Crystallization (Comment) | Organism |
---|---|
crystals of K226M and K226Q mutant enzymes and of the complex of mutant enzyme K226Q with Gly or mutant enzyme K226M with Ser. Crystals are obtained by mixing 0.004 ml of protein solution 0.375 mM with 0.004 mM of reservoir solution containing 100 mM Hepes buffer, pH 7.5, 0.2 mM EDTA, 5 mM 2-mercaptoethanol, and 50% 2-methyl-2,4-pentanediol | Geobacillus stearothermophilus |
Protein Variants | Comment | Organism |
---|---|---|
K226M | mutant enzymes is inactive, drastic rate of formation of the quinoid intermediate. It contains 1 mol of pyridoxal 5'-phosphate per mol of subunit. pyridoxal 5'-phosphate is bound at the active site in an orientation different from that of the wild-type enzyme. K-226 is responsible for flipping of pyridoxal 5'-phosphate from one orientation to another which is crucial for tetrahydropteroylglutamate-dependent Calpha-Cbeta bond cleavage of L-Ser | Geobacillus stearothermophilus |
K226Q | mutant enzymes is inactive, drastic rate of formation of the quinoid intermediate. It contains 1 mol of pyridoxal 5'-phosphate oer mol of subunit. pyridoxal 5'-phosphate is bound at the active site in an orientation different from that of the wild-type enzyme. K-226 is responsible for flipping of pyridoxal 5'-phosphate from one orientation to another which is crucial for tetrahydropteroylglutamate-dependent Calpha-Cbeta bond cleavage of L-Ser | Geobacillus stearothermophilus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Geobacillus stearothermophilus | - |
- |
- |
Purification (Comment) | Organism |
---|---|
- |
Geobacillus stearothermophilus |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-Ser + tetrahydrofolate | - |
Geobacillus stearothermophilus | Gly + 5,10-methylenetetrahydrofolate | - |
? |
Synonyms | Comment | Organism |
---|---|---|
SHMT | - |
Geobacillus stearothermophilus |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
pyridoxal 5'-phosphate | mutant enzymes K226M and K226Q contain 1 mol of pyridoxal 5'-phosphate per mol of subunit. Pyridoxal 5'-phosphate is bound at the active site in an orientation different from that of the wild-type enzyme. K226 is responsible for flipping of pyridoxal 5'-phosphate from one orientation to another which is crucial for tetrahydropteroylglutamate-dependent Calpha-Cbeta bond cleavage of L-Ser | Geobacillus stearothermophilus |