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Information on EC 6.3.4.5 - argininosuccinate synthase
for references in articles please use BRENDA:EC6.3.4.5
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EC Tree 6 Ligases
6.3 Forming carbon-nitrogen bonds
6.3.4 Other carbon-nitrogen ligases
6.3.4.5 argininosuccinate synthase
The enzyme appears in viruses and cellular organisms
- 6.3.4.5
- ornithine
- citrullinemia
- arginase
- ammonia
- hyperammonemia
- deiminase
-
transcarbamylase
- l-arginine
-
pegylated
-
auxotrophic
-
adi-peg20
-
carbamyl
-
adult-onset
- coma
- argininosuccinase
- carbamoylphosphate
-
carbamoyltransferase
-
citrin
- tropoelastin
-
urea-cycle
-
consciousness
- medicine
-
ureogenesis
-
elastogenesis
-
ornithine-urea
-
elastin-derived
- jararaca
-
coinduction
-
bothrops
- n-acetylglutamate
- drug development
- molecular biology
Reaction Schemes
showSynonyms
argininosuccinate synthetase, argininosuccinate synthase, elastin-binding protein, argininosuccinate synthase 1, argininosuccinic acid synthetase, arginine succinate synthetase, citrulline-aspartate ligase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ARGG
Arginine succinate synthetase
-
-
-
-
Argininosuccinate synthetase
Argininosuccinic acid synthetase
-
-
-
-
AS
ASS
ASS1
Citrulline--aspartate ligase
-
-
-
-
Citrulline-aspartate ligase
Elastin-binding protein
-
-
-
-
Synthetase, argininosuccinate
-
-
-
-
tAsS
Argininosuccinate synthetase
-
-
-
-
Argininosuccinate synthetase
-
-
ASS
-
-
-
-
Citrulline-aspartate ligase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + L-citrulline + L-aspartate = AMP + diphosphate + 2-(Nomega-L-arginino)succinate
rapid-equilibrium random mechanism
-
ATP + L-citrulline + L-aspartate = AMP + diphosphate + 2-(Nomega-L-arginino)succinate
ordered addition of MgATP2-, citrulline, and aspartate, followed by ordered release of argininosuccinate, magnesiumdiphosphate and AMP
-
ATP + L-citrulline + L-aspartate = AMP + diphosphate + 2-(Nomega-L-arginino)succinate
mechanism
-
ATP + L-citrulline + L-aspartate = AMP + diphosphate + 2-(Nomega-L-arginino)succinate
essential Arg in the active site participates in the binding of ATP and diphosphate. The binding of ATP and diphosphate at the same site is mutually exclusive
-
ATP + L-citrulline + L-aspartate = AMP + diphosphate + 2-(Nomega-L-arginino)succinate
-
-
-
-
ATP + L-citrulline + L-aspartate = AMP + diphosphate + 2-(Nomega-L-arginino)succinate
catalytic mechanism
-
ATP + L-citrulline + L-aspartate = AMP + diphosphate + 2-(Nomega-L-arginino)succinate
detailed catalytic mechanism
-
ATP + L-citrulline + L-aspartate = AMP + diphosphate + 2-(Nomega-L-arginino)succinate
detailed catalytic mechanism, stereochemistry
ATP + L-citrulline + L-aspartate = AMP + diphosphate + 2-(Nomega-L-arginino)succinate
it is found that argininosuccinate synthetase is the major lipid A-interacting protein in liver. Argininosuccinate synthetase also inhibits the biological activities of natural lipid A and rough-type lipopolysaccharide and but not smooth-type lipopolysaccharide. Argininosuccinate synthetase enzyme activity is inhibited by lipid A and rough-type lipopolysaccharide and smooth-type lipopolysaccharide.
-
ATP + L-citrulline + L-aspartate = AMP + diphosphate + 2-(Nomega-L-arginino)succinate
rapid-equilibrium random mechanism
-
-
ATP + L-citrulline + L-aspartate = AMP + diphosphate + 2-(Nomega-L-arginino)succinate
catalytic mechanism
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
-
ATP + L-citrulline + L-aspartate = AMP + diphosphate + 2-(Nomega-L-arginino)succinate
detailed catalytic mechanism, stereochemistry
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
amination
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
MetaCyc
canavanine biosynthesis, L-arginine biosynthesis I (via L-ornithine), L-arginine biosynthesis II (acetyl cycle), L-arginine biosynthesis III (via N-acetyl-L-citrulline), L-arginine biosynthesis IV (archaea), nitric oxide biosynthesis II (mammals), urea cycle
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SYSTEMATIC NAME
IUBMB Comments
L-citrulline:L-aspartate ligase (AMP-forming)
-
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CAS REGISTRY NUMBER
COMMENTARY
9023-58-9
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + L-citrulline + 3-nitro-2-aminopropanoate
?
-
Substrates: 60% of the maximal activity with Asp
Products: -
Products: -
?
dATP + L-citrulline + L-Asp
dAMP + diphosphate + L-argininosuccinate
-
Substrates: 2.6% as active as ATP
Products: -
Products: -
?
ATP + citrulline + aspartate
AMP + diphosphate + 2-(Nomega-L-arginino)succinate
-
Substrates: -
Products: -
Products: -
?
ATP + citrulline + aspartate
AMP + diphosphate + 2-(Nomega-L-arginino)succinate
-
Substrates: -
Products: -
Products: -
?
ATP + citrulline + aspartate
AMP + diphosphate + 2-(Nomega-L-arginino)succinate
Substrates: assay at pH 7.8, 37°C, reaction stopped by addition of molybdate buffer
Products: -
Products: -
?
ATP + citrulline + aspartate
AMP + diphosphate + 2-(Nomega-L-arginino)succinate
-
Substrates: -
Products: -
Products: -
?
ATP + L-citrulline + L-Asp
?
-
Substrates: mechanism to recycle citrulline, formed in the nervous system via nitric oxide synthetase, EC 1.14.13.39, activity, back to the nitric oxide precursor, L-Arg
Products: -
Products: -
?
ATP + L-citrulline + L-Asp
?
-
Substrates: third reaction of urea cycle
Products: -
Products: -
?
ATP + L-citrulline + L-Asp
?
-
Substrates: anabolic function in biosynthesis of Arg and catabolic function as the first enzyme of citrulline utilization as nitrogen source
Products: -
Products: -
?
