EC Number   |
Application |
Reference |
|---|
    4.3.1.18 | analysis |
development of a simple, rapid, and inexpensive method of measuring the concentration of intrinsic free D-serine in tissue samples. The method uses chicken D-serine dehydratase in an enzymatic reaction to produce pyruvate, which is detected spectrophotometrically. The presence of Zn2+ or EDTA dioes not have any effect on pyruvate formation under the present assay conditions. The method is not affected by the presence of a large excess of L-serine, nor by the presence of tissue extracts, and accurately determines concentrations of 2-30 microM of D-serine. The entire assay requires only 60 min |
715734 |
| 4.3.1.18 | analysis |
enzymatic assay for D-serine. D-serine dehydratase converts D-serine to pyruvate, which is in turn oxidized by pyruvate oxidase. Then, in the presence of horseradish peroxidase, hydrogen peroxide formed during the oxidation converts 10-acetyl-3,7-dihydroxy-phenoxazine, i.e. Amplex Red, to resorufin, which exhibits a strong fluorescence. This improved assay can be used to determine the concentration of D-serine in calf serum |
715949 |
| 4.3.1.18 | degradation |
the enzyme is applied to remove endogenous D-serine from organotypic hippocampal slices. Complete removal of D-serine virtually abolishes NMDA-elicited neurotoxicity |
-, 666133 |
| 4.3.1.18 | medicine |
loss of serine deaminase activity results in a hypercolonization phenotype, hypercolonization plays a role in urinary tract infections |
680142 |
| 4.3.1.18 | medicine |
the established enzymatic method could be used for the quantitative determination of D-serine in human urine |
677539 |
| 4.3.1.18 | molecular biology |
the dsdA gene is used as a selectable marker for transformation of Arabidopsis |
666610 |
| 4.3.1.18 | pharmacology |
decrease in D-serine content may provide a therapeutic strategy for the treatment of the neurological disorders in which overstimulation of N-methyl-D-aspartate receptors plays a pathological role. D-Serine dehydratase (Dsd1p), which acts dominantly on D-serine, may be a useful D-serine reducing agent. A linear 5-kDa polyethylene glycol (PEG) is conjugated to Dsd1p and the effects of PEG-conjugation on its biochemical and pharmacokinetic properties are examined. PEG-Dsd1p retains activity, specificity, and stability of the enzyme. The PEG modification extended the serum half-life of Dsd1p in mice 6fold, from 3.8 h to 22.4 h. PEG-Dsd1p is much less immunogenic compared to the unmodified enzyme. Intraperitoneal administration of PEG-Dsd1p is effective in decreasing the D-serine content in the mouse hippocampus |
-, 748453 |
| 4.3.1.18 | pharmacology |
the D-serine dehydratase gene is an excellent marker, especially in the construction of strains for which the use of antibiotic resistance genes as selective markers is not allowed |
210817 |
