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Enzyme Nomenclature
Information on EC 2.7.7.40 - D-ribitol-5-phosphate cytidylyltransferase
for references in articles please use BRENDA:EC2.7.7.40
Word Map on EC 2.7.7.40
- 2.7.7.40
- polysaccharide
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teichoic
- influenzae
- aureus
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capsulation
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haemophilus
- subtilis
- capsular
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dispensability
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polyribitol
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virulence-associated
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paradox
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
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EC NUMBER 
COMMENTARY 
2.7.7.40
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RECOMMENDED NAME
GeneOntology No.
D-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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-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
nucleotidyl group transfer
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-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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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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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
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
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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
-
ordered bi-bi mechanism
-
?
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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-
-
?
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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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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additional information
?
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enzyme has also ribitol 5-phosphate dehydrogenase activity
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-
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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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-
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additional information
?
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no activity with ATP, GTP, UTP, ADP or CDP
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-
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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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NATURAL SUBSTRATES
NATURAL PRODUCTS
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
?
-
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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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INHIBITORS
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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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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PDB
SCOP
CATH
ORGANISM
UNIPROT
Bacillus subtilis subsp. spizizenii (strain ATCC 23059 / NRRL B-14472 / W23)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
129000
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calculation from gel filtration and sedimentation velocity data
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
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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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Crystallization/COMMENTARY
ORGANISM
UNIPROT
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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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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LINKS TO OTHER DATABASES (specific for EC-Number 2.7.7.40)
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