ATP + L-citrulline + L-Asp
?
-
Substrates: anabolic function in biosynthesis of Arg and catabolic function as the first enzyme of citrulline utilization as nitrogen source
Products: -
Products: -
?
ATP + L-citrulline + L-Asp
AMP + diphosphate + L-argininosuccinate
-
Substrates: -
Products: -
Products: -
?
ATP + L-citrulline + L-Asp
AMP + diphosphate + L-argininosuccinate
-
Substrates: r
Products: -
Products: -
?
ATP + L-citrulline + L-Asp
AMP + diphosphate + L-argininosuccinate
-
Substrates: D-Asp is inactive as substrate
Products: -
Products: -
?
ATP + L-citrulline + L-Asp
AMP + diphosphate + L-argininosuccinate
-
Substrates: argininosuccinate synthase expression is required to maintain nitric oxide production and cell viability in aortic endothelial cells
Products: -
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?
ATP + L-citrulline + L-Asp
AMP + diphosphate + L-argininosuccinate
-
Substrates: argininosuccinate synthase catalyzes the rate-limiting step in the recycling of citrulline to arginine, which in endothelial cells, is tighly coupled to the production of nitric oxide. The upstream open reading frame found in the extended, overlapping 5'-untranslated region of argininosuccinate synthase mRNA species suppresses endothelial argininosuccinate expression providing a novel mechanism for regulating endothelial NO production by limiting the availability of arginine
Products: -
Products: -
?
ATP + L-citrulline + L-Asp
AMP + diphosphate + L-argininosuccinate
-
Substrates: -
Products: -
Products: -
?
ATP + L-citrulline + L-Asp
AMP + diphosphate + L-argininosuccinate
-
Substrates: -
Products: -
Products: -
?
ATP + L-citrulline + L-Asp
AMP + diphosphate + L-argininosuccinate
-
Substrates: the substrate for NO synthesis, L-arginine can be regenerated from the L-citrulline the coproduct of nitric-oxide synthase. This requires the sequential action of two enzymes, argininosuccinate synthetase and argininosuccinate lyase
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?
ATP + L-citrulline + L-Asp
AMP + diphosphate + L-argininosuccinate
-
Substrates: IL-1beta stimulates argininosuccinate synthetase gene expression through NF-kappaB in Caco-2 cells
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?
ATP + L-citrulline + L-Asp
AMP + diphosphate + L-argininosuccinate
-
Substrates: -
Products: -
Products: -
?
ATP + L-citrulline + L-Asp
AMP + diphosphate + L-argininosuccinate
-
Substrates: -
Products: -
Products: -
?
ATP + L-citrulline + L-Asp
AMP + diphosphate + L-argininosuccinate
-
Substrates: -
Products: -
Products: -
?
ATP + L-citrulline + L-Asp
AMP + diphosphate + L-argininosuccinate
-
Substrates: r
Products: -
Products: -
?
ATP + L-citrulline + L-Asp
AMP + diphosphate + L-argininosuccinate
-
Substrates: r
Products: -
Products: -
?
ATP + L-citrulline + L-Asp
AMP + diphosphate + L-argininosuccinate
-
Substrates: r
Products: -
Products: -
?
ATP + L-citrulline + L-Asp
AMP + diphosphate + L-argininosuccinate
-
Substrates: -
Products: -
Products: -
?
ATP + L-citrulline + L-aspartate
AMP + diphosphate + 2-(Nomega-L-arginino)succinate
-
Substrates: argininosuccinate synthase is essential for endothelial nitric oxide production, vascular NO production is regulated by dynamic argininosuccinate synthase phosphorylation
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?
ATP + L-citrulline + L-aspartate
AMP + diphosphate + 2-(Nomega-L-arginino)succinate
-
Substrates: the caveolar-localized endothelial argininosuccinate synthase catalyzes the rate-limiting step of the citrulline-NO cycle, involving not only the regulation of endothelial nitric oxide synthase, but also regulation of cycle, overview
Products: -
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?
ATP + L-citrulline + L-aspartate
AMP + diphosphate + 2-(Nomega-L-arginino)succinate
-
Substrates: -
Products: -
Products: -
?
ATP + L-citrulline + L-aspartate
AMP + diphosphate + 2-(Nomega-L-arginino)succinate
Substrates: citrulline-aspartate ligase is the rate-limiting enzyme in the synthesis of the amino acid arginine. Type I citrullinaemia is a disorder caused by mutations in the ASS gene leading to reduced or abolished activity of the ASS enzyme
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?
ATP + L-citrulline + L-aspartate
AMP + diphosphate + 2-(Nomega-L-arginino)succinate
-
Substrates: the key enzyme in the urea cycle participates in many metabolic processes including arginine biosynthesis and the citrulline-nitric oxide cycle
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?
ATP + L-citrulline + L-aspartate
AMP + diphosphate + 2-(Nomega-L-arginino)succinate
-
Substrates: -
Products: -
Products: -
?
ATP + L-citrulline + L-aspartate
AMP + diphosphate + 2-(Nomega-L-arginino)succinate
Substrates: rate-limiting enzyme in nitric oxide synthesis, negative feedback mechanism, overview
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Products: -
?
ATP + L-citrulline + L-aspartate
AMP + diphosphate + 2-(Nomega-L-arginino)succinate
Substrates: substrate binding structures, overview
Products: -
Products: -
?
ATP + L-citrulline + L-aspartate
AMP + diphosphate + 2-(Nomega-L-arginino)succinate
-
Substrates: -
Products: -
Products: -
?
ATP + L-citrulline + L-aspartate
AMP + diphosphate + 2-(Nomega-L-arginino)succinate
Substrates: -
Products: -
Products: -
?
ATP + L-citrulline + L-aspartate
AMP + diphosphate + 2-(Nomega-L-arginino)succinate
Substrates: -
Products: -
Products: -
?
ATP + L-citrulline + L-aspartate
AMP + diphosphate + 2-(Nomega-L-arginino)succinate
Substrates: the enzyme plays an important role as the rate-limiting step required for converting L-citrulline to argininosuccinate to provide arginine
Products: -
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?
ATP + L-citrulline + L-aspartate
AMP + diphosphate + 2-(Nomega-L-arginino)succinate
Substrates: -
Products: -
Products: -
?
