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Literature summary for 2.1.2.1 extracted from
- Overexpression of serine hydroxymethyltransferase from halotolerant cyanobacterium in Escherichia coli results in increased accumulation of choline precursors and enhanced salinity tolerance (2012), FEMS Microbiol. Lett., 333, 46-53.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| DNA and amino acid sequence determination and analysis, overexpression in Escherichia coli resulting in the increased accumulation of glycine and L-serine. Choline and glycine betaine levels are also significantly increased. Under high salinity, the growth rate of ApSHMT-expressing cells is faster compared to its respective control | Aphanothece halophytica |
General Stability
| General Stability | Organism |
|---|---|
| glycine betaine protects the ApSHMT enzyme activity in vitro | Aphanothece halophytica |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| NaCl | 60% inhibition at 100 mM, restored to 66-71% activity in presence of 50 mM glycine betaine | Aphanothece halophytica |  |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 5,10-methylenetetrahydrofolate + glycine + H2O | Aphanothece halophytica | - |
tetrahydrofolate + L-serine | - |
r | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Aphanothece halophytica | I7H6W6 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant enzyme from Escherichia coli | Aphanothece halophytica |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 5,10-methylenetetrahydrofolate + glycine + H2O | - |
Aphanothece halophytica | tetrahydrofolate + L-serine | - |
r | |
| additional information | purified recombinant ApSHMT protein exhibits catalytic reactions for DL-threo-3-phenylserine as well as for L-serine | Aphanothece halophytica | ? | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| serine hydroxymethyltransferase | - |
Aphanothece halophytica |
| SHMT | - |
Aphanothece halophytica |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 25 | - |
assay at | Aphanothece halophytica |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 9 | - |
assay at | Aphanothece halophytica |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| pyridoxal 5'-phosphate | dependent on | Aphanothece halophytica | |
Expression
| Organism | Comment | Expression |
|---|---|---|
| Aphanothece halophytica | high salinity also strongly induces the transcript level of ApSHMT in Aphanothece halophytica | up |
General Information
| General Information | Comment | Organism |
|---|---|---|
| additional information | amino acid residues important for the structure and function of SHMT are Y56, D202, and K231 for the interaction with pyridoxal 5'-phosphate, R64 and D73 for inter-subunit interaction, H127 for cofactor binding, and P258 and R363 for substrate interaction | Aphanothece halophytica |
| physiological function | salt-induced ApSHMT increases the level of glycine betaine via L-serine and choline and confers tolerance to salinity stress | Aphanothece halophytica |
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