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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
-
muscular
-
dystrophy
- polysaccharide
-
teichoic
-
dystroglycanopathy
-
fukutin-related
-
fukutin
- influenzae
-
walker-warburg
-
haemophilus
- glycan
-
o-mannose
- capsular
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virulence-associated
- alpha-dystroglycan
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hydrocephalus
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dispensability
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malformation
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polyribitol
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lissencephaly
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hypoplasia
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
Bcs1, CDP-L-ribitol pyrophosphorylase A, CDP-ribitol (ribose) pyrophosphorylase, CDP-ribitol pyrophosphorylase, CDP-ribitol synthase, CDPribitol pyrophosphorylase, CRPPA, cytidine diphosphate ribitol pyrophosphorylase, cytidine diphosphate-l-ribitol pyrophosphorylase A, Cytidine diphosphoribitol pyrophosphorylase, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Bcs1
CDP-L-ribitol pyrophosphorylase A
CDP-ribitol pyrophosphorylase
CDPribitol pyrophosphorylase
-
-
-
-
CRPPA
cytidine diphosphate ribitol pyrophosphorylase
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-
-
-
cytidine diphosphate-l-ribitol pyrophosphorylase A
Cytidine diphosphoribitol pyrophosphorylase
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-
-
-
cytidylyltransferase
cytidylyltransferase, ribitol 5-phosphate
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-
-
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IspD
ribitol 5-phosphate cytidylyltransferase
Bcs1
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harbors both ribulose 5-phosphate reductase activity and ribitol 5-phosphate cytidylyltransferase activity
CDP-ribitol pyrophosphorylase
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-
-
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ribitol 5-phosphate cytidylyltransferase
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-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
CTP + D-ribitol 5-phosphate = diphosphate + CDP-ribitol
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-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
nucleotidyl group transfer
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-
-
-
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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-arabitol 5-phosphate
diphosphate + CDP-arabitol
up to 10% activity compared to D-ribitol 5-phosphate
-
-
?
CTP + D-xylitol 5-phosphate
diphosphate + CDP-xylitol
up to 10% activity compared to D-ribitol 5-phosphate
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-
?
CTP + D-ribitol 5-phosphate
diphosphate + CDP-ribitol
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ordered bi-bi mechanism
-
?
CTP + D-ribitol 5-phosphate
diphosphate + CDP-ribitol
highest activity
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-
r
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
-
?
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
?
-
-
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 has no activity with UTP, or in the presence of CTP and 2-C-methyl-D-erythritol 4-phosphate
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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
-
-
-
-
?
additional information
?
-
-
enzyme functions possibly in synthesis of teichoic acids, repression of enzyme synthesis occurs at the onset of phosphate starvation
-
-
?
additional information
?
-
-
enzyme functions possibly in synthesis of teichoic acids, repression of enzyme synthesis occurs at the onset of phosphate starvation
-
-
?
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Muscular Diseases
Cytidine Diphosphate-Ribitol Analysis for Diagnostics and Treatment Monitoring of Cytidine Diphosphate-L-Ribitol Pyrophosphorylase A Muscular Dystrophy.
Muscular Dystrophies
Cytidine Diphosphate-Ribitol Analysis for Diagnostics and Treatment Monitoring of Cytidine Diphosphate-L-Ribitol Pyrophosphorylase A Muscular Dystrophy.
Muscular Dystrophies
Homozygous deletion, c. 1114-1116del, in exon 8 of the CRPPA gene causes congenital muscular dystrophy in Chinese family: A case report.
Muscular Dystrophies, Limb-Girdle
Cytidine Diphosphate-Ribitol Analysis for Diagnostics and Treatment Monitoring of Cytidine Diphosphate-L-Ribitol Pyrophosphorylase A Muscular Dystrophy.
Walker-Warburg Syndrome
Analysis of genotype-phenotype correlation in Walker-Warburg syndrome with a novel CRPPA mutation in different clinical manifestations.
Walker-Warburg Syndrome
Cytidine Diphosphate-Ribitol Analysis for Diagnostics and Treatment Monitoring of Cytidine Diphosphate-L-Ribitol Pyrophosphorylase A Muscular Dystrophy.
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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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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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
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
metabolism
CDP-ribitol pyrophosphorylase activity of the enzyme is required for correct alpha-dystroglycan glycosylation
Show AA Sequence and Transmembrane Helices (1618 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, 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
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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
-
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, Chlorella vulgaris, Lactiplantibacillus 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
e14473
2016
Homo sapiens (A4D126), Homo sapiens
brenda
van Tol, W.; van Scherpenzeel, M.; Alsady, M.; Riemersma, M.; Hermans, E.; Kragt, E.; Tasca, G.; Kamsteeg, E.J.; Pennings, M.; van Beusekom, E.; Vermeulen, J.R.; van Bokhoven, H.; Voermans, N.C.; Willemsen, M.A.; Ashikov, A.; Lefeber, D.J.
Cytidine diphosphate-ribitol analysis for diagnostics and treatment monitoring of cytidine diphosphate-l-ribitol pyrophosphorylase A muscular dystrophy
Clin. Chem.
65
1295-1306
2019
Homo sapiens (A4D126), Homo sapiens, Mus musculus (Q5RJG7), Mus musculus
brenda
Gerin, I.; Ury, B.; Breloy, I.; Bouchet-Seraphin, C.; Bolsee, J.; Halbout, M.; Graff, J.; Vertommen, D.; Muccioli, G.G.; Seta, N.; Cuisset, J.M.; Dabaj, I.; Quijano-Roy, S.; Grahn, A.; Van Schaftingen, E.; Bommer, G.T.
ISPD produces CDP-ribitol used by FKTN and FKRP to transfer ribitol phosphate onto alpha-dystroglycan
Nat. Commun.
7
11534
2016
Mus musculus (Q5RJG7)
brenda
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