ATP + L-citrulline + L-aspartate
AMP + diphosphate + 2-(Nomega-L-arginino)succinate
Substrates: the enzyme plays an important role as the rate-limiting step required for converting L-citrulline to argininosuccinate to provide arginine
Products: -
Products: -
?
ATP + L-citrulline + L-aspartate
AMP + diphosphate + 2-(Nomega-L-arginino)succinate
Substrates: -
Products: -
Products: -
?
ATP + L-citrulline + L-aspartate
AMP + diphosphate + 2-(Nomega-L-arginino)succinate
-
Substrates: rate-limiting enzyme of the urea cycle
Products: -
Products: -
?
ATP + L-citrulline + L-aspartate
AMP + diphosphate + 2-(Nomega-L-arginino)succinate
-
Substrates: -
Products: -
Products: -
?
ATP + L-citrulline + L-aspartate
AMP + diphosphate + 2-(Nomega-L-arginino)succinate
-
Substrates: -
Products: -
Products: -
?
ATP + L-citrulline + L-aspartate
AMP + diphosphate + 2-(Nomega-L-arginino)succinate
-
Substrates: Sulfolobus solfataricus lacks ornithine acetyltransferase and thus forms N-acetylglutamate exclusively via the energetically less favourable reaction catalysed by N-acetylglutamate synthase, investing 1 mol of acetyl CoA per mol of N-acetyl intermediate synthesized
Products: -
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?
ATP + L-citrulline + L-aspartate
AMP + diphosphate + 2-(Nomega-L-arginino)succinate
-
Substrates: -
Products: -
Products: -
?
ATP + L-citrulline + L-aspartate
AMP + diphosphate + 2-(Nomega-L-arginino)succinate
-
Substrates: Sulfolobus solfataricus lacks ornithine acetyltransferase and thus forms N-acetylglutamate exclusively via the energetically less favourable reaction catalysed by N-acetylglutamate synthase, investing 1 mol of acetyl CoA per mol of N-acetyl intermediate synthesized
Products: -
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?
ATP + L-citrulline + L-aspartate
AMP + diphosphate + L-argininosuccinate
-
Substrates: catalyzes the coupling reaction between citrulline and arginine to form argininosuccinic acid
Products: -
Products: -
?
ATP + L-citrulline + L-aspartate
AMP + diphosphate + L-argininosuccinate
-
Substrates: the rate-limiting enzyme for converting citrulline to arginine
Products: -
Products: -
?
ATP + L-citrulline + L-aspartate
AMP + diphosphate + L-argininosuccinate
-
Substrates: ATP induces conformational changes in the nucleotide binding domain, each monomer of tetrameric EAS consists of a nucleotide binding domain and a novel catalytic/multimerization domain, detailed catalytic mechanism via adenylated citrulline intermediate, active site structure
Products: -
Products: -
r
ATP + L-citrulline + L-aspartate
AMP + diphosphate + L-argininosuccinate
-
Substrates: ATP-dependent ligation of citrulline and aspartate
Products: -
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r
ATP + L-citrulline + L-aspartate
AMP + diphosphate + L-argininosuccinate
-
Substrates: penultimate step in the biosnthesis of arginine, rate-limiting enzyme of both the urea and arginine-citrulline cycles
Products: -
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?
ATP + L-citrulline + L-aspartate
AMP + diphosphate + L-argininosuccinate
-
Substrates: -
Products: -
Products: -
?
ATP + L-citrulline + L-aspartate
AMP + diphosphate + L-argininosuccinate
-
Substrates: catalyzes the coupling reaction between citrulline and arginine to form argininosuccinic acid
Products: -
Products: -
?
ATP + L-citrulline + L-aspartate
AMP + diphosphate + L-argininosuccinate
-
Substrates: the rate-limiting enzyme for converting citrulline to arginine
Products: -
Products: -
?
ATP + L-citrulline + L-aspartate
AMP + diphosphate + L-argininosuccinate
-
Substrates: catalyzes the coupling reaction between citrulline and arginine to form argininosuccinic acid
Products: -
Products: -
?
ATP + L-citrulline + L-aspartate
AMP + diphosphate + L-argininosuccinate
-
Substrates: the rate-limiting enzyme for converting citrulline to arginine
Products: -
Products: -
?
ATP + L-citrulline + L-aspartate
AMP + diphosphate + L-argininosuccinate
-
Substrates: -
Products: -
Products: -
?
ATP + L-citrulline + L-aspartate
AMP + diphosphate + L-argininosuccinate
-
Substrates: -
Products: -
Products: -
?
ATP + L-citrulline + L-aspartate
AMP + diphosphate + L-argininosuccinate
-
Substrates: mediates transformation of L-citrulline to L-arginine in the ureum cycle in hepatocytes, first step in L-citrulline recycling pathway
Products: -
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?
ATP + L-citrulline + L-aspartate
AMP + diphosphate + L-argininosuccinate
-
Substrates: -
Products: -
Products: -
?
ATP + L-citrulline + L-aspartate
AMP + diphosphate + L-argininosuccinate
Substrates: ATP-dependent condensation of citrulline with aspartate, detailed mechanism via citrullyl-AMP intermediate, stereochemistry of catalysis, no conformational change upon binding of ATP, active site structure
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r
ATP + L-citrulline + L-aspartate
AMP + diphosphate + L-argininosuccinate
-
Substrates: ATP-dependent condensation of citrulline with aspartate, no conformational change upon binding of substrates, mechanism via citrullyl-AMP intermediate, active site structure
Products: -
Products: -
r
ATP + L-citrulline + L-aspartate
AMP + diphosphate + L-argininosuccinate
-
Substrates: second step of urea cycle
Products: -
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?
ATP + L-citrulline + L-aspartate
AMP + diphosphate + L-argininosuccinate
Substrates: seventh step of the arginine biosynthesis, second step of the urea cycle
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?
ATP + L-citrulline + L-aspartate
AMP + diphosphate + L-argininosuccinate
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
Substrates: ATP-dependent condensation of citrulline with aspartate, no conformational change upon binding of substrates, mechanism via citrullyl-AMP intermediate, active site structure
Products: -
Products: -
r
ATP + L-citrulline + L-aspartate
AMP + diphosphate + L-argininosuccinate
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
Substrates: second step of urea cycle
Products: -
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?
