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Literature summary extracted from
- Distribution of eukaryotic serine racemases in the bacterial domain and characterization of a representative protein in Roseobacter litoralis Och 149 (2016), Microbiology, 162, 53-61 .
Activating Compound
| EC Number | Activating Compound | Comment | Organism | Structure |
|---|---|---|---|---|
| 5.1.1.18 | ATP | MgATP- enhances both activities of RiSR, racemization and dehydration. At 1 mM MgATP on dehydration and racemization activities are enhanced 3fold and 13fold, respectively | Roseobacter litoralis |  |
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 5.1.1.18 | DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, recombinant expression in Escherichia coli strains JM109 and BL21(DE3) | Roseobacter litoralis |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 5.1.1.18 | EDTA | abolishes racemization and dehydration activites of the enzyme | Roseobacter litoralis | |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 5.1.1.18 | 36.8 | - |
D-serine | pH 8.0, 30°C, recombinant His-tagged enzyme | Roseobacter litoralis | |
| 5.1.1.18 | 39 | - |
L-serine | pH 8.0, 30°C, recombinant His-tagged enzyme | Roseobacter litoralis | |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 5.1.1.18 | Mg2+ | enhances both activities of RiSR, racemization and dehydration | Roseobacter litoralis | |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 5.1.1.18 | L-serine | Roseobacter litoralis | - |
D-serine | - |
r | |
| 5.1.1.18 | L-serine | Roseobacter litoralis ATCC 49566 / DSM 6996 / JCM 21268 / NBRC 15278 / OCh 149 | - |
D-serine | - |
r | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 5.1.1.18 | Roseobacter litoralis | F7ZG00 | - |
- |
| 5.1.1.18 | Roseobacter litoralis ATCC 49566 / DSM 6996 / JCM 21268 / NBRC 15278 / OCh 149 | F7ZG00 | - |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 5.1.1.18 | recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and dialysis | Roseobacter litoralis |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 5.1.1.18 | L-serine | - |
Roseobacter litoralis | D-serine | - |
r | |
| 5.1.1.18 | L-serine | - |
Roseobacter litoralis ATCC 49566 / DSM 6996 / JCM 21268 / NBRC 15278 / OCh 149 | D-serine | - |
r | |
| 5.1.1.18 | additional information | the recombinant enzyme RiSR exhibits both racemization and dehydration activities exclusively towards serine. The catalytic efficiency for L-serine racemization of RiSR is 34fold higher than that of L-serine dehydration. RiSR primarily catalyses serine racemization rather than dehydration. The kcat/Km ratios of D-/L-serine and the racemization/dehydration ratio for RiSR are 0.95/1.01 and 34.4/38.3, respectively | Roseobacter litoralis | ? | - |
? | |
| 5.1.1.18 | additional information | the recombinant enzyme RiSR exhibits both racemization and dehydration activities exclusively towards serine. The catalytic efficiency for L-serine racemization of RiSR is 34fold higher than that of L-serine dehydration. RiSR primarily catalyses serine racemization rather than dehydration. The kcat/Km ratios of D-/L-serine and the racemization/dehydration ratio for RiSR are 0.95/1.01 and 34.4/38.3, respectively | Roseobacter litoralis ATCC 49566 / DSM 6996 / JCM 21268 / NBRC 15278 / OCh 149 | ? | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 5.1.1.18 | ? | x * 35000, His-tagged recombinant enzyme, SDS-PAGE | Roseobacter litoralis |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 5.1.1.18 | RiSR | - |
Roseobacter litoralis |
| 5.1.1.18 | RLO149_c015450 | - |
Roseobacter litoralis |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 5.1.1.18 | 30 | - |
assay at | Roseobacter litoralis |
Turnover Number [1/s]
| EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 5.1.1.18 | 2.04 | - |
L-serine | pH 8.0, 30°C, recombinant His-tagged enzyme | Roseobacter litoralis | |
| 5.1.1.18 | 2.22 | - |
D-serine | pH 8.0, 30°C, recombinant His-tagged enzyme | Roseobacter litoralis | |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 5.1.1.18 | 8 | - |
assay at | Roseobacter litoralis |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 5.1.1.18 | pyridoxal 5'-phosphate | - |
Roseobacter litoralis | |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 5.1.1.18 | evolution | the enzyme belongs to the fold-type II group of pyridoxal 5'-phosphate enzymes | Roseobacter litoralis |
kcat/KM [mM/s]
| EC Number | kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 5.1.1.18 | 0.052 | - |
L-serine | pH 8.0, 30°C, recombinant His-tagged enzyme | Roseobacter litoralis | |
| 5.1.1.18 | 0.06 | - |
D-serine | pH 8.0, 30°C, recombinant His-tagged enzyme | Roseobacter litoralis | |
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