4.3.1.15: Diaminopropionate ammonia-lyase
This is an abbreviated version!
For detailed information about Diaminopropionate ammonia-lyase, go to the full flat file.
Word Map on EC 4.3.1.15
-
4.3.1.15
-
typhimurium
-
5'-phosphate
-
plp-dependent
-
alpha,beta-elimination
-
d-isomer
-
l-2,3-diaminopropionate
-
monoclinic
-
l-forms
-
monovalent
-
etch
-
pseudomonad
-
tetragonal
-
neurotoxins
-
dehydratase
-
d-serine
-
medicine
-
analysis
- 4.3.1.15
- typhimurium
- 5'-phosphate
-
plp-dependent
-
alpha,beta-elimination
-
d-isomer
- l-2,3-diaminopropionate
-
monoclinic
-
l-forms
-
monovalent
-
etch
-
pseudomonad
-
tetragonal
-
neurotoxins
- dehydratase
- d-serine
- medicine
- analysis
Reaction
Synonyms
2,3-Diaminopropionate:ammonia-lyase, alpha,beta-Diaminopropionate ammonia-lyase, ammonia-lyase, diaminopropionate, DAP ammonia-lyase, DAPAL, Diaminopropionatase, diaminopropionate ammonia lyase, diaminopropionate ammonia-lyase, DpaL, EcDAPAL, L-Diaminopropionate ammonia-lyase, sDAPAL, STM1002, ygeX
ECTree
4.3.1.15 Diaminopropionate ammonia-lyaseAdvanced search results
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results (Substrates Products
Substrates Products on EC 4.3.1.15 - Diaminopropionate 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
2-[5-amino-2-(4-fluoro-phenyl)-6-oxo-6H-pyrimidin-1-yl]-N-(1-benzyl-2-oxo-2-thiazol-2-yl-ethyl)-acetamide + H2O
?
-
-
-
-
?
D-2,3-diaminopropanoate + 2 H2O
pyruvate + 2 NH3
-
-
-
?
DL-2,3-diaminopropanoate + 2 H2O
pyruvate + 2 NH3
-
-
-
?
L-2,3-diaminopropanoate + 2 H2O
pyruvate + 2 NH3
-
-
-
?
additional information
?
-
-
the enzyme is induced only by L-2,3-diaminopropionate or D-2,3-diaminopropanoate
-
-
?
2,3-diaminopropanoate + H2O
pyruvate + 2 NH3
specific role for the enzyme in degrading 2,3-diaminopropanoate to avoid metabolic stress
-
-
?
2,3-diaminopropanoate + H2O
pyruvate + 2 NH3
diaminopropionate ammonia-lyase-dependent degradation of 2,3-diaminopropanoate to pyruvate proceeds through an unbound 2-aminoacrylate intermediate
-
-
?
2,3-diaminopropanoate + H2O
pyruvate + 2 NH3
Salmonella enterica DM14828
specific role for the enzyme in degrading 2,3-diaminopropanoate to avoid metabolic stress
-
-
?
2,3-diaminopropanoate + H2O
pyruvate + 2 NH3
Salmonella enterica DM14828
diaminopropionate ammonia-lyase-dependent degradation of 2,3-diaminopropanoate to pyruvate proceeds through an unbound 2-aminoacrylate intermediate
-
-
?
2,3-diaminopropanoate + H2O
pyruvate + NH3
-
precursor of a neurotoxin in Lathyrus sativus seed extracts
-
-
?
2,3-diaminopropanoate + H2O
pyruvate + NH3
-
precursor of a neurotoxin in Lathyrus sativus seed extracts
-
-
?
D-2,3-diaminopropanoate + H2O
pyruvate + 2 NH3
the enzyme degrades both the D and L forms of diaminopropionic acid. A phosphate group is located in the active site of the enzyme and expulsion of this phosphate is probably essential to bring Asp125 to a conformation suitable for proton abstraction from the substrate
-
-
?
D-2,3-diaminopropanoate + H2O
pyruvate + 2 NH3
the enzyme degrades both the D and L forms of diaminopropionic acid. A phosphate group is located in the active site of the enzyme and expulsion of this phosphate is probably essential to bring Asp125 to a conformation suitable for proton abstraction from the substrate
-
-
?
D-2,3-Diaminopropanoate + H2O
Pyruvate + NH3
-
only 12% of the activity with L-2,3-diaminopropanoate
-
?
D-2,3-Diaminopropanoate + H2O
Pyruvate + NH3
-
-
-
?
D-serine
pyruvate + NH3
-
-
-
?
D-serine + H2O
pyruvate + NH3
-
-
-
?
DL-2,3-diaminopropanoate + H2O
pyruvate + NH3
-
-
-
?
L-2,3-diaminopropanoate + H2O
pyruvate + 2 NH3
the enzyme degrades both the D and L forms of diaminopropionic acid. A phosphate group is located in the active site of the enzyme and expulsion of this phosphate is probably essential to bring Asp125 to a conformation suitable for proton abstraction from the substrate
-
-
?
L-2,3-diaminopropanoate + H2O
pyruvate + 2 NH3
the enzyme degrades both the D and L forms of diaminopropionic acid. A phosphate group is located in the active site of the enzyme and expulsion of this phosphate is probably essential to bring Asp125 to a conformation suitable for proton abstraction from the substrate
-
-
?
L-2,3-Diaminopropanoate + H2O
Pyruvate + NH3
-
-
-
?
L-2,3-Diaminopropanoate + H2O
Pyruvate + NH3
-
-
-
?
L-serine
pyruvate + NH3
-
-
-
?