ATP + L-citrulline + L-aspartate
AMP + diphosphate + L-argininosuccinate
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
Substrates: ATP-dependent condensation of citrulline with aspartate, detailed mechanism via citrullyl-AMP intermediate, stereochemistry of catalysis, no conformational change upon binding of ATP, active site structure
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Products: -
r
ATP + L-citrulline + L-aspartate
AMP + diphosphate + L-argininosuccinate
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
Substrates: seventh step of the arginine biosynthesis, second step of the urea cycle
Products: -
Products: -
?
additional information
?
-
-
Substrates: rate-limiting enzyme in the metabolic pathway leading from L-citrulline to L-arginine, urea cycle
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?
additional information
?
-
-
Substrates: citrullinemia is an autosomal recessive disease caused by a deficiency of argininosuccinate synthetase
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?
additional information
?
-
-
Substrates: adult-type citrullinemia with neuro-psychiatric symptoms of late onset, 24-28 years old, caused by argininosuccinate synthetase abnormalities
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additional information
?
-
Substrates: in mammals, the urea-cycle enzymes ASS and argininosuccinatelyase are part of an additional pathway together with the enzyme nitric oxide synthase, forming the arginine-citrulline cycle
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additional information
?
-
-
Substrates: in mammals, the urea-cycle enzymes ASS and argininosuccinatelyase are part of an additional pathway together with the enzyme nitric oxide synthase, forming the arginine-citrulline cycle
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?
additional information
?
-
-
Substrates: factors like diets, hormones and pro-inflammatory stimuli regulate ASS gene expression primarily at the transcription level
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Products: -
?
additional information
?
-
-
Substrates: pancreatic cancer cell lines deficient in argininosuccinate synthetase are sensitive to arginine deprivation by arginine deiminase
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?
additional information
?
-
Substrates: the enzyme interacts and cooperates with NADPH sensor protein, HSCARG, in downregulation of nitric oxide synthesis, the enzyme interacts with the dimerization region of HSCARG, amino acid residues 153-189, HSCARG regulation of AS activity is crucial for maintaining the intracellular balance between redox state and nitric oxide levels, overview
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?
additional information
?
-
-
Substrates: involved in L-arginine synthesis from L-citrulline, urea cycle, rate-limiting enzyme for high output NO generation, inducible enzyme, AS synthesis is more strictly regulated at the posttranscriptional than the transcriptional level in vivo
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?
additional information
?
-
-
Substrates: urea cycle, enzyme of citrulline-arginine recycling, which is important for high output production of NO in activated microglial cells, inducible enzyme
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?
additional information
?
-
-
Substrates: ASS binds to and inactivates lipopolysaccharide and lipid A, overview
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?
additional information
?
-
-
Substrates: involved in the recycling of L-citrulline to L-arginine
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Products: -
?
additional information
?
-
-
Substrates: urea cycle, enzyme of citrulline-arginine recycling, which is important for high output production of NO in activated microglial cells, inducible enzyme
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + L-citrulline + L-Asp
?
-
Substrates: mechanism to recycle citrulline, formed in the nervous system via nitric oxide synthetase, EC 1.14.13.39, activity, back to the nitric oxide precursor, L-Arg
Products: -
Products: -
?
ATP + L-citrulline + L-Asp
?
-
Substrates: third reaction of urea cycle
Products: -
Products: -
?
ATP + L-citrulline + L-Asp
?
-
Substrates: anabolic function in biosynthesis of Arg and catabolic function as the first enzyme of citrulline utilization as nitrogen source
Products: -
Products: -
?
ATP + L-citrulline + L-Asp
?
-
Substrates: anabolic function in biosynthesis of Arg and catabolic function as the first enzyme of citrulline utilization as nitrogen source
Products: -
Products: -
?
ATP + L-citrulline + L-Asp
AMP + diphosphate + L-argininosuccinate
-
Substrates: argininosuccinate synthase expression is required to maintain nitric oxide production and cell viability in aortic endothelial cells
Products: -
Products: -
?
ATP + L-citrulline + L-Asp
AMP + diphosphate + L-argininosuccinate
-
Substrates: argininosuccinate synthase catalyzes the rate-limiting step in the recycling of citrulline to arginine, which in endothelial cells, is tighly coupled to the production of nitric oxide. The upstream open reading frame found in the extended, overlapping 5'-untranslated region of argininosuccinate synthase mRNA species suppresses endothelial argininosuccinate expression providing a novel mechanism for regulating endothelial NO production by limiting the availability of arginine
Products: -
Products: -
?
ATP + L-citrulline + L-Asp
AMP + diphosphate + L-argininosuccinate
-
Substrates: the substrate for NO synthesis, L-arginine can be regenerated from the L-citrulline the coproduct of nitric-oxide synthase. This requires the sequential action of two enzymes, argininosuccinate synthetase and argininosuccinate lyase
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ATP + L-citrulline + L-Asp
AMP + diphosphate + L-argininosuccinate
-
Substrates: IL-1beta stimulates argininosuccinate synthetase gene expression through NF-kappaB in Caco-2 cells
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ATP + L-citrulline + L-aspartate
AMP + diphosphate + 2-(Nomega-L-arginino)succinate
-
Substrates: argininosuccinate synthase is essential for endothelial nitric oxide production, vascular NO production is regulated by dynamic argininosuccinate synthase phosphorylation
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ATP + L-citrulline + L-aspartate
AMP + diphosphate + 2-(Nomega-L-arginino)succinate
-
Substrates: the caveolar-localized endothelial argininosuccinate synthase catalyzes the rate-limiting step of the citrulline-NO cycle, involving not only the regulation of endothelial nitric oxide synthase, but also regulation of cycle, overview
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ATP + L-citrulline + L-aspartate
AMP + diphosphate + 2-(Nomega-L-arginino)succinate
Substrates: citrulline-aspartate ligase is the rate-limiting enzyme in the synthesis of the amino acid arginine. Type I citrullinaemia is a disorder caused by mutations in the ASS gene leading to reduced or abolished activity of the ASS enzyme
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ATP + L-citrulline + L-aspartate
AMP + diphosphate + 2-(Nomega-L-arginino)succinate
-
Substrates: the key enzyme in the urea cycle participates in many metabolic processes including arginine biosynthesis and the citrulline-nitric oxide cycle
