and TarJ individually from their respective genes using the T7 expression system
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Shaw, D.R.D.
Phosphorolysis and enzymic synthesis of cytidine diphosphate glycerol and cytidine diphosphate ribitol
Biochem. J.
82
297-312
1962
Bacillus subtilis, Saccharomyces cerevisiae, Chlorella vulgaris, Lactiplantibacillus plantarum, Lactococcus lactis, Staphylococcus aureus, Propionibacterium freudenreichii subsp. shermanii
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
e14473
2016
Homo sapiens (A4D126), Homo sapiens
brenda
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