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Literature summary for 5.1.1.18 extracted from
- Modulating the function of human serine racemase and human serine dehydratase by protein engineering (2012), Protein Eng. Des. Sel., 25, 741-749.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression of C-terminally His6-tagged wild-type and mutant enzymes in Escherichia coli strain MC1061 | Homo sapiens |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| S84A | site-directed mutagenesis, the mutant is inactive in L- or D-serine racemization, but still shows dehydration activity | Homo sapiens |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| L-serine | Homo sapiens | - |
D-serine | - |
? |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | Q9GZT4 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant C-terminally His6-tagged wild-type and mutant enzymes from Escherichia coli strain MC1061 by nickel affinity chromatography and gel filtration | Homo sapiens |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| L-serine = D-serine | L-serine forms Schiff base with the cofactor pyridoxal 5'-phosphate, the free (non-pyridoxal 5'-phosphate cofactor binding) amino group of K56 is in the vicinity of the hydrogen on the Calpha atom, allowing the side chain of K56 to extract the proton away from the Ca atom and form a planar intermediate. the hydroxyl group of S84, on the re-face of this planar intermediate, donates its hydrogen to the Calpha atom of the intermediate resulting in the formation of D-serine. The subsequent attack of K56 on the cofactor forms the Schiff base and releases D-serine as the product. If the starting substrate is D-serine, S84 is likely to be protonated, favoring the extraction of hydrogen from the Calpha atom of pyridoxal 5'-phosphate-D-serine. The resulting planar intermediate allows K56 amino group to provide a proton from the si-face, restoring the L-serine intermediate. As a result, K56 reacts with pyridoxal 5'-phosphate to form the Schiff base and releases the L-serine as the final product. Catalytic mechanism, overview | Homo sapiens |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| brain | - |
Homo sapiens | - |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 0.139 | - |
purified His-tagged wild-type enzyme, pH 8.0, 37°C, substrate D-serine | Homo sapiens |
| 0.263 | - |
purified His-tagged wild-type enzyme, pH 8.0, 37°C, substrate L-serine | Homo sapiens |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| L-serine | - |
Homo sapiens | D-serine | - |
? | |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
assay at | Homo sapiens |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8 | - |
assay at | Homo sapiens |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| pyridoxal 5'-phosphate | dependent on | Homo sapiens | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| additional information | a A65S hSDH mutant of serine dehydratase, EC 4.2.1.13, acquires an additional function of using D-serine as a substrate | Homo sapiens |
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