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Information on EC 2.7.7.24 - glucose-1-phosphate thymidylyltransferase and Organism(s) Sulfurisphaera tokodaii and UniProt Accession Q975F9
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2.7.7.24 glucose-1-phosphate thymidylyltransferaseIUBMB Comments
Involved in the biosynthesis of L-rhamnose in bacteria.
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Word Map
- 2.7.7.24
- l-rhamnose
- dtdp-l-rhamnose
-
4,6-dehydratase
-
deoxysugars
-
uridylyltransferase
- dtdp-4-keto-6-deoxy-d-glucose
-
3,5-epimerase
-
deoxyhexose
- dtmp
- analysis
- medicine
The taxonomic range for the selected organisms is: Sulfurisphaera tokodaii
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
glucose-1-phosphate thymidylyltransferase, dtdp-glucose synthase, cps2l, sgca1, glc-1-p-tt, sugar-1-phosphate nucleotidyltransferase, dtdp-d-glucose synthase, d-glucose-1-phosphate thymidylyltransferase, rml-1, cps23fl, 
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topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ST0452
dTDP-glucose synthase
-
-
-
-
dTDP-glucose-pyrophosphorylase
-
-
-
-
dTDPglucose pyrophosphorylase
-
-
-
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glucose 1-phosphate thymidylyltransferase
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-
-
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TDP-glucose pyrophosphorylase
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-
-
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thymidine diphosphate glucose pyrophosphorylase
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-
-
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thymidine diphosphoglucose pyrophosphorylase
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-
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thymidylyltransferase, glucose 1-phosphate
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
nucleotidyl group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
KEGG
-
-, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
dTTP:alpha-D-glucose-1-phosphate thymidylyltransferase
Involved in the biosynthesis of L-rhamnose in bacteria.
CAS REGISTRY NUMBER
COMMENTARY
9026-03-3
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
diphosphate + dTDP-alpha-D-glucose
dTTP + alpha-D-glucose 1-phosphate
-
-
-
r
additional information
?
-
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
-
-
?
dTTP + alpha-D-glucose 1-phosphate
diphosphate + dTDP-alpha-D-glucose
-
-
-
?
dTTP + alpha-D-glucose 1-phosphate
diphosphate + dTDP-alpha-D-glucose
-
-
-
r
dTTP + alpha-D-glucose 1-phosphate
diphosphate + dTDP-alpha-D-glucose
maximal velocity of the reverse reaction is 11.4fold of the maximal velocity of the forward reaction. The multifunctional enzyme also shows activity with UTP + alpha-D-glucose 1-phosphate (EC 2.7.7.9, UTP-glucose-1-phosphate uridylyltransferase), UTP + N-acetylglucosamine 1-phosphate (EC 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase), dTTP + N-acetylglucosamine 1-phosphate (N-acetylglucosamine 1-phosphate thymidylyltransferase), dCTP + alpha-D-glucose 1-phosphate (glucose-1-phosphate cytidylyltransferase), dGTP + alpha-D-glucose 1-phosphate (glucose-1-phosphate guanylyltransferase), dATP + alpha-D-glucose 1-phosphate (glucose-1-phosphate adenylyltransferase). No activity with: alpha-D-glucose 1-phosphate + dATP, alpha-D-glucose 1-phosphate + dCTP, alpha-D-glucose 1-phosphate + dGTP, UTP + alpha-D-mannose1-phosphate, UTP + alpha-D-galactose 1-phosphate, UTP + alpha-D-glucosamine 1-phosphate
-
-
r
dTTP + alpha-D-glucose 1-phosphate
diphosphate + dTDP-alpha-D-glucose
the enzyme also shows activity of EC 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase
-
-
?
dTTP + alpha-D-glucose 1-phosphate
diphosphate + dTDP-alpha-D-glucose
the enzyme is involved in biosynthesis of L-rhamnose
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
dTTP + alpha-D-glucose 1-phosphate
diphosphate + dTDP-alpha-D-glucose
the enzyme is involved in biosynthesis of L-rhamnose
-
-
?
additional information
?
