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CTP + sn-glycerol 3-phosphate
diphosphate + CDP-glycerol
CTP + sn-glycerol 3-phosphate
diphosphate + CDPglycerol
dCTP + glycerol 3-phosphate
diphosphate + dCDPglycerol
-
about 95% of the activity with CTP
-
-
?
additional information
?
-
CTP + sn-glycerol 3-phosphate
diphosphate + CDP-glycerol
the enzyme from gene AQ185 is absolutely specific for sn-glycerol 3-phosphate
-
-
?
CTP + sn-glycerol 3-phosphate
diphosphate + CDP-glycerol
the enzyme from gene AQ1368 has a 2:1 preference for sn-glycerol 3-phosphate over sn-glycerol 1-phosphate
-
-
?
CTP + sn-glycerol 3-phosphate
diphosphate + CDP-glycerol
-
-
-
?
CTP + sn-glycerol 3-phosphate
diphosphate + CDPglycerol
-
-
-
-
?
CTP + sn-glycerol 3-phosphate
diphosphate + CDPglycerol
-
enzyme is inactivated under phosphate-limited conditions
-
-
?
CTP + sn-glycerol 3-phosphate
diphosphate + CDPglycerol
-
enzyme is possibly a control point in synthesis of the cell wall in Bacillus licheniformis
-
-
?
CTP + sn-glycerol 3-phosphate
diphosphate + CDPglycerol
-
-
-
?
CTP + sn-glycerol 3-phosphate
diphosphate + CDPglycerol
-
-
-
-
?
CTP + sn-glycerol 3-phosphate
diphosphate + CDPglycerol
-
-
?
CTP + sn-glycerol 3-phosphate
diphosphate + CDPglycerol
-
enzyme of teichoic acid synthesis
-
-
?
CTP + sn-glycerol 3-phosphate
diphosphate + CDPglycerol
-
repression of synthesis occurs at the onset of phosphate starvation and is accompanied by inhibition or inactivation of CDPglycerol pyrophosphorylase
-
-
?
CTP + sn-glycerol 3-phosphate
diphosphate + CDPglycerol
-
CDPglycerol may function in: synthesis of lipids
-
-
?
CTP + sn-glycerol 3-phosphate
diphosphate + CDPglycerol
-
-
-
-
?
CTP + sn-glycerol 3-phosphate
diphosphate + CDPglycerol
-
repression of synthesis occurs at the onset of phosphate starvation and is accompanied by inhibition or inactivation of CDPglycerol pyrophosphorylase
-
-
?
CTP + sn-glycerol 3-phosphate
diphosphate + CDPglycerol
-
-
-
?
CTP + sn-glycerol 3-phosphate
diphosphate + CDPglycerol
-
CDPglycerol may function in: synthesis of lipids
-
-
?
CTP + sn-glycerol 3-phosphate
diphosphate + CDPglycerol
-
-
-
?
CTP + sn-glycerol 3-phosphate
diphosphate + CDPglycerol
-
CDPglycerol may function in: synthesis of lipids
-
-
?
CTP + sn-glycerol 3-phosphate
diphosphate + CDPglycerol
-
-
-
r
CTP + sn-glycerol 3-phosphate
diphosphate + CDPglycerol
-
CDPglycerol may function in: synthesis of lipids
-
-
r
CTP + sn-glycerol 3-phosphate
diphosphate + CDPglycerol
-
-
-
?
CTP + sn-glycerol 3-phosphate
diphosphate + CDPglycerol
-
CDPglycerol may function in: synthesis of lipids
-
-
?
CTP + sn-glycerol 3-phosphate
diphosphate + CDPglycerol
-
-
-
?
CTP + sn-glycerol 3-phosphate
diphosphate + CDPglycerol
-
-
-
-
?
CTP + sn-glycerol 3-phosphate
diphosphate + CDPglycerol
-
CDPglycerol may function in: synthesis of lipids
-
-
?
CTP + sn-glycerol 3-phosphate
diphosphate + CDPglycerol
-
-
-
?, r
CTP + sn-glycerol 3-phosphate
diphosphate + CDPglycerol
-
-
-
-
r
CTP + sn-glycerol 3-phosphate
diphosphate + CDPglycerol
-
CDPglycerol may function in: synthesis of lipids
-
-
?, r
additional information
?
-
-
no substrate: phosphoethanolamine
-
-
?
additional information
?