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ATP + L-citrulline + L-aspartate
AMP + diphosphate + 2-(Nomega-L-arginino)succinate
-
Substrates: -
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ATP + L-citrulline + L-aspartate
AMP + diphosphate + 2-(Nomega-L-arginino)succinate
Substrates: rate-limiting enzyme in nitric oxide synthesis, negative feedback mechanism, overview
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ATP + L-citrulline + L-aspartate
AMP + diphosphate + 2-(Nomega-L-arginino)succinate
Substrates: -
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ATP + L-citrulline + L-aspartate
AMP + diphosphate + 2-(Nomega-L-arginino)succinate
Substrates: the enzyme plays an important role as the rate-limiting step required for converting L-citrulline to argininosuccinate to provide arginine
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ATP + L-citrulline + L-aspartate
AMP + diphosphate + 2-(Nomega-L-arginino)succinate
Substrates: the enzyme plays an important role as the rate-limiting step required for converting L-citrulline to argininosuccinate to provide arginine
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ATP + L-citrulline + L-aspartate
AMP + diphosphate + 2-(Nomega-L-arginino)succinate
-
Substrates: rate-limiting enzyme of the urea cycle
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ATP + L-citrulline + L-aspartate
AMP + diphosphate + 2-(Nomega-L-arginino)succinate
-
Substrates: -
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ATP + L-citrulline + L-aspartate
AMP + diphosphate + 2-(Nomega-L-arginino)succinate
-
Substrates: Sulfolobus solfataricus lacks ornithine acetyltransferase and thus forms N-acetylglutamate exclusively via the energetically less favourable reaction catalysed by N-acetylglutamate synthase, investing 1 mol of acetyl CoA per mol of N-acetyl intermediate synthesized
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ATP + L-citrulline + L-aspartate
AMP + diphosphate + 2-(Nomega-L-arginino)succinate
-
Substrates: Sulfolobus solfataricus lacks ornithine acetyltransferase and thus forms N-acetylglutamate exclusively via the energetically less favourable reaction catalysed by N-acetylglutamate synthase, investing 1 mol of acetyl CoA per mol of N-acetyl intermediate synthesized
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ATP + L-citrulline + L-aspartate
AMP + diphosphate + L-argininosuccinate
-
Substrates: the rate-limiting enzyme for converting citrulline to arginine
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ATP + L-citrulline + L-aspartate
AMP + diphosphate + L-argininosuccinate
-
Substrates: penultimate step in the biosnthesis of arginine, rate-limiting enzyme of both the urea and arginine-citrulline cycles
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ATP + L-citrulline + L-aspartate
AMP + diphosphate + L-argininosuccinate
-
Substrates: the rate-limiting enzyme for converting citrulline to arginine
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ATP + L-citrulline + L-aspartate
AMP + diphosphate + L-argininosuccinate
-
Substrates: the rate-limiting enzyme for converting citrulline to arginine
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ATP + L-citrulline + L-aspartate
AMP + diphosphate + L-argininosuccinate
-
Substrates: mediates transformation of L-citrulline to L-arginine in the ureum cycle in hepatocytes, first step in L-citrulline recycling pathway
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ATP + L-citrulline + L-aspartate
AMP + diphosphate + L-argininosuccinate
-
Substrates: second step of urea cycle
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ATP + L-citrulline + L-aspartate
AMP + diphosphate + L-argininosuccinate
Substrates: seventh step of the arginine biosynthesis, second step of the urea cycle
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ATP + L-citrulline + L-aspartate
AMP + diphosphate + L-argininosuccinate
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
Substrates: second step of urea cycle
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ATP + L-citrulline + L-aspartate
AMP + diphosphate + L-argininosuccinate
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
Substrates: seventh step of the arginine biosynthesis, second step of the urea cycle
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?
additional information
?
-
-
Substrates: rate-limiting enzyme in the metabolic pathway leading from L-citrulline to L-arginine, urea cycle
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?
additional information
?
-
-
Substrates: citrullinemia is an autosomal recessive disease caused by a deficiency of argininosuccinate synthetase
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?
additional information
?
-
-
Substrates: adult-type citrullinemia with neuro-psychiatric symptoms of late onset, 24-28 years old, caused by argininosuccinate synthetase abnormalities
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?
additional information
?
-
Substrates: in mammals, the urea-cycle enzymes ASS and argininosuccinatelyase are part of an additional pathway together with the enzyme nitric oxide synthase, forming the arginine-citrulline cycle
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additional information
?
-
-
Substrates: in mammals, the urea-cycle enzymes ASS and argininosuccinatelyase are part of an additional pathway together with the enzyme nitric oxide synthase, forming the arginine-citrulline cycle
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?
additional information
?
-
-
Substrates: factors like diets, hormones and pro-inflammatory stimuli regulate ASS gene expression primarily at the transcription level
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?
additional information
?
-
-
Substrates: pancreatic cancer cell lines deficient in argininosuccinate synthetase are sensitive to arginine deprivation by arginine deiminase
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?
additional information
?
-
Substrates: the enzyme interacts and cooperates with NADPH sensor protein, HSCARG, in downregulation of nitric oxide synthesis, the enzyme interacts with the dimerization region of HSCARG, amino acid residues 153-189, HSCARG regulation of AS activity is crucial for maintaining the intracellular balance between redox state and nitric oxide levels, overview
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?
additional information
?
-
-
Substrates: involved in L-arginine synthesis from L-citrulline, urea cycle, rate-limiting enzyme for high output NO generation, inducible enzyme, AS synthesis is more strictly regulated at the posttranscriptional than the transcriptional level in vivo
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?
additional information
?
-
-
Substrates: urea cycle, enzyme of citrulline-arginine recycling, which is important for high output production of NO in activated microglial cells, inducible enzyme
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?
additional information
?
-
-
Substrates: ASS binds to and inactivates lipopolysaccharide and lipid A, overview
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?
additional information
?
-
-
Substrates: involved in the recycling of L-citrulline to L-arginine
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additional information
?
