Cloned (Comment) | Organism |
---|---|
sequence comparisons, cloning from leaf DNA, recombinant expression of C-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3) | Zea mays |
Crystallization (Comment) | Organism |
---|---|
purified recombinant His6-tagged enzyme, hanging drop vapour diffusion method, mixing of 0.001 ml of 10 mg/ml protein in 20 mM Tris-HCl, 100 mM NaCl, 10% glycerol, pH 8.0, with 0.001 ml of reservoir solution containing 0.2 M calcium acetate, 0.1 M sodium cacodylate, pH 6.5, 18% PEG 8000, equilibration agains 0.2 ml of reservoir solution, at 4°C, X-ray diffraction structure determination and analysis at 2.1 A resolution, molecular replacement based on the Rattus norvegicus serine racemase, PDB ID 3hmk | Zea mays |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
82000 | - |
recombinant His6-tagged enzyme, gel filtration | Zea mays |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-serine | Zea mays | - |
D-serine | - |
r |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Zea mays | F5CAQ9 | - |
- |
Purification (Comment) | Organism |
---|---|
recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and ultrafiltration | Zea mays |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
L-serine = D-serine | reversible racemization and irreversible dehydration reactions are catalyzed by eukaryotic serine racemase, overview | Zea mays |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
leaf | - |
Zea mays | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-serine | - |
Zea mays | D-serine | - |
r |
Subunits | Comment | Organism |
---|---|---|
homodimer | 2 * 35000, recombinant His6-tagged enzyme, SDS-PAGE | Zea mays |
Synonyms | Comment | Organism |
---|---|---|
Zm-SR | - |
Zea mays |
ZmSR | - |
Zea mays |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
pyridoxal 5'-phosphate | PLP, dependent on, the PLP is bound to each monomer by forming a Schiff base with Lys67 | Zea mays |
General Information | Comment | Organism |
---|---|---|
evolution | the enzyme from Zea mays belongs to the type II PLP-dependent enzymes and differs from the enzyme of a vancomycin-resistant bacterium | Zea mays |
additional information | structural comparison with Rattus norvegicus and Schizosaccharomyces pombe serine racemases reveals a similar arrangement of active-site residues but a different orientation of the C-terminal helix, structure modeling, overview. Active site structure comparisons | Zea mays |
physiological function | the enzyme is responsible for D-serine biosynthesis in vivo | Zea mays |