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Information on EC 2.7.7.40 - D-ribitol-5-phosphate cytidylyltransferase and Organism(s) Homo sapiens and UniProt Accession A4D126

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Homo sapiens
UNIPROT: A4D126 not found.
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
crppa, cdp-ribitol synthase, tarij, cdp-ribitol pyrophosphorylase, isoprenoid synthase domain-containing protein, cdp-ribitol (ribose) pyrophosphorylase, cytidine diphosphate-l-ribitol pyrophosphorylase a, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CDP-L-ribitol pyrophosphorylase A
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CDP-ribitol (ribose) pyrophosphorylase
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cytidine diphosphate-l-ribitol pyrophosphorylase A
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CDP-ribitol pyrophosphorylase
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-
-
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CDPribitol pyrophosphorylase
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-
-
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cytidine diphosphate ribitol pyrophosphorylase
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-
-
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Cytidine diphosphoribitol pyrophosphorylase
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-
-
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cytidylyltransferase, ribitol 5-phosphate
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-
-
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ribitol 5-phosphate cytidylyltransferase
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-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
nucleotidyl group transfer
-
-
-
-
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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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-ribitol 5-phosphate
diphosphate + CDP-ribitol
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
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
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
highest activity
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
ISPD_HUMAN
451
0
49873
Swiss-Prot
other Location (Reliability: 4)
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A122P
the mutation potentially affects cytidyltransferase activity
A216D
the mutation potentially affects cytidyltransferase activity
G54A
the mutation potentially affects cytidyltransferase activity
R184G
the mutation potentially affects cytidyltransferase activity
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from HEK-293F cells
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant expression of His-tagged enzyme in HEK-293F cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team