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CTP + D-arabitol 5-phosphate
diphosphate + CDP-arabitol
up to 10% activity compared to D-ribitol 5-phosphate
-
-
?
CTP + D-arabitol 5-phosphate
diphosphate + CDParabitol
-
-
-
-
?
CTP + D-ribitol 5-phosphate
diphosphate + CDP-ribitol
CTP + D-ribitol 5-phosphate
diphosphate + CDPribitol
CTP + D-xylitol 5-phosphate
diphosphate + CDP-xylitol
up to 10% activity compared to D-ribitol 5-phosphate
-
-
?
additional information
?
-
CTP + D-ribitol 5-phosphate
diphosphate + CDP-ribitol
-
-
-
-
?
CTP + D-ribitol 5-phosphate
diphosphate + CDP-ribitol
-
ordered bi-bi mechanism
-
?
CTP + D-ribitol 5-phosphate
diphosphate + CDP-ribitol
-
-
-
?
CTP + D-ribitol 5-phosphate
diphosphate + CDP-ribitol
-
-
-
-
?
CTP + D-ribitol 5-phosphate
diphosphate + CDP-ribitol
-
-
-
?
CTP + D-ribitol 5-phosphate
diphosphate + CDP-ribitol
-
-
-
r
CTP + D-ribitol 5-phosphate
diphosphate + CDP-ribitol
highest activity
-
-
r
CTP + D-ribitol 5-phosphate
diphosphate + CDP-ribitol
-
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
-
-
-
?
CTP + D-ribitol 5-phosphate
diphosphate + CDPribitol
-
-
-
?
CTP + D-ribitol 5-phosphate
diphosphate + CDPribitol
-
-
-
-
?
CTP + D-ribitol 5-phosphate
diphosphate + CDPribitol
-
-
-
?
CTP + D-ribitol 5-phosphate
diphosphate + CDPribitol
-
-
-
?
CTP + D-ribitol 5-phosphate
diphosphate + CDPribitol
-
-
-
?
CTP + D-ribitol 5-phosphate
diphosphate + CDPribitol
-
-
-
?
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
-
-
?
additional information
?
-
-
enzyme has also ribitol 5-phosphate dehydrogenase activity
-
-
?
additional information
?
-
-
enzyme has also ribitol 5-phosphate dehydrogenase activity
-
-
?
additional information
?
-
-
no activity with erythritol 4-phosphate, sorbitol 6-phosphate and UTP
-
-
?
additional information
?
-
-
no activity with ATP, GTP, UTP, ADP or CDP
-
-
?
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
-
-
?
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
-
-
?
additional information
?
-
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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CTP + D-ribitol 5-phosphate
diphosphate + CDP-ribitol
CTP + D-ribitol 5-phosphate
diphosphate + CDPribitol
additional information
?
-
CTP + D-ribitol 5-phosphate
diphosphate + CDP-ribitol
-
-
-
?
CTP + D-ribitol 5-phosphate
diphosphate + CDP-ribitol
-
-
-
-
?
CTP + D-ribitol 5-phosphate
diphosphate + CDP-ribitol
-
-
-
?
CTP + D-ribitol 5-phosphate
diphosphate + CDP-ribitol
-
-
-
r
CTP + D-ribitol 5-phosphate
diphosphate + CDPribitol
-
-
-
-
?
CTP + D-ribitol 5-phosphate
diphosphate + CDPribitol
-
-
-
-
?
CTP + D-ribitol 5-phosphate
diphosphate + CDPribitol
-
-
-
-
?
CTP + D-ribitol 5-phosphate
diphosphate + CDPribitol
-
-
-
-
?
CTP + D-ribitol 5-phosphate
diphosphate + CDPribitol
-
-
-
-
?
CTP + D-ribitol 5-phosphate
diphosphate + CDPribitol
-
-
-
-
?
CTP + D-ribitol 5-phosphate
diphosphate + CDPribitol
-
-
-
-
?
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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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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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
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