Cloned (Comment) | Organism |
---|---|
gene ST0452, recombinant expression of C-terminally His6-tagged wild-type and mutant enzymes in Escherichia coli strain BL21-Codon Plus(DE3)-RIL | Sulfurisphaera tokodaii |
Protein Variants | Comment | Organism |
---|---|---|
H308A | site-directed mutagenesis | Sulfurisphaera tokodaii |
K337A | site-directed mutagenesis | Sulfurisphaera tokodaii |
K340A | site-directed mutagenesis | Sulfurisphaera tokodaii |
additional information | construction of expression vectors encoding a series of ST0452 C-terminal deletion mutants with hexahistidine tags at their C-termini, designated pST0452(DC005)H, pST0452(DC011)H, pST0452(DC021)H, pST0452(DC031)H, pST0452(DC041) H, pST0452(DC051)H, pST0452(DC071)H, pST0452 (DC121)H and pST0452(DC171)H. The deletion mutants retain the same tertiary structures as the wild-type ST0452 protein | Sulfurisphaera tokodaii |
N331A | site-directed mutagenesis | Sulfurisphaera tokodaii |
Y311A | site-directed mutagenesis | Sulfurisphaera tokodaii |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | required | Sulfurisphaera tokodaii |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
NDP + alpha-D-aldose 1-phosphate | Sulfurisphaera tokodaii | - |
phosphate + NDP-aldose | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Sulfurisphaera tokodaii | Q975F9 | - |
- |
Sulfurisphaera tokodaii DSM 16993 / JCM 10545 / NBRC 100140 / 7 | Q975F9 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | the enzyme has multiple sugar-1-phosphate nucleotidylyltransferase, EC 2.7.7.37, and amino-sugar-1-phosphate acetyltransferase, EC 2.3.1.157, activities, overview. In addition to glucosamine-1-phosphate acetyltransferase activity, it possesses unique galactosamine-1-phosphate acetyltransferase activity, EC 2.7.7.83. Also, the enzyme possesses GlcNAc-1-phosphate nucleotidylyltransferase and N-acetyl-D-galactosamine-1-phosphate uridyltransferase, EC 2.7.7.23, activities, as well as the expected glucose-1-phosphate thymidylyltransferase, EC 2.7.7.24, activity | Sulfurisphaera tokodaii | ? | - |
? | |
NDP + alpha-D-aldose 1-phosphate | - |
Sulfurisphaera tokodaii | phosphate + NDP-aldose | - |
? |
Subunits | Comment | Organism |
---|---|---|
More | the enzyme contains the the N-terminal nucleotidylyltransferase domain (residues 1210) and the C-terminal acetyltransferase domain (residues 211401), 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 | Sulfurisphaera tokodaii |
trimer | 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 | Sulfurisphaera tokodaii |
Synonyms | Comment | Organism |
---|---|---|
dual sugar-1-phosphate nucleotidylyltransferase | UniProt | Sulfurisphaera tokodaii |
multiple sugar-1-phosphate nucleotidylyltransferase | - |
Sulfurisphaera tokodaii |
ST0452 | - |
Sulfurisphaera tokodaii |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
80 | - |
assay at | Sulfurisphaera tokodaii |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.5 | - |
assay at | Sulfurisphaera tokodaii |
General Information | Comment | Organism |
---|---|---|
additional information | the ST0452 protein contains only two Cys residues, it is unlikely that CysCys bonds contribute to its thermostability | Sulfurisphaera tokodaii |