4.3.1.18: D-Serine ammonia-lyase
This is an abbreviated version!
For detailed information about D-Serine ammonia-lyase, go to the full flat file.
Word Map on EC 4.3.1.18
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4.3.1.18
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5'-phosphate
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l-serine
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d-threonine
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tryptophanase
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coagonists
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fold-type
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5'-phosphate-dependent
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pyridoxal-p
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merodiploids
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medicine
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pharmacology
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analysis
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molecular biology
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degradation
- 4.3.1.18
- 5'-phosphate
- l-serine
- d-threonine
- tryptophanase
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coagonists
-
fold-type
-
5'-phosphate-dependent
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pyridoxal-p
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merodiploids
- medicine
- pharmacology
- analysis
- molecular biology
- degradation
Reaction
Synonyms
chDSD, D-Hydroxy amino acid dehydratase, D-Ser dehydratase, D-serine ammonia lyase, D-serine ammonia-lyase, D-Serine deaminase, D-Serine dehydrase, D-serine dehydratase, D-Serine hydrolase (deaminating), DDB_G0289463, Dehydratase, D-serine, DSD, Dsd1p, DsdA, Dsdase, DsdSC, EC 4.2.1.14, PA3357, PH0054, Serine deaminase
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Application on EC 4.3.1.18 - D-Serine ammonia-lyase
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APPLICATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
analysis
degradation
medicine
molecular biology
the dsdA gene is used as a selectable marker for transformation of Arabidopsis
pharmacology
analysis
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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
analysis
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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
degradation
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the enzyme is applied to remove endogenous D-serine from organotypic hippocampal slices. Complete removal of D-serine virtually abolishes NMDA-elicited neurotoxicity
degradation
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the enzyme is applied to remove endogenous D-serine from organotypic hippocampal slices. Complete removal of D-serine virtually abolishes NMDA-elicited neurotoxicity
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medicine
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loss of serine deaminase activity results in a hypercolonization phenotype, hypercolonization plays a role in urinary tract infections
medicine
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the established enzymatic method could be used for the quantitative determination of D-serine in human urine
pharmacology
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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
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
pharmacology
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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
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