Activating Compound | Comment | Organism | Structure |
---|---|---|---|
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 (Comment) | Organism |
---|---|
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 | Comment | Organism | Structure |
---|---|---|---|
EDTA | abolishes racemization and dehydration activites of the enzyme | Roseobacter litoralis |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
36.8 | - |
D-serine | pH 8.0, 30°C, recombinant His-tagged enzyme | Roseobacter litoralis | |
39 | - |
L-serine | pH 8.0, 30°C, recombinant His-tagged enzyme | Roseobacter litoralis |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | enhances both activities of RiSR, racemization and dehydration | Roseobacter litoralis |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-serine | Roseobacter litoralis | - |
D-serine | - |
r | |
L-serine | Roseobacter litoralis ATCC 49566 / DSM 6996 / JCM 21268 / NBRC 15278 / OCh 149 | - |
D-serine | - |
r |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Roseobacter litoralis | F7ZG00 | - |
- |
Roseobacter litoralis ATCC 49566 / DSM 6996 / JCM 21268 / NBRC 15278 / OCh 149 | F7ZG00 | - |
- |
Purification (Comment) | Organism |
---|---|
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and dialysis | Roseobacter litoralis |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-serine | - |
Roseobacter litoralis | D-serine | - |
r | |
L-serine | - |
Roseobacter litoralis ATCC 49566 / DSM 6996 / JCM 21268 / NBRC 15278 / OCh 149 | D-serine | - |
r | |
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 | ? | - |
? | |
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 | Comment | Organism |
---|---|---|
? | x * 35000, His-tagged recombinant enzyme, SDS-PAGE | Roseobacter litoralis |
Synonyms | Comment | Organism |
---|---|---|
RiSR | - |
Roseobacter litoralis |
RLO149_c015450 | - |
Roseobacter litoralis |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
30 | - |
assay at | Roseobacter litoralis |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
2.04 | - |
L-serine | pH 8.0, 30°C, recombinant His-tagged enzyme | Roseobacter litoralis | |
2.22 | - |
D-serine | pH 8.0, 30°C, recombinant His-tagged enzyme | Roseobacter litoralis |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8 | - |
assay at | Roseobacter litoralis |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
pyridoxal 5'-phosphate | - |
Roseobacter litoralis |
General Information | Comment | Organism |
---|---|---|
evolution | the enzyme belongs to the fold-type II group of pyridoxal 5'-phosphate enzymes | Roseobacter litoralis |
kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.052 | - |
L-serine | pH 8.0, 30°C, recombinant His-tagged enzyme | Roseobacter litoralis | |
0.06 | - |
D-serine | pH 8.0, 30°C, recombinant His-tagged enzyme | Roseobacter litoralis |