Activating Compound | Comment | Organism | Structure |
---|---|---|---|
ATP | - |
Rattus norvegicus | |
ATP | - |
Homo sapiens |
Application | Comment | Organism |
---|---|---|
drug development | serine racemase is a promising target for the development of specific inhibitors in the treatment of disorders related to NMDAR dysfunction. Analysis of the molecular basis for rational drug design using the X-ray crystal structures of human and rat serine racemase | Rattus norvegicus |
drug development | serine racemase is a promising target for the development of specific inhibitors in the treatment of disorders related to NMDAR dysfunction. Analysis of the molecular basis for rational drug design using the X-ray crystal structures of human and rat serine racemase | Homo sapiens |
pharmacology | because D-serine affects NMDAR signaling throughout the brain, serine racemase is a promising target for the treatment of disorders related to NMDAR dysfunction | Homo sapiens |
Cloned (Comment) | Organism |
---|---|
expression of His-tagged enzyme mutant in Escherichia coli strain Rosetta 2 (DE3) | Rattus norvegicus |
expression of His-tagged enzyme mutant in Escherichia coli strain Rosetta 2 (DE3) | Homo sapiens |
Crystallization (Comment) | Organism |
---|---|
purified recombinant mutant C2D/C6D by sitting drop vapor diffusion, 10 mg/ml protein in 20 mM Tris-HCl, pH 8.0, 100 mM NaCl, 10% glycerol, 0.05 mM PLP, 2 mM MgCl2, 5 mM dithiothreitol, mixed with 25% PEG 3350, 200 mM sodium malonate, and 50 mM MnCl2 as the reservoir solution, 4 days, the selenomethionine-labeled enzyme crystals grow under similar conditions, X-ray diffraction structure determination and analysis at 1.5-1.7 A resolution | Homo sapiens |
purified recombinant mutant C2D/C6D by sitting drop vapor diffusion, 35 mg/ml protein, from 55% v/v Tacsimate, i.e. 1.8305 M malonic acid, 0.25 M ammonium citrate tribasic, 0.12 M succinic acid, 0.3 M DL-malic acid, 0.4 M sodium acetate trihydrate, 0.5 M sodium formate, and 0.16 M ammonium tartrate dibasic, pH 8.0, and 100 mM Bis-Tris propane, pH 7.8, 10 days, X-ray diffraction structure determination and analysis at 1.8-1.95 A resolution | Rattus norvegicus |
Protein Variants | Comment | Organism |
---|---|---|
C2D/C6D | site-directed mutagenesis | Rattus norvegicus |
C2D/C6D | site-directed mutagenesis | Homo sapiens |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
phosphatidylinositol-4,5-bisphosphate | - |
Homo sapiens | |
phosphatidylinositol-4,5-bisphosphate | - |
Rattus norvegicus |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | activates | Rattus norvegicus | |
Mg2+ | activates | Homo sapiens |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-serine | Rattus norvegicus | - |
D-serine | - |
r | |
L-serine | Homo sapiens | - |
D-serine | - |
r |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | Q9GZT4 | - |
- |
Rattus norvegicus | - |
- |
- |
Purification (Comment) | Organism |
---|---|
recombinant His-tagged enzyme mutant from Escherichia coli strain Rosetta 2 (DE3) by affinity chromatography and gel filtration to over 98% purity | Rattus norvegicus |
recombinant His-tagged enzyme mutant from Escherichia coli strain Rosetta 2 (DE3) by affinity chromatography and gel filtration to over 98% purity | Homo sapiens |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
L-serine = D-serine | racemase and dehydratase reaction mechanism of serine racemase, overview | Rattus norvegicus | |
L-serine = D-serine | racemase and dehydratase reaction mechanism of serine racemase, overview | Homo sapiens |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
brain | - |
Rattus norvegicus | - |
brain | - |
Homo sapiens | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-serine | - |
Rattus norvegicus | D-serine | - |
r | |
L-serine | - |
Homo sapiens | D-serine | - |
r |
Subunits | Comment | Organism |
---|---|---|
More | the enzyme structures shows a fold typical of beta-family pyridoxal 5'-phosphate enzymes, with both a large domain and a flexible small domain associated into a symmetric dimer, and indicated a ligand-induced rearrangement of the small domain that organizes the active site for specific turnover of the substrate, ligand-induced shift of small and large domains of the racemase, structure analysis, overview | Rattus norvegicus |
More | the enzyme structures shows a fold typical of beta-family pyridoxal 5'-phosphate enzymes, with both a large domain and a flexible small domain associated into a symmetric dimer, and indicated a ligand-induced rearrangement of the small domain that organizes the active site for specific turnover of the substrate, ligand-induced shift of small and large domains of the racemase, structure analysis, overview | Homo sapiens |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Rattus norvegicus |
37 | - |
assay at | Homo sapiens |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
9 | - |
assay at | Rattus norvegicus |
9 | - |
assay at | Homo sapiens |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
pyridoxal 5'-phosphate | dependent on, binding site structure, overview | Rattus norvegicus | |
pyridoxal 5'-phosphate | dependent on, binding site structure, overview | Homo sapiens |