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Results 1 - 6 of 6
EC Number Subunits Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 2.7.7.83? x * 57000, SDS-PAGE 643069
Display the word mapDisplay the reaction diagram Show all sequences 2.7.7.83? x * 64000, SDS-PAGE 643069
Display the word mapDisplay the reaction diagram Show all sequences 2.7.7.83homodimer 2 * 74000, gel filtration 722110
Display the word mapDisplay the reaction diagram Show all sequences 2.7.7.83monomer 74000, gel filtration 722110
Display the word mapDisplay the reaction diagram Show all sequences 2.7.7.83More the enzyme contains the the N-terminal nucleotidylyltransferase domain (residues 1–210) and the C-terminal acetyltransferase domain (residues 211–401), respectively. Comparisons of the crystal structures of the ST0452 protein, PDB ID GGO, and Escherichia coli protein EcGlmU2, PDB ID 2OI5, comparison with ST0452 mutant enzymes, overview. Despite the structural similarities between the N- and C-termini of the ST0452 protein and those of Escherichia coli EcGlmU, the thermostabilities of the two proteins differ greatly, as EcGlmU is a mesophilic enzyme. The structures of these proteins do not correlate directly with their thermostability 729696
Display the word mapDisplay the reaction diagram Show all sequences 2.7.7.83trimer the C-terminal domain of the ST0452 protein, with its LbetaH structure, appears to be essential for the formation of its trimeric form and, in turn, the high stability of the entire ST0452 protein 729696
Results 1 - 6 of 6