-
-
Substrates: urea cycle, enzyme of citrulline-arginine recycling, which is important for high output production of NO in activated microglial cells, inducible enzyme
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Mg2+
required for maximal activity, in octahedral coordination with 3 oxygen atoms of the triphosphate group and 3 water molecules
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
diphosphoryl lipid A (DPL)
-
DPL from Escherichia coli, inhibits argininosuccinate synthetase in a dose-dependent manner, concentration for half inhibition of argininosuccinate synthetase enzyme activity: 0.039 mg/ml
-
IL-1beta
-
a long-term 24 h exposure of ASS to IL-1beta in Caco-2 cells inhibits its activity. The inhibiting effect of IL-1beta is linked to the production of nitric oxide (NO) induced by IL-1beta. The inhibiting effect is totally blocked in the presence of N-methyl-L-arginine an inhibitor of the inducible nitric oxide synthase or by culturing the cells in an arginine-deprived medium
-
monophosphoryl lipid A (MPL)
-
MPL from Escherichia coli, inhibits argininosuccinate synthetase in a dose-dependent manner, concentration for half inhibition of argininosuccinate synthetase enzyme activity: 0.270 mg/ml
-
N-methylaspartic acid
at 1 mM methyl-DL-aspartic acid the enzyme activity is reduced by about 60%, while at 5 mM the catalytic activity is completely abolished
NO
-
mediates reversible S-nitrosylation and inactivation of argininosuccinate synthetase in vitro and in lipopolysaccharide-treated cells and mice. S-nitrosylation of Cys132 is noth necessary and sufficient for the inhibition of argininosuccinate synthase by NO donors
R-lipopolysaccharide (LPS)
-
rough-type LPS from Escherichia coli, inhibits argininosuccinate synthetase in a dose-dependent manner, concentration for half inhibition of argininosuccinate synthetase enzyme activity: 0.230 mg/ml
-
recombinant mycoplasma arginine deiminase
-
36% decrease in AS activity after rADI treatment
-
S-lipopolysaccharide (LPS)
-
smooth-type-LPS from Escherichia coli, inhibits argininosuccinate synthetase in a dose-dependent manner, concentration for half inhibition of argininosuccinate synthetase enzyme activity: 0.024 mg/ml
-
sodium 2-deoxy-2-(3S-(9-phenyl-nonanoyl-oxy) tetradecanoyl) amino-3-O-(9-phenyl-nonanoyl)-D-glucopyranose 4-sulfate
-
synthesized lipid A analog, inhibits argininosuccinate synthetase in a dose-dependent manner, concentration for half inhibition of argininosuccinate synthetase enzyme activity: 0.0065 mg/ml
alpha-methyl-DL-aspartic acid
specific inhibitor for Ass1, can significantly increase the rate of embryonic reabsorption
additional information
-
1-D-ribofuranosylbenzimidazole suppresses enzyme expression
-
additional information
-
study of the effect of recombinant mycoplasma arginine deiminase on cell proliferation, correlation of the low resistance to this treatment with a low AS activity in the sensitive cell line
-
additional information
-
pancreatic cancer cell lines deficient in argininosuccinate synthetase are sensitive to arginine deprivation by arginine deiminase, overview
-
additional information
-
study of the effect of recombinant mycoplasma arginine deiminase on cell proliferation, good correlation of the high resistance to this treatment with a high AS activity in the cell line
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(2R,3aS,5aR,5bS,9S,13S,14R,16aS,16bR)-9-ethyl-13-[[(2R,5S,6R)-5-[[2-hydroxy-3-(piperazin-1-yl)propyl](methyl)amino]-6-methyloxan-2-yl]oxy]-14-methyl-7,15-dioxo-2,3,3a,5a,5b,6,7,9,10,11,12,13,14,15,16a,16b-hexadecahydro-1H-as-indaceno[3,2-d]oxacyclododecin-2-yl 6-deoxy-2,3,4-tri-O-methyl-alpha-L-mannopyranoside
compound suppresses breast tumor cell proliferation and growth by binding to and activating ASS1. The C13-C14 double bond in the compound and the Cys97 site in ASS1 are critical for the interaction with ASS1. The initial binding step is the noncovalent reversible binding to ASS1, which places the moderately reactive electrophile of the compound close to a specific nucleophile on the ASS1 protein. The second chemical step is irreversible, leading to specific covalent linkage and the complex activation
-
Bradykinin-potentiating peptide 10c
i.e. ENWPHPQIPP, BBP-10c. Pre-treatment of cells significantly reduces cell death induced by H2O2. The peptide reduces ROS generation and lipid peroxidation in relation to cells treated only with H2O2. BBP-10c increases ASS expression and is not neuroprotective in the presence of inhibitor alpha-methyl-DL-aspartic acid
-
Bradykinin-potentiating peptide 12b
i.e. EWGRPPGPPIPP, BBP-12b. Pr-treatment of cells significantly reduces cell death induced by H2O2
-
IL-1beta
-
ASS is rapidly induced by a short time exposure of IL-1beta to Caco-2 cells. By contrast, a long-term 24 h exposure to IL-1beta inhibited the ASS activity despite an increase in both specific mRNA-level and protein amount, demonstrating a post-translational effect
-
recombinant mycoplasma arginine deiminase
-
350% increase in AS activity in HeLa cells after rADI treatment, no activity change in umbilical vein endothelial cells
-
spinosyn A
compound suppresses breast tumor cell proliferation and growth by binding to and activating ASS1. The C13-C14 double bond in the compound and the Cys97 site in ASS1 are critical for the interaction with ASS1. The initial binding step is the noncovalent reversible binding to ASS1, which places the moderately reactive electrophile of the compound close to a specific nucleophile on the ASS1 protein. The second chemical step is irreversible, leading to specific covalent linkage and the complex activation
lipopolysaccharide
argininosuccinate synthase accumulates in circulation within 1 h after treatment with both lipopolysaccharide alone and hepatotoxic combination of lipopolysaccharide and D-Galactosamine. Enzyme physically binds to lipopolysaccharide
lipopolysaccharide
-
argininosuccinate synthase accumulates in circulation within 1 h after treatment with both lipopolysaccharide alone and hepatotoxic combination of lipopolysaccharide and D-Galactosamine. Enzyme physically binds to lipopolysaccharide
additional information
-
troglitazone, a PPARgamma ligand, and thiazolidinedione up-regulate vascular endothelial argininosuccinate synthase expression, quantitative real time RT-PCR, overview
-
additional information
-
study of the effect of recombinant mycoplasma arginine deiminase on cell proliferation, good correlation of the resistance to this treatment with the AS activity in the cell lines
-
additional information
-
CRE-1 is the cis-element responsible for liver-specific cAMP induction of the human ASS gene
-
additional information
-
interaction with Bj-BPP-10c, snake venom anti-hypertensive peptide of Botrops jararaca, activates the catalytic activity of argininosuccinate snythetase in a dose-dependent manner
-
additional information
-
inducible enzyme, immunostimulation of AS synthesis with lipopolysaccharide or cytokines, such as TNF-alpha, interleukin 1 and interferon-gamma
-
additional information
-
AS mRNA is 4-6fold induced by Escherichia coli lipopolysaccharide and mouse interferon-gamma, kinetics of induction
-
additional information
interaction with Bj-BPP-10c, snake venom anti-hypertensive peptide of Botrops jararaca, activates the catalytic activity of argininosuccinate snythetase in a dose-dependent manner
