Information on EC 4.3.1.13 - carbamoyl-serine ammonia-lyase

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The expected taxonomic range for this enzyme is: Rattus norvegicus

EC NUMBER
COMMENTARY hide
4.3.1.13
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RECOMMENDED NAME
GeneOntology No.
carbamoyl-serine ammonia-lyase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
O-carbamoyl-L-serine + H2O = pyruvate + 2 NH3 + CO2
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
elimination
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of NH3, C-N bond cleavage
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additional information
SYSTEMATIC NAME
IUBMB Comments
O-carbamoyl-L-serine ammonia-lyase (decarboxylating; pyruvate-forming)
A pyridoxal-phosphate protein. The enzyme cleaves a carbon-oxygen bond, releasing CO2, ammonia, and an unstable enamine product that tautomerizes to an imine form, which undergoes a hydrolytic deamination to form pyruvate and a second ammonia molecule. The latter reaction, which can occur spontaneously, can also be catalysed by EC 3.5.99.10, 2-iminobutanoate/2-iminopropanoate deaminase.
CAS REGISTRY NUMBER
COMMENTARY hide
52227-64-2
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
O-Carbamoyl-L-serine
?
show the reaction diagram
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-
-
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O-carbamoyl-L-serine
pyruvate + 2 NH3 + CO2
show the reaction diagram
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S-carbamoyl-L-cysteine
pyruvate + ?
show the reaction diagram
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10% pyruvate formation of that towards O-carbamoyl-L-serine
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
O-Carbamoyl-L-serine
?
show the reaction diagram
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-
-
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
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omission leads to 60% decrease of activity
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
beta-chloro-L-alanine
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irreversible
L-Albizziin
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20 mM, 20% inhibition
L-glutamine
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20 mM, 60% inhibition
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
17
O-Carbamoyl-L-serine
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.8 - 8.8
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in 0.1 M sodium borate buffer
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
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enzyme assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, no loss of activity after 2 weeks in 20% glycerol containing 0.1 mM pyridoxal 5-phosphate, 1 mM 2-mercaptoethanol and 10 mM potassium phosphate bufer, pH 7.2
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE