2.7.7.24	D208A	UDP-N-acetylglucosamine diphosphorylase activity is very low	725308	
2.7.7.24	D208A	very low Glc-1-P TTase activity	748123	
2.7.7.24	D99A	very low Glc-1-P TTase activity	748123	
2.7.7.24	E146A	UDP-N-acetylglucosamine diphosphorylase activity is very low	725308	
2.7.7.24	E146A	very low Glc-1-P TTase activity	748123	
2.7.7.24	G9A	UDP-N-acetylglucosamine diphosphorylase activity is very low	725308	
2.7.7.24	G9A	very low Glc-1-P TTase activity	748123	
2.7.7.24	K147A	UDP-N-acetylglucosamine diphosphorylase activity is very low	725308	
2.7.7.24	K147A	very low Glc-1-P TTase activity	748123	
2.7.7.24	K23A	very low Glc-1-P TTase activity	748123	
2.7.7.24	additional information	a truncated enzyme form lacking the 170-residues C-terminal domain has decreased thermostability	-, 662454	
2.7.7.24	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	-, 748158	
2.7.7.24	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	-, 723689	
2.7.7.24	Q83A	0.2% relative activity compared to the wild type enzyme, using dTTP as a substrate	674813	
2.7.7.24	Q83A	reduced activity with dTTP and increased activity with dATP and ATP compared to the wild type enzyme	674813	
2.7.7.24	Q83D	0.2% relative activity compared to the wild type enzyme, using dTTP as a substrate	-, 674813	
2.7.7.24	Q83D	reduced activity with dTTP and increased activity with dGTP and GTP compared to the wild type enzyme	-, 674813	
2.7.7.24	Q83E	1.0% relative activity compared to the wild type enzyme, using dTTP as a substrate	674813	
2.7.7.24	Q83E	wild type activity with dTTP	674813	
2.7.7.24	Q83N	0.3% relative activity compared to the wild type enzyme, using dTTP as a substrate	-, 674813	
2.7.7.24	Q83N	reduced activity with dTTP and increased activity with dATP and ATP compared to the wild type enzyme	674813	
2.7.7.24	Q83S	0.3% relative activity compared to the wild type enzyme, using dTTP as a substrate	-, 674813	
2.7.7.24	Q83S	reduced activity with dTTP and increased activity with dATP and ATP compared to the wild type enzyme	-, 674813	
2.7.7.24	R13A	UDP-N-acetylglucosamine diphosphorylase activity is very low	725308	
2.7.7.24	R13A	very low Glc-1-P TTase activity	748123	
2.7.7.24	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	-, 723689	
2.7.7.24	T80A	enhanced UDP-N-acetylglucosamine diphosphorylase activity under optimal conditions	725308	
2.7.7.24	T80A	Glc-1-P TTase activity is about 1.5fold higher than that of wild-type ST0452 protein	748123	
2.7.7.24	T80L	very low Glc-1-P TTase activity	748123	
2.7.7.24	Y97A	enhanced UDP-N-acetylglucosamine diphosphorylase activity under optimal conditions	725308	
2.7.7.24	Y97A	Glc-1-P TTase activity is about 2.2fold higher than that of wild-type ST0452 protein	748123	
2.7.7.24	Y97A	very low Glc-1-P TTase activity	748123	
2.7.7.24	Y97F	UDP-N-acetylglucosamine diphosphorylase activity is very low	725308