-
additional information
-
AS mRNA is induced by Escherichia coli lipopolysaccharide and mouse interferon-gamma
-
additional information
-
expression of argininosuccinate synthetase mRNA is inducible by lipopolysaccharides
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
ATP: biphasic double-reciprocal plot
-
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
Mus musculus
-
substrate: S-lipopolysaccharide, IC50: 0.024 mg/ml
-
additional information
additional information
Mus musculus
-
substrate: R-lipopolysaccharide, IC50: 0.230 mg/ml
-
additional information
additional information
Mus musculus
-
substrate: monophosphoryl lipid A, IC50: 0.270 mg/ml
-
additional information
additional information
Mus musculus
-
substrate: diphosphoryl lipid A, IC50: 0.039 mg/ml
-
additional information
additional information
Mus musculus
-
substrate: sodium 2-deoxy-2-(3S-(9-phenyl-nonanoyl-oxy) tetradecanoyl) amino-3-O-(p-phenyl-nonanoyl)-D-glucopyranose 4-sulfate (ONO-4007), IC50: 0.0065 mg/ml
-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.0002
-
pH 8.7, 70°C, activity in cell culture in growth medium 0.5% peptone and 0.1% yeast extract
0.00045
-
pH 8.7, 70°C, activity in cell culture in growth medium with 0.2% yeast extract
0.0007
-
pH 8.7, 70°C, activity in cell culture in minimal growth medium with 20 mM glucose and 5 mM NH4+
0.002
-
in the presence of 5 mM (NH4)2SO4 and after addition of 20 mM L-norvaline in root-free compartments
0.0028
-
in the presence of 5 mM (NH4)2SO4 and after addition of 20 mM L-norvaline in the root-free compartments
0.0071
-
in the presence of 5 mM (NH4)2SO4 and after addition of 0.5 mM phenyl phosphorodiamidate in root-free compartments
0.0166
0.049
1
-
specific activity of ASS in Caco-2 cells after long time exposure (24h) to 1 ng/ml IL-1beta
1.27
-
specific activity of ASS in Caco-2 cells after the addition of 0.5 mM S-nitroso-acetylpenicillamine for 24h, an NO donor. This clearly demonstrates that NO induces an inhibition of the ASS activity in Caco-2 cells.
2.5
-
specific activity of ASS in Caco-2 cells after short time exposure (4h) to 1 ng/ml IL-1beta
0.049
-
in the presence of 5 mM (NH4)2SO4 in the root-free compartments
0.049
-
in the presence of 5 mM (NH4)2SO4 and after addition of 0.5 mM phenyl phosphorodiamidate in the root-free compartments
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
7.8
8.7
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5 - 8.5
-
6.5: about 55% of maximal activity, 8.5: about 70% of maximal activity, reaction of ATP + citrulline + L-argininosuccinate
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
26
37
70
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
antimonial-sensitive and antimonial-resistant strains
UniProt
brenda
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
-
-
brenda
-
UniProt
brenda
adult-type citrullinemia with neuro-psychiatric symptoms of late onset, 24-28 years old, caused by ASS abnormalities
-
-
brenda
citrullinemia is an autosomal recessive disease caused by a deficiency of argininosuccinate synthetase
-
-
brenda
patients with Alzheimer disease and nondemented, age-matched controls
-
-
brenda
human tumor necrosis factor-alpha transgenic mice, 4 and 8 weeks old, and age-matched CBA x C57B1/6 wild-type controls
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
more abundantly expressed in amastigotes than in promastigotes
brenda
Northern analyses of ass during fruiting body formation and post-harvest development reveals that expression is significantly up-regulated from developmental stage 3 on for all the tissues studied (gills, stip and cap). The expression reaches a maximum at the later stages of fruiting body growth, stages 6 and 7
brenda
-
in a rat ischemia model the striatum is examined at 24, 72 and 144 h after reperfusion and compared with rats in normal conditions. At 24 h after reperfusion, the number of the nitric oxide synthase-positive neurons and the percentage of those co-expressing argininosuccinate synthetase and argininsuccinate lyase and nitric oxide synthase are significantly increased in the animals with a longer survival
brenda
Ass1 is highly expressed in mouse decidua and uterine stromal cells undergoing decidualization, and argininosuccinate lyase Asl is weakly expressed in mouse decidua and uterine stromal cells undergoing decidualization
brenda
-
expression analysis is performed in bovine aortic endothelial cells (BAEC)
brenda
Northern analyses of ass during fruiting body formation and post-harvest development reveals that expression is significantly up-regulated from developmental stage 3 on for all the tissues studied (gills, stip and cap). The expression reaches a maximum at the later stages of fruiting body growth, stages 6 and 7
brenda
-
parental cell line MGL8B2 and canavanine-resistant cell line MGL8D1
brenda
primary embryonic metanephric mesenchymal cells
brenda
-
pancreatic cancer cell line, very low ASS expression level
brenda
-
increased co-expression of AS and TNF-a mRNA is observed in non-small cell lung and stomach cancer, compared with normal corresponding tissues
brenda
-
pancreatic cancer cell line, low ASS expression level
brenda
argininosuccinate synthase accumulates in circulation within 1 h after treatment with both lipopolysaccharide alone and hepatotoxic combination of lipopolysaccharide and D-Galactosamine
brenda
decrease in Ass mRNA expression level during aestivation, accompanied with decreases in the concentrations of arginine and NO
brenda
Northern analyses of ass during fruiting body formation and post-harvest development reveals that expression is significantly up-regulated from developmental stage 3 on for all the tissues studied (gills, stip and cap). The expression reaches a maximum at the later stages of fruiting body growth, stages 6 and 7
brenda
-
increased co-expression of AS and TNF-a mRNA is observed in non-small cell lung and stomach cancer, compared with normal corresponding tissues
brenda
Ass1 is highly expressed in mouse decidua and uterine stromal cells undergoing decidualization, and argininosuccinate lyase Asl is weakly expressed in mouse decidua and uterine stromal cells undergoing decidualization
brenda
additional information
changes in Ass and Asl mRNA expression levels during the three phases of aestivation can be related to the supply of arginine for NO synthesis
brenda
significant decrease in Ass mRNA expression level after 6 months of aestivation
brenda
strong expression of both argininosuccinate synthase and argininosuccinate lyase. mRNA expression levels of Ass and Asl increase significantly during the induction phase of aestivation
brenda
-
AS mRNA increases 2- to 3fold by 24 h in both the IGROV-1 cell line, and a second ovarian cancer cell line OVCAR-3, following treatment with TNF-alpha. In contrast, although the ovarian cancer cell lines, PEO1 and SKOV-3, express AS in abundance, this is not TNF-a-inducible
brenda
-
TNF-alpha induces prolonged expression of AS mRNA and protein in ovarian tumour cells, contrasting with short-lived expression of AS mRNA in the normal ovarian epithelial cells. AS mRNA is higher expressed in ovarian tumor tissue compared to normal ovarian tissue. Moreover, AS protein colocalises with TNF-alpha in ovarian cancer cells, with significantly higher levels of AS in malignant compared with normal ovarian tissue.