-
-
no substrate: UTP
-
-
?
additional information
?
-
-
no substrate: GTP
-
-
?
additional information
?
-
-
no substrate: ATP
-
-
?
additional information
?
-
-
no substrate: ribitol phosphate
-
-
?
additional information
?
-
-
no substrate: phosphocholine
-
-
?
additional information
?
-
-
no substrate: cytidine diphosphate ribitol
-
-
?
additional information
?
-
-
no substrate: ITP
-
-
?
additional information
?
-
-
no substrate: phosphoethanolamine
-
-
?
additional information
?
-
-
no substrate: UTP
-
-
?
additional information
?
-
-
no substrate: ATP
-
-
?
additional information
?
-
-
no substrate: ribitol phosphate
-
-
?
additional information
?
-
-
no substrate: phosphocholine
-
-
?
additional information
?
-
-
no substrate: cytidine diphosphate ribitol
-
-
?
additional information
?
-
-
no substrate: ITP
-
-
?
additional information
?
-
using an assay method for determination of the catalytic activity measuring the production of radiolabeled CDP-glycerol from 14C-labeled sn-glycerol 3-phosphate, and separation of non-radioactive CDP-glycerol from CTP by C18 reverse phase HPLC with a mobile phase of 0.1 M ammonium bicarbonate (98%) and acetonitrile (2%) at pH 7.4
-
-
?
additional information
?
-
-
no substrate: phosphoethanolamine
-
-
?
additional information
?
-
-
no substrate: UTP
-
-
?
additional information
?
-
-
no substrate: ATP
-
-
?
additional information
?
-
-
no substrate: ribitol phosphate
-
-
?
additional information
?
-
-
no substrate: phosphocholine
-
-
?
additional information
?
-
-
no substrate: cytidine diphosphate ribitol
-
-
?
additional information
?
-
-
no substrate: ITP
-
-
?
additional information
?
-
-
no substrate: phosphoethanolamine
-
-
?
additional information
?
-
-
no substrate: UTP
-
-
?
additional information
?
-
-
no substrate: ATP
-
-
?
additional information
?
-
-
no substrate: ribitol phosphate
-
-
?
additional information
?
-
-
no substrate: phosphocholine
-
-
?
additional information
?
-
-
no substrate: cytidine diphosphate ribitol
-
-
?
additional information
?
-
-
no substrate: ITP
-
-
?
additional information
?
-
-
no substrate: phosphoethanolamine
-
-
?
additional information
?
-
-
no substrate: UTP
-
-
?
additional information
?
-
-
no substrate: ATP
-
-
?
additional information
?
-
-
no substrate: ribitol phosphate
-
-
?
additional information
?
-
-
no substrate: phosphocholine
-
-
?
additional information
?
-
-
no substrate: cytidine diphosphate ribitol
-
-
?
additional information
?
-
-
no substrate: ITP
-
-
?
additional information
?
-
-
no substrate: phosphoethanolamine
-
-
?
additional information
?
-
-
no substrate: UTP
-
-
?
additional information
?
-
-
no substrate: ATP
-
-
?
additional information
?
-
-
no substrate: ribitol phosphate
-
-
?
additional information
?
-
-
no substrate: phosphocholine
-
-
?
additional information
?
-
-
no substrate: cytidine diphosphate ribitol
-
-
?
additional information
?
-
-
no substrate: ITP
-
-
?
additional information
?
-
-
no substrate: phosphoethanolamine
-
-
?
additional information
?
-
-
no substrate: UTP
-
-
?
additional information
?
-
-
no substrate: ATP
-
-
?
additional information
?
-
-
no substrate: ribitol phosphate
-
-
?
additional information
?
-
-
no substrate: phosphocholine
-
-
?
additional information
?
-
-
no substrate: cytidine diphosphate ribitol
-
-
?
additional information
?
-
-
no substrate: ITP
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CTP + sn-glycerol 3-phosphate
diphosphate + CDP-glycerol
CTP + sn-glycerol 3-phosphate
diphosphate + CDPglycerol
CTP + sn-glycerol 3-phosphate
diphosphate + CDP-glycerol
the enzyme from gene AQ185 is absolutely specific for sn-glycerol 3-phosphate
-
-
?
CTP + sn-glycerol 3-phosphate
diphosphate + CDP-glycerol
-
-
-
?
