Information on EC 2.7.7.33 - glucose-1-phosphate cytidylyltransferase

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The expected taxonomic range for this enzyme is: Bacteria

EC NUMBER
COMMENTARY hide
2.7.7.33
-
RECOMMENDED NAME
GeneOntology No.
glucose-1-phosphate cytidylyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
CTP + alpha-D-glucose 1-phosphate = diphosphate + CDP-glucose
show the reaction diagram
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-
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-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
nucleotidyl group transfer
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Amino sugar and nucleotide sugar metabolism
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-
CDP-4-dehydro-3,6-dideoxy-D-glucose biosynthesis
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Metabolic pathways
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Starch and sucrose metabolism
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streptomycin biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
CTP:alpha-D-glucose-1-phosphate cytidylyltransferase
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CAS REGISTRY NUMBER
COMMENTARY hide
9027-10-5
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain O
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-
Manually annotated by BRENDA team
strain O
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-
Manually annotated by BRENDA team
no activity in Streptomyces griseus
streptomycin producing strain N2-3-11
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Manually annotated by BRENDA team
LT2, ecombinant, overproducing strain P9254
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Manually annotated by BRENDA team
strain GLA.0
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Manually annotated by BRENDA team
strain GLA.0
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Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
CTP + alpha-D-glucose 1-phosphate
diphosphate + CDP-glucose
show the reaction diagram
CTP + alpha-D-glucose 1-phosphate
diphosphate + CDPglucose
show the reaction diagram
CTP + alpha-D-xylose 1-phosphate
diphosphate + CDPxylose
show the reaction diagram
-
poor substrate
-
?
CTP + D-glucosamine 1-phosphate
diphosphate + CDPglucosamine
show the reaction diagram
CTP + D-glucose 1-phosphate
?
show the reaction diagram
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
show the reaction diagram
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 + alpha-D-glucose 1-phosphate
diphosphate + CDP-glucose
show the reaction diagram
Q8KN04
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-
-
?
CTP + D-glucose 1-phosphate
?
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ADPglucose
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weak
CDP-2-O-methyldeoxyaldose
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CDP-4-keto-6-deoxy-D-glucose
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CDP-ascarylose
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synonym: 3,6-dideoxy-L-mannose, strong, kinetics
CDP-D-fucose/CDP-6-deoxy-D-glucose mixture
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CDP-D-galactose
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weak
CDPabequose
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synonym: 3,6-dideoxy-D-galactose, strong
CDPglucose
CDPparatose
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synonym: 3,6-dideoxy-D-glucose, feed-back inhibition, CDPglucose partially reverses, maximal inhibition at 0.6 mM
diphosphate
dTTP
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strong, competitive with CTP, kinetics
phosphate
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weak
additional information
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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no activation by dTDP-L-rhamnose, dTDP-4-amino-4,6-dideoxy-D-glucose and its N-acetyl-derivative, UDP-D-galactose, UDP-D-glucuronic acid, UDP-N-acetyl-D-glucosamine, GDP-D-mannose, D-glucose 6-phosphate, D-glucose 1,6-diphosphate, D-galactose 1-phosphate, D-glucosamine 1-phosphate, D-mannose 1-phosphate, N-acetyl-D-glucosamine 1-phosphate, D-fructose 6-phosphate, D-fructose 1,6-diphosphate, D-ribitol 5-phosphate, L-glycerol 3-phosphate, phosphoenolpyruvate, pyruvate, ADP, AMP, GMP, UMP, beta-NAD+ or beta-NADP+
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.052 - 0.64
alpha-D-glucose 1-phosphate
0.11
alpha-D-glucose-1-phosphate
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pH 7.5, 30C
0.41
CDP-D-glucose
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pH 7.5, 30C, Mg2+ as cation
0.034 - 0.28
CTP
5
D-glucosamine 1-phosphate
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pH 8.5, 37C
0.067 - 1.89
diphosphate
0.43 - 0.56
magnesium diphosphate
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.35
CDPglucose
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pH 8.5, 37C
0.3
diphosphate
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pH 8.5, 37C
0.04
dTTP
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pH 8.5, 37C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8 - 10
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broad, Mg2+ as activating cation
8.3
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diphosphorolysis
8.5
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CDPglucose synthesis
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.2 - 9.5
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about half-maximal activity at pH 6.2 and about 70% of maximal activity at pH 9.5
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PDB
SCOP
CATH
ORGANISM
UNIPROT
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30900
including 2.5 kDa of His-tag originated from pET30a, determined by SDS-PAGE
116000
gel filtration
120000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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x * 29035, calculated from amino acid composition deduced from nucleotide sequence, x * 31000, SDS-PAGE
monomer
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1 * 110000, SDS-PAGE
tetramer
4 * 29000, SDS-PAGE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging-drop vapour-diffusion method, crystallized in the presence of its product, CDP-glucose. Enzyme exists as a fully integrated hexamer with 32-point group symmetry
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hanging-drop vapour-diffusion method.The structure of the enzyme with bound MgCTP reveals that the binding pocket for the nucleotide is contained within one subunit rather than shared between two. Key side chains involved in nucleotide binding include Thr14, Arg15, Lys25, and Arg111
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6
irreversible inactivation below pH 6
643242
6.5
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rapid and irreversible inactivation below
643239
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
during the latter stages of purification the enzyme preparation is quite unstable to cold room conditions over a period of 2 to 3 days
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Stable to repeated freeze-thawing
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-18C, in EDTA-containing Tris-HCl buffer, at least 1 year
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-20C, about 30% loss of activity within 1 month
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-80C stable for months with no loss of activity, freezing and thawing does not affect the enzyme activity
frozen, 2-3 months stable
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
on a Ni-NTA His-Bind resin column
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
the ste17 gene coding region is cloned into the plasmid pET30a for expression in Escherichia coli BL21 cells
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
ebosin is an exopolysaccharide with antagonist activity for interleukin-1 receptor in vitro and remarkable anti-rheumatic arthritis activity in vivo
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