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
-
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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General Information
General Information on EC 4.3.1.18 - D-Serine ammonia-lyase
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malfunction
metabolism
physiological function
DsdA contributes to virulence within the urinary tract of mice
malfunction
dsd-null cells exhibit delay in development and arrest at the early culmination stage. The efficiency of spore formation is considerably reduced in the mutant cells
malfunction
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dsd-null cells exhibit delay in development and arrest at the early culmination stage. The efficiency of spore formation is considerably reduced in the mutant cells
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due to its low level of expression and the lack of induction by exogenous D-serine, this dsdA gene does not have any apparent contribution to D-serine utilization in Pseudomonas aeruginosa PAO1. However, a high level of DsdA when overexpressed from a recombinant plasmid is able to support growth on D-serine as the sole source of carbon and nitrogen
metabolism
the enzyme is 460fold and 1700fold more active than D-amino acid oxidase and serine racemase, respectively, in degrading D-Ser. D-Ser dehydrogenase is the primary enzyme responsible for D-Ser decomposition in Dictyostelium discoideum
metabolism
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the enzyme is 460fold and 1700fold more active than D-amino acid oxidase and serine racemase, respectively, in degrading D-Ser. D-Ser dehydrogenase is the primary enzyme responsible for D-Ser decomposition in Dictyostelium discoideum
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