KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.027 | - |
L-4-hydroxythreonine | pH 8.0, 25°C | Escherichia coli | |
0.052 | - |
L-allo-threonine | pH 8.0, 25°C | Escherichia coli | |
4 | - |
L-threonine | pH 8.0, 25°C | Escherichia coli |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
glycine + glycolaldehyde | Escherichia coli | low-specificity L-threonine aldolase is involved in a serendipitous pathway that converts 3-phosphohydroxypyruvate, an intermediate in the serine biosynthesis pathway, to L-4-phosphohydroxythreonine, an intermediate in the pyridoxal-5'-phosphate synthesis pathway in a strain of Escherichia coli that lacks 4-phosphoerythronate dehydrogenase | L-4-hydroxythreonine | - |
r |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
glycine + glycolaldehyde | low-specificity L-threonine aldolase is involved in a serendipitous pathway that converts 3-phosphohydroxypyruvate, an intermediate in the serine biosynthesis pathway, to L-4-phosphohydroxythreonine, an intermediate in the pyridoxal-5'-phosphate synthesis pathway in a strain of Escherichia coli that lacks 4-phosphoerythronate dehydrogenase | Escherichia coli | L-4-hydroxythreonine | - |
r | |
L-4-hydroxythreonine | cleavage of L-4-hydroxythreonine is as efficient as cleavage of L-allo-threonine | Escherichia coli | glycine + glycolaldehyde | - |
r | |
L-allo-threonine | - |
Escherichia coli | glycine + acetaldehyde | - |
r | |
L-threonine | - |
Escherichia coli | glycine + acetaldehyde | - |
r |
Synonyms | Comment | Organism |
---|---|---|
LtaE | - |
Escherichia coli |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | - |
assay at | Escherichia coli |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
1.1 | - |
L-threonine | pH 8.0, 25°C | Escherichia coli | |
1.44 | - |
L-4-hydroxythreonine | pH 8.0, 25°C | Escherichia coli | |
3.2 | - |
L-allo-threonine | pH 8.0, 25°C | Escherichia coli |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8 | - |
assay at | Escherichia coli |
General Information | Comment | Organism |
---|---|---|
physiological function | low-specificity L-threonine aldolase is involved in a serendipitous pathway that converts 3-phosphohydroxypyruvate, an intermediate in the serine biosynthesis pathway, to L-4-phosphohydroxythreonine, an intermediate in the pyridoxal-5'-phosphate synthesis pathway in a strain of Escherichia coli that lacks 4-phosphoerythronate dehydrogenase | Escherichia coli |
kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
2.8 | - |
L-threonine | pH 8.0, 25°C | Escherichia coli | |
5.3 | - |
L-4-hydroxythreonine | pH 8.0, 25°C | Escherichia coli | |
6.2 | - |
L-allo-threonine | pH 8.0, 25°C | Escherichia coli |