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
-
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
ECTree
4.3.1.18 D-Serine ammonia-lyaseAdvanced search results
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results (Substrates Products
Substrates Products on EC 4.3.1.18 - D-Serine ammonia-lyase
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
beta-chloro-D-alanine
3-chloro-D-alanine
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activity of approximately 2%
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-
?
D-allo-Thr
2-oxobutanoate + NH3
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-
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?
additional information
?
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the enzyme does not show 1-aminocyclopropane-1-carboxylate deaminase activity at high temperature as well as at room temperature though it has significant sequence similarity to 1-aminocyclopropane-1-carboxylate deaminase from the yeast Hansenula saturnus
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-
?
D-serine
?
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adaptive enzyme, which enables cells to grow with D-Ser as the sole source of carbon and nitrogen
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-
?
D-serine
?
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adaptive enzyme, which enables cells to grow with D-Ser as the sole source of carbon and nitrogen
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-
?
D-serine
?
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the enzyme enables cells to grow with D-Ser as the sole source of nitrogen
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-
?
D-serine
pyruvate + NH3
the enzyme is 460fold and 1700fold more active than D-amino acid oxidase and serine racemase, respectively, in degrading D-Ser
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-
?
D-serine
pyruvate + NH3
the enzyme is 460fold and 1700fold more active than D-amino acid oxidase and serine racemase, respectively, in degrading D-Ser
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-
?
D-serine
pyruvate + NH3
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210802, 210803, 210804, 210805, 210806, 210808, 210810, 210811, 210812, 210813, 210814, 210815, 210816, 210817
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-
?
D-serine
pyruvate + NH3
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none of the reaction products that would be expected from side reactions of the PLP-D-serine Schiff base are detected during the more than 6000 catalytic cycles of dehydration, indicating high reaction specificity. Neither transamination product 3-hydroxypyruvate, retro-aldol cleavage product glycine, decarboxylation product 2-aminoethanol, or racemization product L-serine are detected
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-
?
D-serine
pyruvate + NH3
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-
-
?
D-threonine
2-oxobutanoate + NH3
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activity of approximately 3%
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-
?
