Protein Variants | Comment | Organism |
---|---|---|
L276A | the mutation has the effect of lowering the cooperativity of urea denaturation process | Escherichia coli |
L785A/L276A | the mutation has the effect of lowering the cooperativity of urea denaturation process | Escherichia coli |
L85A | the mutation affect the quaternary structure stability of SHMT | Escherichia coli |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
Urea | in 1 M urea, almost all the cofactor is bound to the enzyme as internal aldimine, indicating that the loss of activity does not result from the denaturation of the active site, these observations suggest that urea might act as an enzyme inhibitor | Escherichia coli |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
91000 | - |
SDS-PAGE | Escherichia coli |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | P0A825 | - |
- |
Purification (Comment) | Organism |
---|---|
DEAE-Sepharose column chromatography and Phenyl-Sepharose column chromatography | Escherichia coli |
Renatured (Comment) | Organism |
---|---|
denatured SHMT samples (0.023 mM in 8 M urea at 20°C) are able to recover after 4 h when kept with 8 M urea in 50 mM Na-HEPES, pH 7.2, containing 0.2 mM dithiothreitol and 0.1 mM EDTA for 15 h at 20°C | Escherichia coli |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-serine + tetrahydrofolate | - |
Escherichia coli | glycine + 5,10-methylenetetrahydrofolate + H2O | - |
? |
Synonyms | Comment | Organism |
---|---|---|
serine hydroxymethyltransferase | - |
Escherichia coli |
SHMT | - |
Escherichia coli |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
pyridoxal 5'-phosphate | - |
Escherichia coli |