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Information on EC 2.7.7.24 - glucose-1-phosphate thymidylyltransferase and Organism(s) Sulfurisphaera tokodaii and UniProt Accession Q975F9

for references in articles please use BRENDA:EC2.7.7.24
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IUBMB Comments
Involved in the biosynthesis of L-rhamnose in bacteria.
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Select one or more organisms in this record:
This record set is specific for:
Sulfurisphaera tokodaii
UNIPROT: Q975F9
Word Map
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The taxonomic range for the selected organisms is: Sulfurisphaera tokodaii
Synonyms
Cps2L, D-glucose-1-phosphate thymidylyltransferase, DnmL, dTDP-D-glucose synthase, dTDP-glucose synthase, dTDP-glucose-pyrophosphorylase, dTDPglucose pyrophosphorylase, Glc-1-P TTase, Glc-1-P-TT, glucose 1-phosphate thymidylyltransferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dTDP-glucose synthase
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-
-
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dTDP-glucose-pyrophosphorylase
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-
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dTDPglucose pyrophosphorylase
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-
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Glc-1-P TTase
299945
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glucose 1-phosphate thymidylyltransferase
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glucose-1-phosphate thymidylyltransferase
299945
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ST0452
TDP-glucose pyrophosphorylase
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thymidine diphosphate glucose pyrophosphorylase
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thymidine diphosphoglucose pyrophosphorylase
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thymidylyltransferase, glucose 1-phosphate
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
nucleotidyl group transfer
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SYSTEMATIC NAME
IUBMB Comments
dTTP:alpha-D-glucose-1-phosphate thymidylyltransferase
Involved in the biosynthesis of L-rhamnose in bacteria.
CAS REGISTRY NUMBER
COMMENTARY hide
9026-03-3
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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
diphosphate + dTDP-alpha-D-glucose
dTTP + alpha-D-glucose 1-phosphate
show the reaction diagram
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-
-
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r
dTTP + alpha-D-glucose 1-phosphate
diphosphate + dTDP-alpha-D-glucose
show the reaction diagram
additional information
?
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the multifunctional enzyme is involved in biosynthesis of UDP-N-acetyl-alpha-D-glucosamine, an activated and essential form of N-acetyl-alpha-D-glucosamine that is an important component in the polysaccharide structure of most organisms
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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
dTTP + alpha-D-glucose 1-phosphate
diphosphate + dTDP-alpha-D-glucose
show the reaction diagram
-
the enzyme is involved in biosynthesis of L-rhamnose
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?
additional information
?
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the multifunctional enzyme is involved in biosynthesis of UDP-N-acetyl-alpha-D-glucosamine, an activated and essential form of N-acetyl-alpha-D-glucosamine that is an important component in the polysaccharide structure of most organisms
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.12
alpha-D-glucose 1-phosphate
0.39
diphosphate
0.05
dTDP-alpha-D-glucose
0.02
dTTP
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1.35
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pH 7.5, 80°C, substrates: dTTP + alpha-D-glucose 1-phosphate
9.4
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pH 7.5, 80°C, substrates: diphosphate + dTDP-alpha-D-glucose
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 10
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pH 6.0: about 50% of maximal activity, pH 10.0: about 60% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
70 - 100
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70°C: about 40% of maximal activity, 100°C: about 80% of maximal activity
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
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the multifunctional enzyme is involved in biosynthesis of UDP-N-acetyl-alpha-D-glucosamine, an activated and essential form of N-acetyl-alpha-D-glucosamine that is an important component in the polysaccharide structure of most organisms
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D208A
D99A
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very low Glc-1-P TTase activity
E146A
K147A
K23A
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very low Glc-1-P TTase activity
T80L
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very low Glc-1-P TTase activity
Y97F
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UDP-N-acetylglucosamine diphosphorylase activity is very low
additional information
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
80
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half-life: 180 min
95
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half-life: 60 min
PURIFICATION/commentary
ORGANISM
UNIPROT
LITERATURE
CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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expression in Escherichia coli BL21-Codon Plus (DE3)-RIL cells
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expression in Escherichia coli, wild-type and truncated enzyme form lacking the 170-residues C-terminal domain
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Zhang, Z.; Tsujimura, M.; Akutsu, J.; Sasaki, M.; Tajima, H.; Kawarabayasi, Y.
Identification of an extremely thermostable enzyme with dual sugar-1-phosphate nucleotidylyltransferase activities from an acidothermophilic archaeon, Sulfolobus tokodaii strain 7
J. Biol. Chem.
280
9698-9705
2005
Sulfurisphaera tokodaii (Q975F9), Sulfurisphaera tokodaii 7 (Q975F9)
Manually annotated by BRENDA team
Zhang, Z.; Akutsu, J.; Tsujimura, M.; Kawarabayasi, Y.
Increasing in archaeal GlcNAc-1-P uridyltransferase activity by targeted mutagenesis while retaining its extreme thermostability
J. Biochem.
141
553-562
2007
Sulfurisphaera tokodaii (Q975F9), Sulfurisphaera tokodaii 7 (Q975F9)
Manually annotated by BRENDA team
Zhang, Z.; Akutsu, J.; Tsujimura, M.; Kawarabayasi, Y.
Increasing in archaeal GlcNAc-1-P uridyltransferase activity by targeted mutagenesis while retaining its extreme thermostability
J. Biochem.
141
553-562
2007
Sulfurisphaera tokodaii (Q975F9), Sulfurisphaera tokodaii DSM 16993 (Q975F9)
Manually annotated by BRENDA team
Zhang, Z.; Tsujimura, M.; Akutsu, J.; Sasaki, M.; Tajima, H.; Kawarabayasi, Y.
Identification of an extremely thermostable enzyme with dual sugar-1-phosphate nucleotidylyltransferase activities from an acidothermophilic archaeon, Sulfolobus tokodaii strain 7
J. Biol. Chem.
280
9698-9705
2005
Sulfurisphaera tokodaii (Q975F9), Sulfurisphaera tokodaii DSM 16993 (Q975F9)
Manually annotated by BRENDA team
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