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Information on EC 4.3.2.1 - argininosuccinate lyase
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4.3.2.1 argininosuccinate lyaseSpecify your search results
Word Map
- 4.3.2.1
- ornithine
- arginase
- citrulline
-
transcarbamylase
- ammonia
- aciduria
- l-arginine
-
hyperammonemia
- duck
-
delta-crystallins
-
carbamyl
- lenses
-
carbamoyltransferase
- carbamoylphosphate
- citrullinemia
-
urea-cycle
- n-acetylglutamate
-
ureotelic
- medicine
-
ureogenesis
-
6.3.4.5
-
reptilian
- pharmacology
- drug development
- diagnostics
- analysis
The enzyme appears in viruses and cellular organisms
Synonyms
argininosuccinate lyase, argininosuccinase, argininosuccinic acid lyase, delta2-crystallin, delta2 crystallin, arginosuccinase, l-argininosuccinate arginine-lyase, arginine-succinate lyase, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
AL
ArgH
arginine-succinate lyase
-
-
-
-
argininosuccinase
Argininosuccinate lyase
argininosuccinic acid lyase
-
-
-
-
Arginosuccinase
-
-
-
-
ASAL
-
-
-
-
ASL
delta2-crystallin
-
-
-
-
L-argininosuccinate arginine-lyase
-
-
-
-
lyase, argininosuccinate
-
-
-
-
Rv1659
argininosuccinase
-
-
-
-
Argininosuccinate lyase
-
-
-
-
ASL
-
-
-
-
ASL
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2-(Nomega-L-arginino)succinate = fumarate + L-arginine
5 residues are essential for catalytic activity: R115, N116, T161, S283, and E296
-
2-(Nomega-L-arginino)succinate = fumarate + L-arginine
random mechanism with the formation of two dead-end complexes: enzyme-argininosuccinate-fumarate and enzyme-argininosuccinate-arginine
-
2-(Nomega-L-arginino)succinate = fumarate + L-arginine
stepwise E1cB mechanism, rate-limiting step probably at the C-N bond-cleavage step
-
2-(Nomega-L-arginino)succinate = fumarate + L-arginine
random uni-bi kinetic mechanism
-
2-(Nomega-L-arginino)succinate = fumarate + L-arginine
random uni-bi kinetic mechanism
-
2-(Nomega-L-arginino)succinate = fumarate + L-arginine
random uni-bi kinetic mechanism
-
2-(Nomega-L-arginino)succinate = fumarate + L-arginine
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
elimination
elimination
-
-
C-N bond cleavage
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
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SYSTEMATIC NAME
IUBMB Comments
2-(Nomega-L-arginino)succinate arginine-lyase (fumarate-forming)
-
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CAS REGISTRY NUMBER
COMMENTARY
9027-34-3
-
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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
argininosuccinate
?
-
urea cycle enzyme, deficiency results in argininosuccinic aciduria
-
-
?
N,N'-bis(tert-butoxycarbonyl)-5-[(3-aminopropyl)amino]pentan-1-ol
?
-
-
-
-
?
(Nomega-L-arginino)succinate
fumarate + L-arginine
-
last step in the biosynthesis of arginine
-
r
2-(Nomega-L-arginino)succinate
fumarate + L-arginine
as part of the urea cycle, the enzyme is essential for ammonia detoxification and L-arginine synthesis
-
-
?
2-(Nomega-L-arginino)succinate
fumarate + L-arginine
-
-
-
?
2-(Nomega-L-arginino)succinate
fumarate + L-arginine
last enzyme of the arginine biosynthesis pathway
-
-
?
2-(Nomega-L-arginino)succinate
fumarate + L-arginine
-
-
-
?
2-(Nomega-L-arginino)succinate
fumarate + L-arginine
last enzyme of the arginine biosynthesis pathway
-
-
?
argininosuccinate
fumarate + L-Arg
-
biological activity in liver, ileum, small intestine, heart, lung and kidney within the urea and nitric oxide cycle
-
-
?
fumarate + L-arginine
2-(Nomega-L-arginino)succinate
-
accumulation of fumarate leads to reversed argininosuccinate lyase activity in fumarate hydratase-deficient cancer cells
-
-
r
fumarate + L-arginine
2-(Nomega-L-arginino)succinate
-
accumulation of fumarate leads to reversed argininosuccinate lyase activity in fumarate hydratase-deficient cancer cells
-
-
r
additional information
?
-
-
the genetic variant OsASL1.1 has argininosuccinate lyase activity, while variant OsASL1.2 has no activity
-
-
?
additional information
?
-
-
enzyme is involved in arginine biosynthesis and in urea cycle
-
-
?
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NATURAL SUBSTRATE
NATURAL 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
argininosuccinate
?
-
urea cycle enzyme, deficiency results in argininosuccinic aciduria
-
-
?
(Nomega-L-arginino)succinate
fumarate + L-arginine
-
last step in the biosynthesis of arginine
-
r
2-(Nomega-L-arginino)succinate
fumarate + L-arginine
as part of the urea cycle, the enzyme is essential for ammonia detoxification and L-arginine synthesis
-
-
?
2-(Nomega-L-arginino)succinate
fumarate + L-arginine
last enzyme of the arginine biosynthesis pathway
-
-
?
2-(Nomega-L-arginino)succinate
fumarate + L-arginine
last enzyme of the arginine biosynthesis pathway
-
-
?
argininosuccinate
fumarate + L-Arg
-
biological activity in liver, ileum, small intestine, heart, lung and kidney within the urea and nitric oxide cycle
-
-
?
fumarate + L-arginine
2-(Nomega-L-arginino)succinate
-
accumulation of fumarate leads to reversed argininosuccinate lyase activity in fumarate hydratase-deficient cancer cells
-
-
r
fumarate + L-arginine
2-(Nomega-L-arginino)succinate
-
accumulation of fumarate leads to reversed argininosuccinate lyase activity in fumarate hydratase-deficient cancer cells
-
-
r
additional information
?
-
-
enzyme is involved in arginine biosynthesis and in urea cycle
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
bromomesaconic acid
-
argininosuccinate completely protects, Lys51 has an essential role in binding of argininosuccinate and consequently is essential in catalysis; inactivation follows pseudo-first-order kinetics
D-glucose
-
12.5 mM glucose decreases activity of ASL by 20%, 25 mM glucose by 50%
citrulline
-
competitive versus Arg and noncompetitive versus argininosuccinate and fumarate
fumarate
a potential feedback mechanism is proposed, wherein the Cys441 is covalently modified to S-(2-succinyl) cysteine by one of the products, fumarate
additional information
-
the antibody of the liver enzyme is an effective inhibitor of brain enzyme
-
additional information
-
mRNA expression and activity of liver argininosuccinate lyase decrease with age
-
additional information
-
acetylation at Lys288 or Lys69 decreases activity of ASL
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
amino acids
-
extra amino acids in culture media increases activity of ASL by decreasing inhibitory acetylation rate
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.032
2-(Nomega-L-arginino)succinate
pH 7.4, 25°C, mutant enzyme C441S
0.112
2-(Nomega-L-arginino)succinate
pH 7.4, 25°C, wild-type enzyme