Application | Comment | Organism |
---|---|---|
synthesis | improved method for preparation of optically pure beta-hydroxy-alpha-amino acids, catalyzed by serine hydroxymethyl transferase with threonine aldolase activity. Usage of substrates beta-phenylserine, beta-(nitrophenyl) serine and beta-(methylsulfonylphenyl) serine with immobilized recombinant enzyme for SHMT activity, optimal at pH 7.5 and 45°C. The immobilized cells are continuously used 10 times, yielding an average conversion rate of 60.4% | Escherichia coli |
Cloned (Comment) | Organism |
---|---|
expression in Escherichia coli strain BL21 (DE3) | Escherichia coli |
Protein Variants | Comment | Organism |
---|---|---|
additional information | immobilization of cells using 3% alginate (w/v), 5 g cells (wet), and 2% (w/v) CaCl2 solution | Escherichia coli |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |
Escherichia coli K-12 MG1655 | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | SHMT activity with beta-phenylserine as substrate is about 1.48fold and 1.25fold higher than that with beta-(methylsulfonylphenyl) serine and beta-(nitrophenyl) serine as substrate, respectively. Besides SHMT activity, the enzyme also shows L-allo-threonine aldolase activity, EC 4.1.2.48 | Escherichia coli | ? | - |
? | |
additional information | SHMT activity with beta-phenylserine as substrate is about 1.48fold and 1.25fold higher than that with beta-(methylsulfonylphenyl) serine and beta-(nitrophenyl) serine as substrate, respectively. Besides SHMT activity, the enzyme also shows L-allo-threonine aldolase activity, EC 4.1.2.48 | Escherichia coli K-12 MG1655 | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
serine hydroxymethyl transferase | - |
Escherichia coli |
SHMT | - |
Escherichia coli |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
45 | - |
- |
Escherichia coli |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.5 | - |
- |
Escherichia coli |
pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
4 | 10 | activity range | Escherichia coli |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
pyridoxal 5'-phosphate | dependent on | Escherichia coli |