Information on EC 2.7.7.40 - D-ribitol-5-phosphate cytidylyltransferase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY hide
2.7.7.40
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RECOMMENDED NAME
GeneOntology No.
D-ribitol-5-phosphate cytidylyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
CTP + D-ribitol 5-phosphate = diphosphate + CDP-ribitol
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
nucleotidyl group transfer
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-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Mannose type O-glycan biosynthesis
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Metabolic pathways
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Pentose and glucuronate interconversions
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poly(ribitol phosphate) wall teichoic acid biosynthesis I (B. subtilis)
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poly(ribitol phosphate) wall teichoic acid biosynthesis II (S. aureus)
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type IV lipoteichoic acid biosynthesis (S. pneumoniae)
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SYSTEMATIC NAME
IUBMB Comments
CTP:D-ribitol-5-phosphate cytidylyltransferase
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CAS REGISTRY NUMBER
COMMENTARY hide
9027-07-0
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
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
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
CTP + D-arabitol 5-phosphate
diphosphate + CDParabitol
show the reaction diagram
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-
-
-
?
CTP + D-ribitol 5-phosphate
diphosphate + CDP-ribitol
show the reaction diagram
CTP + D-ribitol 5-phosphate
diphosphate + CDPribitol
show the reaction diagram
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
CTP + D-ribitol 5-phosphate
diphosphate + CDP-ribitol
show the reaction diagram
A4D126
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-
-
?
CTP + D-ribitol 5-phosphate
diphosphate + CDPribitol
show the reaction diagram
additional information
?
-
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
CDP-ribitol
diphosphate
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00851 - 0.39
CTP
0.0147 - 1.28
D-ribitol 5-phosphate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.8 - 76.8
CTP
0.14 - 13
D-ribitol 5-phosphate
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
15.7
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CDP-ribitol pyrophosphorylase activity
37.5
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ribitol 5-phosphate dehydrogenase activity
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Bacillus subtilis subsp. spizizenii (strain ATCC 23059 / NRRL B-14472 / W23)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
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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
53000
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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
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
to 1.78 A resolution. Space group C2, dimer in the asymmetric unit
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
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
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
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
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K368A
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kinetic values similar to wild-type enzyme
R18A
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reduced enzyme activity