Cloned (Comment) | Organism |
---|---|
- |
Geobacillus stearothermophilus |
Crystallization (Comment) | Organism |
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in complex with phosphate.The phosphate-binding site is formed by the side chain of Arg13, the backbone amides of the phosphate-loop and the positive end of the macrodipole of helix H1, which together generate a highly positively charged pocket at the bottom of the substrate-binding cleft. The substrate-mimicking Arg149 is sandwiched between Thr11, Asp118, and Phe120 with its guanidinium group hydrogen bonding to Asp118. Structure of mutant C7S in complex with phosphate shows the formation of a covalent phospho-Ser7 adduct indicating that the crystallized mutant mimics the phospho-enzyme intermediate of the dephosphorylation reaction | Geobacillus stearothermophilus |
Protein Variants | Comment | Organism |
---|---|---|
C7S | structure in complex with phosphate shows the formation of a covalent phospho-Ser7 adduct indicating that the crystallized mutant mimics the phospho-enzyme intermediate of the dephosphorylation reaction | Geobacillus stearothermophilus |
D118A | complete loss of activity | Geobacillus stearothermophilus |
F120A | 60fold reduction of specific activity | Geobacillus stearothermophilus |
T11I | 18fold reduction of specific activity with phospho-arginine substrates, marked increasing in the activity toward phospho-tyrosine substrates | Geobacillus stearothermophilus |
T11V | 18fold reduction of specific activity with phospho-arginine substrates, marked increasing in the activity toward phospho-tyrosine substrates | Geobacillus stearothermophilus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Geobacillus stearothermophilus | S0F332 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
KpRGGGGYIKIIKV + H2O | hydrolysis of the phosphoramidate bond of phospho-arginine residues in peptides | Geobacillus stearothermophilus | KRGGGGYIKIIKV + phosphate | - |
? |