EC Number | Cloned (Comment) | Organism |
---|---|---|
4.1.2.48 | overexpression in Escherichia coli | Pseudomonas sp. |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
4.1.2.48 | K207A | the mutant enzyme shows no detectable enzyme activity. The mutant enzyme show the disappearance of the absorption maximum at 420 nm, indicating that the Schiff base linkage between the epsilon-amino group of the active-site lysine residue and the pyridoxal 5'-phosphate cofactor aldehyde group of the wild type is not present in the mutant enzyme | Pseudomonas sp. |
4.1.2.48 | K207R | the mutant enzyme shows a specific activity of about 1000 times lower than that of the wild-type enzyme. The mutant enzyme show the disappearance of the absorption maximum at 420 nm, indicating that the Schiff base linkage between the epsilon-amino group of the active-site lysine residue and the pyridoxal 5'-phosphate cofactor aldehyde group of the wild type is not present in the mutant enzyme | Pseudomonas sp. |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
4.1.2.48 | 7.3 | - |
L-threo-phenylserine | pH 8.0, 30°C | Pseudomonas sp. | |
4.1.2.48 | 7.4 | - |
L-threo-beta-3,4-methylenedioxyphenylserine | pH 8.0, 30°C | Pseudomonas sp. | |
4.1.2.48 | 8.3 | - |
L-threo-beta-3,4-dihydroxyphenylserine | pH 8.0, 30°C | Pseudomonas sp. | |
4.1.2.48 | 10.2 | - |
L-erythro-phenylserine | pH 8.0, 30°C | Pseudomonas sp. | |
4.1.2.48 | 14.6 | - |
L-allo-threonine | pH 8.0, 30°C | Pseudomonas sp. | |
4.1.2.48 | 14.7 | - |
L-threonine | pH 8.0, 30°C | Pseudomonas sp. |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
4.1.2.48 | 38000 | - |
4 * 38000, SDS-PAGE | Pseudomonas sp. |
4.1.2.48 | 145000 | - |
gel filtration | Pseudomonas sp. |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.1.2.1 | L-serine + tetrahydrofolate | Escherichia coli | catalyzes interconversion of serine and glycine | glycine + 5,10-methylenetetrahydrofolate + H2O | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
2.1.2.1 | Escherichia coli | - |
- |
- |
4.1.2.48 | Pseudomonas sp. | O50584 | - |
- |
4.1.2.48 | Pseudomonas sp. NCIMB 10558 | O50584 | - |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
4.1.2.48 | - |
Pseudomonas sp. |
EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|---|
4.1.2.48 | 41 | - |
pH 8.0, 30°C | Pseudomonas sp. |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.1.2.1 | L-serine + tetrahydrofolate | - |
Escherichia coli | glycine + 5,10-methylenetetrahydrofolate + H2O | - |
? | |
2.1.2.1 | L-serine + tetrahydrofolate | catalyzes interconversion of serine and glycine | Escherichia coli | glycine + 5,10-methylenetetrahydrofolate + H2O | - |
? | |
4.1.2.48 | L-allo-threonine | - |
Pseudomonas sp. | glycine + acetaldehyde | - |
r | |
4.1.2.48 | L-allo-threonine | - |
Pseudomonas sp. NCIMB 10558 | glycine + acetaldehyde | - |
r | |
4.1.2.48 | L-erythro-phenylserine | - |
Pseudomonas sp. | glycine + benzaldehyde | - |
? | |
4.1.2.48 | L-erythro-phenylserine | - |
Pseudomonas sp. NCIMB 10558 | glycine + benzaldehyde | - |
? | |
4.1.2.48 | L-threo-beta-3,4-dihydroxyphenylserine | - |
Pseudomonas sp. | glycine + 3,4-dihydroxybenzaldehyde | - |
? | |
4.1.2.48 | L-threo-beta-3,4-dihydroxyphenylserine | - |
Pseudomonas sp. NCIMB 10558 | glycine + 3,4-dihydroxybenzaldehyde | - |
? | |
4.1.2.48 | L-threo-beta-3,4-methylenedioxyphenylserine | - |
Pseudomonas sp. | ? | - |
? | |
4.1.2.48 | L-threo-beta-3,4-methylenedioxyphenylserine | - |
Pseudomonas sp. NCIMB 10558 | ? | - |
? | |
4.1.2.48 | L-threo-phenylserine | - |
Pseudomonas sp. | glycine + benzaldehyde | - |
? | |
4.1.2.48 | L-threonine | - |
Pseudomonas sp. | glycine + acetaldehyde | - |
r | |
4.1.2.48 | L-threonine | - |
Pseudomonas sp. NCIMB 10558 | glycine + acetaldehyde | - |
r |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
4.1.2.48 | tetramer | 4 * 38000, SDS-PAGE | Pseudomonas sp. |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
4.1.2.48 | L-TA | - |
Pseudomonas sp. |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
4.1.2.48 | 25 | - |
- |
Pseudomonas sp. |
4.1.2.48 | 30 | - |
assay at | Pseudomonas sp. |
EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|---|
4.1.2.48 | 25 | - |
40°C, 15 min, 50% loss of activity | Pseudomonas sp. |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
4.1.2.48 | 8 | - |
assay at | Pseudomonas sp. |
4.1.2.48 | 8 | 8.5 | - |
Pseudomonas sp. |
EC Number | pH Stability | pH Stability Maximum | Comment | Organism |
---|---|---|---|---|
4.1.2.48 | 5.5 | 9 | 30°C, 30 min, stable | Pseudomonas sp. |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
4.1.2.48 | pyridoxal 5'-phosphate | contains 1 mol of pyridoxal 5'-phosphate per mol of 38000 da subunit. Lys207 probably functions as an essential catalytic residue, forming an internal Schiff base with the pyridoxal 5'-phosphate of the enzyme to catalyze the reversible aldol reaction | Pseudomonas sp. |