-
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
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Co2+
Mg2+
Mn2+
Zn2+
Ca2+
2 mM. Activation of UDP-N-acetylglucosamine diphosphorylase activity in the order of decreasing effectiveness: Co2+, Mn2+, Mg2+, Zn2+, Ca2+. No activity is detectable without a divalent cation
Ca2+
no activity is detectable when a divalent cation is removed from the reaction buffer. The order of effectiveness of metal ions on GlcNAc-1-P UTase activity is Mg2+ > Zn2+ > Ca2+ > Co2+ > Mn2+, which is different from that of its Glc-1-P TTase activity, Co2+ > Mn2+ > Mg2+ > Zn2+ > Ca2+
Co2+
absolute requirement for divalent cation. Order of decreasing effectiveness is: Co2+, Mn2+, Mg2+, Zn2+
Co2+
2 mM. Activation of UDP-N-acetylglucosamine diphosphorylase activity in the order of decreasing effectiveness: Co2+, Mn2+, Mg2+, Zn2+, Ca2+. No activity is detectable without a divalent cation
Co2+
absolute requirement for a divalent cation. The order of effectiveness of metal ions on the activity of the enzyme is Co2+, Mn2+, Mg2+ and Zn2+
Co2+
no activity is detectable when a divalent cation is removed from the reaction buffer. The order of effectiveness of metal ions on GlcNAc-1-P UTase activity is Mg2+ > Zn2+ > Ca2+ > Co2+ > Mn2+, which is different from that of its Glc-1-P TTase activity, Co2+ > Mn2+ > Mg2+ > Zn2+ > Ca2+
Mg2+
absolute requirement for divalent cation. Order of decreasing effectiveness is: Co2+, Mn2+, Mg2+, Zn2+. Optimal Mg2+ concentration is 6 mM
Mg2+
2 mM. Activation of UDP-N-acetylglucosamine diphosphorylase activity in the order of decreasing effectiveness: Co2+, Mn2+, Mg2+, Zn2+, Ca2+. No activity is detectable without a divalent cation
Mg2+
absolute requirement for a divalent cation. The order of effectiveness of metal ions on the activity of the enzyme is Co2+, Mn2+, Mg2+ and Zn2+. The optimal Mg2+ concentration is 6 mM, but the enzymatic activity does not change substantially between 2 and 12 mM
Mg2+
no activity is detectable when a divalent cation is removed from the reaction buffer. The order of effectiveness of metal ions on GlcNAc-1-P UTase activity is Mg2+ > Zn2+ > Ca2+ > Co2+ > Mn2+, which is different from that of its Glc-1-P TTase activity, Co2+ > Mn2+ > Mg2+ > Zn2+ > Ca2+
Mn2+
absolute requirement for divalent cation. Order of decreasing effectiveness is: Co2+, Mn2+, Mg2+, Zn2+
Mn2+
2 mM. Activation of UDP-N-acetylglucosamine diphosphorylase activity in the order of decreasing effectiveness: Co2+, Mn2+, Mg2+, Zn2+, Ca2+. No activity is detectable without a divalent cation
Mn2+
absolute requirement for a divalent cation. The order of effectiveness of metal ions on the activity of the enzyme is Co2+, Mn2+, Mg2+ and Zn2+
Mn2+
no activity is detectable when a divalent cation is removed from the reaction buffer. The order of effectiveness of metal ions on GlcNAc-1-P UTase activity is Mg2+ > Zn2+ > Ca2+ > Co2+ > Mn2+, which is different from that of its Glc-1-P TTase activity, Co2+ > Mn2+ > Mg2+ > Zn2+ > Ca2+
Zn2+
absolute requirement for divalent cation. Order of decreasing effectiveness is: Co2+, Mn2+, Mg2+, Zn2+
Zn2+
2 mM. Activation of UDP-N-acetylglucosamine diphosphorylase activity in the order of decreasing effectiveness: Co2+, Mn2+, Mg2+, Zn2+, Ca2+. No activity is detectable without a divalent cation
Zn2+
absolute requirement for a divalent cation. The order of effectiveness of metal ions on the activity of the enzyme is Co2+, Mn2+, Mg2+ and Zn2+
Zn2+
no activity is detectable when a divalent cation is removed from the reaction buffer. The order of effectiveness of metal ions on GlcNAc-1-P UTase activity is Mg2+ > Zn2+ > Ca2+ > Co2+ > Mn2+, which is different from that of its Glc-1-P TTase activity, Co2+ > Mn2+ > Mg2+ > Zn2+ > Ca2+
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
1.35
pH 7.5, 80°C, substrates: dTTP + alpha-D-glucose 1-phosphate
9.4
pH 7.5, 80°C, substrates: diphosphate + dTDP-alpha-D-glucose
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 10
pH 6.0: about 50% of maximal activity, pH 10.0: about 60% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
70 - 100
70°C: about 40% of maximal activity, 100°C: about 80% of maximal activity
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
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
PDB
SCOP
CATH
UNIPROT
ORGANISM
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D208A
E146A
G9A
K147A
R13A
T80A
Y97A
Y97F
UDP-N-acetylglucosamine diphosphorylase activity is very low
additional information
D208A
UDP-N-acetylglucosamine diphosphorylase activity is very low
E146A
UDP-N-acetylglucosamine diphosphorylase activity is very low
G9A
UDP-N-acetylglucosamine diphosphorylase activity is very low
K147A
UDP-N-acetylglucosamine diphosphorylase activity is very low
R13A
UDP-N-acetylglucosamine diphosphorylase activity is very low
T80A
enhanced UDP-N-acetylglucosamine diphosphorylase activity under optimal conditions
T80A
Glc-1-P TTase activity is about 1.5fold higher than that of wild-type ST0452 protein
Y97A
enhanced UDP-N-acetylglucosamine diphosphorylase activity under optimal conditions
Y97A
Glc-1-P TTase activity is about 2.2fold higher than that of wild-type ST0452 protein
additional information
a truncated enzyme form lacking the 170-residues C-terminal domain has decreased thermostability
additional information
analysis of a deletion mutant lacking the 170-residue C-terminal domain indicated that this region has an important role in the thermostability and activity of the protein. Specific initial velocity (glucose-1-phosphate thymidylyltransferase activity) is 23 times lower than that of the native enzyme when measured at 37°C
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli BL21-Codon Plus (DE3)-RIL cells
expression in Escherichia coli, wild-type and truncated enzyme form lacking the 170-residues C-terminal domain
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)
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)
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)
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)
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