CTP + sn-glycerol 3-phosphate
diphosphate + CDPglycerol
-
enzyme is inactivated under phosphate-limited conditions
-
-
?
CTP + sn-glycerol 3-phosphate
diphosphate + CDPglycerol
-
enzyme is possibly a control point in synthesis of the cell wall in Bacillus licheniformis
-
-
?
CTP + sn-glycerol 3-phosphate
diphosphate + CDPglycerol
-
-
-
-
?
CTP + sn-glycerol 3-phosphate
diphosphate + CDPglycerol
-
-
-
?
CTP + sn-glycerol 3-phosphate
diphosphate + CDPglycerol
-
enzyme of teichoic acid synthesis
-
-
?
CTP + sn-glycerol 3-phosphate
diphosphate + CDPglycerol
-
repression of synthesis occurs at the onset of phosphate starvation and is accompanied by inhibition or inactivation of CDPglycerol pyrophosphorylase
-
-
?
CTP + sn-glycerol 3-phosphate
diphosphate + CDPglycerol
-
CDPglycerol may function in: synthesis of lipids
-
-
?
CTP + sn-glycerol 3-phosphate
diphosphate + CDPglycerol
-
repression of synthesis occurs at the onset of phosphate starvation and is accompanied by inhibition or inactivation of CDPglycerol pyrophosphorylase
-
-
?
CTP + sn-glycerol 3-phosphate
diphosphate + CDPglycerol
-
CDPglycerol may function in: synthesis of lipids
-
-
?
CTP + sn-glycerol 3-phosphate
diphosphate + CDPglycerol
-
CDPglycerol may function in: synthesis of lipids
-
-
?
CTP + sn-glycerol 3-phosphate
diphosphate + CDPglycerol
-
CDPglycerol may function in: synthesis of lipids
-
-
r
CTP + sn-glycerol 3-phosphate
diphosphate + CDPglycerol
-
CDPglycerol may function in: synthesis of lipids
-
-
?
CTP + sn-glycerol 3-phosphate
diphosphate + CDPglycerol
-
-
-
-
?
CTP + sn-glycerol 3-phosphate
diphosphate + CDPglycerol
-
CDPglycerol may function in: synthesis of lipids
-
-
?
CTP + sn-glycerol 3-phosphate
diphosphate + CDPglycerol
-
-
-
-
r
CTP + sn-glycerol 3-phosphate
diphosphate + CDPglycerol
-
CDPglycerol may function in: synthesis of lipids
-
-
?, r
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C106A
-
mutant with kinetic constants similar to wild-type enzyme
D11A
-
mutant with low kcat value
D11E
-
mutant with low kcat value
D38A
-
mutant with high Km value
D38E
-
kcat similar to wild-type enzyme
D66A
-
mutant with low kcat value, defective in overall structure
D66E
-
mutant with low kcat value
D87A
-
mutant with kinetic constants similar to wild-type enzyme
D92A
-
mutant with kinetic constants similar to wild-type enzyme
D94A/H14A
-
binding constants for CTP and glycerol 3-phosphate are similar to wild-type enzyme
D94E mutant
-
mutant with low kcat value
E115A
-
mutant with kinetic constants similar to wild-type enzyme
E39A
-
mutant with kinetic constants similar to wild-type enzyme
E67A
-
mutant with kinetic constants similar to wild-type enzyme
H84A
-
mutant with low kcat value
K103A
-
mutant with kinetic constants similar to wild-type enzyme
K19A
-
mutant with kinetic constants similar to wild-type enzyme
K22A
-
mutant with kinetic constants similar to wild-type enzyme
K25A
-
mutant with kinetic constants similar to wild-type enzyme
K44A
less active than wild-type enzyme
K46A
less active than wild-type enzyme
R113A
-
mutant with low kcat value
R113K
-
mutant with low kcat value
R55A
-
mutant with low kcat value
R55K
-
mutant with low kcat value
R63A
-
mutant with low kcat value
S118A
-
mutant with low kcat value t
T114A
-
mutant with low kcat value
T119A
-
mutant with low kcat value
W74A
-
mutant with high Km value
D94A
-
mutant with high Km value
D94A
-
initial binding constant is similar to wild-type enzyme
H14A
-
mutant with low kcat value, dramatic loss of activity
H14A
-
Kd value for binding of a single substrate is similar to those for the wild-type enzyme
H17A
-
mutant with low kcat value, dramatic loss of activity
H17A
-
initial binding constant is similar to wild-type enzyme
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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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, Escherichia coli, Lactiplantibacillus plantarum, 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
Park, Y.S.; Sweitzer, T.D.; Dixon, J.E.; Kent, C.
