Literature summary extracted from
Waditee-Sirisattha, R.; Sittipol, D.; Tanaka, Y.; Takabe, T.
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)
EC Number |
Cloned (Comment) |
Organism |
---|
2.1.2.1 |
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
EC Number |
General Stability |
Organism |
---|
2.1.2.1 |
glycine betaine protects the ApSHMT enzyme activity in vitro |
Aphanothece halophytica |
Inhibitors
EC Number |
Inhibitors |
Comment |
Organism |
Structure |
---|
2.1.2.1 |
NaCl |
60% inhibition at 100 mM, restored to 66-71% activity in presence of 50 mM glycine betaine |
Aphanothece halophytica |
|
Natural Substrates/ Products (Substrates)
EC Number |
Natural Substrates |
Organism |
Comment (Nat. Sub.) |
Natural Products |
Comment (Nat. Pro.) |
Rev. |
Reac. |
---|
2.1.2.1 |
5,10-methylenetetrahydrofolate + glycine + H2O |
Aphanothece halophytica |
- |
tetrahydrofolate + L-serine |
- |
r |
|
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
2.1.2.1 |
Aphanothece halophytica |
I7H6W6 |
- |
- |
Purification (Commentary)
EC Number |
Purification (Comment) |
Organism |
---|
2.1.2.1 |
recombinant enzyme from Escherichia coli |
Aphanothece halophytica |
Substrates and Products (Substrate)
EC Number |
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
---|
2.1.2.1 |
5,10-methylenetetrahydrofolate + glycine + H2O |
- |
Aphanothece halophytica |
tetrahydrofolate + L-serine |
- |
r |
|
2.1.2.1 |
additional information |
purified recombinant ApSHMT protein exhibits catalytic reactions for DL-threo-3-phenylserine as well as for L-serine |
Aphanothece halophytica |
? |
- |
? |
|
Synonyms
EC Number |
Synonyms |
Comment |
Organism |
---|
2.1.2.1 |
serine hydroxymethyltransferase |
- |
Aphanothece halophytica |
2.1.2.1 |
SHMT |
- |
Aphanothece halophytica |
Temperature Optimum [°C]
EC Number |
Temperature Optimum [°C] |
Temperature Optimum Maximum [°C] |
Comment |
Organism |
---|
2.1.2.1 |
25 |
- |
assay at |
Aphanothece halophytica |
pH Optimum
EC Number |
pH Optimum Minimum |
pH Optimum Maximum |
Comment |
Organism |
---|
2.1.2.1 |
9 |
- |
assay at |
Aphanothece halophytica |
Cofactor
EC Number |
Cofactor |
Comment |
Organism |
Structure |
---|
2.1.2.1 |
pyridoxal 5'-phosphate |
dependent on |
Aphanothece halophytica |
|
Expression
EC Number |
Organism |
Comment |
Expression |
---|
2.1.2.1 |
Aphanothece halophytica |
high salinity also strongly induces the transcript level of ApSHMT in Aphanothece halophytica |
up |
General Information
EC Number |
General Information |
Comment |
Organism |
---|
2.1.2.1 |
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 |
2.1.2.1 |
physiological function |
salt-induced ApSHMT increases the level of glycine betaine via L-serine and choline and confers tolerance to salinity stress |
Aphanothece halophytica |