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Information on EC 2.7.7.39 - glycerol-3-phosphate cytidylyltransferase and Organism(s) Bacillus subtilis and UniProt Accession P27623

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IUBMB Comments
Involved in the biosynthesis of teichoic acid linkage units in bacterial cell walls.
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This record set is specific for:
Bacillus subtilis
UNIPROT: P27623
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The taxonomic range for the selected organisms is: Bacillus subtilis
The enzyme appears in selected viruses and cellular organisms
Synonyms
glycerol-3-phosphate cytidylyltransferase, ctp:glycerol-3-phosphate cytidylyltransferase, cdp-glycerol pyrophosphorylase, glycerol 3-phosphate cytidylyltransferase, gro-pct, aq185, aq1368, glycerol phosphate cytidylyltransferase, ctp:glycerol 3-phosphate cytidylyltransferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CDP-glycerol pyrophosphorylase
-
-
-
-
CDPglycerol pyrophosphorylase
-
-
-
-
CTP:glycerol 3-phosphate cytidylyltransferase
-
-
-
-
cytidine diphosphate glycerol pyrophosphorylase
-
-
-
-
cytidine diphosphoglycerol pyrophosphorylase
-
-
-
-
cytidylyltransferase, glycerol 3-phosphate
-
-
-
-
GCT
-
-
-
-
Gro-PCT
-
-
-
-
TarD
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
CTP + sn-glycerol 3-phosphate = diphosphate + CDP-glycerol
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
nucleotidyl group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
CTP:sn-glycerol-3-phosphate cytidylyltransferase
Involved in the biosynthesis of teichoic acid linkage units in bacterial cell walls.
CAS REGISTRY NUMBER
COMMENTARY hide
9027-11-6
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
CTP + sn-glycerol 3-phosphate
diphosphate + CDPglycerol
show the reaction diagram
-
-
?
CTP + sn-glycerol 3-phosphate
diphosphate + CDPglycerol
show the reaction diagram
dCTP + glycerol 3-phosphate
diphosphate + dCDPglycerol
show the reaction diagram
-
about 95% of the activity with CTP
-
-
?
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 + sn-glycerol 3-phosphate
diphosphate + CDPglycerol
show the reaction diagram
-
-
-
?
CTP + sn-glycerol 3-phosphate
diphosphate + CDPglycerol
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Fe2+
-
divalent cation: Co2+, Mg2+, Mn2+ or Fe2+ required
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
CDPglycerol
-
-
diphosphate
-
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.5 - 93.5
CTP
0.45 - 141
glycerol 3-phosphate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.001 - 26.2
CTP
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.9 - 9.5
-
-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
Uniprot
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
14800
-
2 * 14800, gene expression in Escherichia coli, SDS-PAGE
15271
-
2 * 15271, calculated from the nucleotide sequence
30500
-
conditional lethal mutant 168, gel filtration
30900
-
gene expression in E. coli, gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
complexed with CDPglycerol
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K44A
less active than wild-type enzyme
K46A
less active than wild-type enzyme
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
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
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10
-
37°C, 4 h, about 10% loss of activity
645242
6.5
-
37°C, 4 h, about 30% loss of activity
645242
7.5 - 9.5
-
37°C, 4 h, stable
645242
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
-
not stable for longer than 30 min
additional information
-
thermostability of enzyme gro-PCT in extract of strains bearing mutations in tagA, tagB and tagF genes
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, about 20% loss of activity after 1 month
-
-80°C, pure enzyme stable for at least 7 months
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene expression in E. coli
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene expressed in Escherichia coli
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team