Expression, purification, and characterization of CTP:glycerol-3-phosphate cytidylyltransferase from Bacillus subtilis
J. Biol. Chem.
268
16648-16654
1993
Bacillus subtilis
brenda
Pooley, H.M.; Abellan, F.X.; Karamata, D.
A conditional-lethal mutant of bacillus subtilis 168 with a thermosensitive glycerol-3-phosphate cytidylyltransferase, an enzyme specific for the synthesis of the major wall teichoic acid
J. Gen. Microbiol.
137
921-928
1991
Bacillus subtilis
brenda
Hussey, H.; Sueda, S.; Cheah, S.C.; Baddiley, J.
Control of teichoic acid synthesis in Bacillus licheniformis ATCC 9945
Eur. J. Biochem.
82
169-174
1978
Bacillus licheniformis
brenda
Anderson, R.G.; Douglas, L.J.; Hussey, H.; Baddiley, J.
The control of synthesis of bacterial cell walls. Interaction in the synthesis of nucleotide precursors
Biochem. J.
136
871-876
1973
Bacillus licheniformis
brenda
Badurina, D.S.; Zolli-Juran, M.; Brown, E.D.
CTP:glycerol 3-phosphate cytidylyltransferase (TarD) from Staphylococcus aureus catalyzes the cytidylyl transfer via an ordered bi-bi reaction mechanism with micromolar K(m) values
Biochim. Biophys. Acta
1646
196-206
2003
Saccharomyces cerevisiae, Staphylococcus aureus
brenda
Park, Y.S.; Gee, P.; Sanker, S.; Schurter, E.J.; Zuiderweg, E.R.; Kent, C.
Identification of functional conserved residues of CTP:glycerol-3-phosphate cytidylyltransferase. Role of histidines in the conserved HXGH in catalysis
J. Biol. Chem.
272
15161-15166
1997
Bacillus subtilis
brenda
Pattridge, K.A.; Weber, C.H.; Friesen, J.A.; Sanker, S.; Kent, C.; Ludwig, M.L.
Glycerol-3-phosphate cytidylyltransferase: Structural changes induced by binding of CDP-glycerol and the role of lysine residues in catalysis
J. Biol. Chem.
278
51863-51871
2003
Bacillus subtilis (P27623), Bacillus subtilis
brenda
Sanker, S.; Campbell, H.A.; Kent, C.
Negative cooperativity of substrate binding but not enzyme activity in wild-type and mutant forms of CTP:glycerol-3-phosphate cytidylyltransferase
J. Biol. Chem.
276
37922-37928
2001
Bacillus subtilis
brenda
Yim, V.C.; Zolli, M.; Badurina, D.S.; Rossi, L.; Brown, E.D.; Berghuis, A.M.
Crystallization and preliminary X-ray diffraction studies of glycerol 3-phosphate cytidylyltransferase from Staphylococcus aureus
Acta Crystallogr. Sect. D
57
918-920
2001
Saccharomyces cerevisiae, Staphylococcus aureus
brenda
Fong, D.H.; Yim, V.C.; DElia, M.A.; Brown, E.D.; Berghuis, A.M.
Crystal structure of CTP:glycerol-3-phosphate cytidylyltransferase from Staphylococcus aureus: Examination of structural basis for kinetic mechanism
Biochim. Biophys. Acta
1764
63-69
2006
Staphylococcus aureus
brenda
Brault, J.P.; Friesen, J.A.
Characterization of cytidylyltransferase enzyme activity through high performance liquid chromatography
Anal. Biochem.
510
26-32
2016
Enterococcus faecalis (Q836D9)
brenda
Rodrigues, M.V.; Borges, N.; Santos, H.
Glycerol phosphate cytidylyltransferase stereospecificity is key to understanding the distinct stereochemical compositions of glycerophosphoinositol in Bacteria and Archaea
Appl. Environ. Microbiol.
83
e02462-16
2016
Aquifex aeolicus (O66572), Aquifex aeolicus (O67380), Aquifex aeolicus
brenda