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Q83N
Salmonella enterica typhimurium LT2
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0.3% relative activity compared to the wild type enzyme, using dTTP as a substrate
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R313S/T317V/H322A/A339S/S341H/D348H
D99A
very low Glc-1-P TTase activity
K23A
very low Glc-1-P TTase activity
T80L
very low Glc-1-P TTase activity
Y97F
UDP-N-acetylglucosamine diphosphorylase activity is very low
Q83A
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0.2% relative activity compared to the wild type enzyme, using dTTP as a substrate
Q83A
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reduced activity with dTTP and increased activity with dATP and ATP compared to the wild type enzyme
Q83D
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0.2% relative activity compared to the wild type enzyme, using dTTP as a substrate
Q83D
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reduced activity with dTTP and increased activity with dGTP and GTP compared to the wild type enzyme
Q83E
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1.0% relative activity compared to the wild type enzyme, using dTTP as a substrate
Q83E
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wild type activity with dTTP
Q83N
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0.3% relative activity compared to the wild type enzyme, using dTTP as a substrate
Q83N
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reduced activity with dTTP and increased activity with dATP and ATP compared to the wild type enzyme
Q83S
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0.3% relative activity compared to the wild type enzyme, using dTTP as a substrate
Q83S
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reduced activity with dTTP and increased activity with dATP and ATP compared to the wild type enzyme
Q83D
Salmonella enterica typhimurium LT2
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0.2% relative activity compared to the wild type enzyme, using dTTP as a substrate
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Q83D
Salmonella enterica typhimurium LT2
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reduced activity with dTTP and increased activity with dGTP and GTP compared to the wild type enzyme
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Q83S
Salmonella enterica typhimurium LT2
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0.3% relative activity compared to the wild type enzyme, using dTTP as a substrate
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Q83S
Salmonella enterica typhimurium LT2
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reduced activity with dTTP and increased activity with dATP and ATP compared to the wild type enzyme
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R313S/T317V/H322A/A339S/S341H/D348H
mutation of residues to the corresponing residues of isoform RmbA, giving rise to highly similar hydrophobicity pattern with RmbA. Mutations render the protein expressed in soluble form, the mutant is catalytically active
R313S/T317V/H322A/A339S/S341H/D348H
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mutation of residues to the corresponing residues of isoform RmbA, giving rise to highly similar hydrophobicity pattern with RmbA. Mutations render the protein expressed in soluble form, the mutant is catalytically active
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D208A
UDP-N-acetylglucosamine diphosphorylase activity is very low
D208A
very low Glc-1-P TTase activity
E146A
UDP-N-acetylglucosamine diphosphorylase activity is very low
E146A
very low Glc-1-P TTase activity
G9A
UDP-N-acetylglucosamine diphosphorylase activity is very low
G9A
very low Glc-1-P TTase activity
K147A
UDP-N-acetylglucosamine diphosphorylase activity is very low
K147A
very low Glc-1-P TTase activity
R13A
UDP-N-acetylglucosamine diphosphorylase activity is very low
R13A
very low Glc-1-P TTase activity
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
Y97A
very low Glc-1-P TTase activity
additional information
deletion of the C-terminal sequence of isoform DnmL increases the expression level of truncated DnmL, albeit without enzymic activity. Substitution of the C-terminal sequence of DnmL with that of isoform RmbA also leads to expression of the recombinant protein in soluble form. The fusion protein is catalytically active
additional information
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deletion of the C-terminal sequence of isoform DnmL increases the expression level of truncated DnmL, albeit without enzymic activity. Substitution of the C-terminal sequence of DnmL with that of isoform RmbA also leads to expression of the recombinant protein in soluble form. The fusion protein is catalytically active
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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
additional information
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a truncated enzyme form lacking the 170-residues C-terminal domain has decreased thermostability
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additional information
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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
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