brenda
additional information
ASS is up-regulated within 3 h after harvest showing that the induction mechanism is very sensitive to the harvest event and emphasizes the importance of the arginine biosynthetic pathway/ornithine cycle in post-harvest physiology
brenda
additional information
-
ASS is up-regulated within 3 h after harvest showing that the induction mechanism is very sensitive to the harvest event and emphasizes the importance of the arginine biosynthetic pathway/ornithine cycle in post-harvest physiology
brenda
additional information
-
treatment of BAEC cells with tumor necrosis factor-alpha supresses argininosuccinate synthase expression. reporter gene analysis demonstrates that TNF-alpha suppresses the AS proximal promoter and electrophoretic mobility shift assay shows reduced binding to three essential Sp1 elements
brenda
additional information
-
87% of human tumors and 5 of 7 cancer cell lines lack ASS expression, overview
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
only a small proportion of the total cellular enzyme is localized in vesicles
brenda
additional information
-
at the activity level, the colocation of argininosuccinate synthetase is changing during fetal and neonatal developement and is under the control of corticosteroid and pancreatic hormones
-
brenda
-
the enzyme is mainly mitochondrial in fetal and new-born liver, and cytoplasmic in adult liver
brenda
-
the enzyme is mainly mitochondrial in fetal and new-born liver, and cytoplasmic in adult liver
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
malfunction
-
malfunction results in citrullinemia type 1 argininosuccinate argininosuccinate synthetase deficiency
malfunction
-
epigenetic silencing triggers apoptosis in arginine auxotroph tumours
malfunction
a cell line lacking two of three LdASS-/-/+ alleles, with greatly reduced argininosuccinate synthase activity, is generated by a double-targeted gene replacement strategy in Leishmania donovani promastigote
malfunction
-
a cell line lacking two of three LdASS-/-/+ alleles, with greatly reduced argininosuccinate synthase activity, is generated by a double-targeted gene replacement strategy in Leishmania donovani promastigote
-
metabolism
-
Sulfolobus solfataricus lacks ornithine acetyltransferase and thus forms N-acetylglutamate exclusively via the energetically less favourable reaction catalysed by N-acetylglutamate synthase, investing 1 mol of acetyl CoA per mol of N-acetyl intermediate synthesized
metabolism
the enzyme plays an important role as the rate-limiting step required for converting L-citrulline to argininosuccinate to provide arginine
metabolism
-
the enzyme plays an important role as the rate-limiting step required for converting L-citrulline to argininosuccinate to provide arginine
-
physiological function
-
rate-limiting enzyme in urea and arginine(NO)-citrulline cycles
physiological function
part of citrulline-NO cycle, limiting step in NO synthesis
physiological function
-
part of citrulline-NO cycle, limiting step in NO synthesis
physiological function
-
recombinant argininosuccinate synthase reduces lipolysaccharide cytotoxicity, TNF-alpha production, and increases cell viability in cultured mouse macrophages, even when added one h following lipopolysaccharide challenge. Intraperitoneal injection of recombinant argininosuccinate synthase at 5 mg/kg after treatment with a high dose of lipopolysaccharide remarkably increases survival of rodents, with a concomitant decrease of sepsis markers TNF-alpha, C-reactive protein, and lactate dehydrogenase levels in blood
physiological function
exogenous expression of either nitric oxide synthase NOS3 or argininosuccinate synthetaseASS1 increases NO production and decreases monocyte adhesion stimulated by tumor necrosis factor-alpha. The latter effect is reduced when human umbilical vein endothelial cells are co-treated with small interfering RNAs for ASS1 or NOS3. SiRNAs of NOS3 and ASS1 attenuate the increase of NO production in human aortic endothelial cells stimulated by laminar shear stress for 24 h
physiological function
the enzyme is essential for parasite survival and growth in the mammalian host
physiological function
argininosuccinate synthase ASS1 is significantly downregulated in the urine of 30 depressed subjects while remaining unchanged in the plasma
physiological function
argininosuccinate synthase 1 (ASS1), is directly transactivated by p53 in response to genotoxic stress, resulting in the rearrangement of arginine metabolism. x-Ray irradiation promotes the systemic induction of Ass1 and concomitantly increases plasma arginine levels in p53+/+ mice but not in p53-/- mice. Ass1+/- mice exhibit hypersensitivity to whole-body irradiation owing to increased apoptosis in the small intestinal crypts. ASS1 plays a pivotal role in limiting Akt phosphorylation. Aberrant activation of Akt resulting from ASS1 loss disrupts Akt-mediated cell survival signaling activity under genotoxic stress
physiological function
argininosuccinate synthase is important for Leishmania donovani to survive in stressed environments and can be exploited as anti-leishmanial drug target
physiological function
-
functioning of arginine related genes is required to deploy defense response against Pseudomonas syringae. Argininosuccinate lyase and argininosuccinate synthase expression is strongly induced upon infection with P. syringae. Silencing of argininosuccinate synthase or lyase leads to enhanced susceptibility to virulent as well as avirulent strains of P. syringae
physiological function
heterologous expression in Lactobacillus plantarum leads to stronger growth performance compared with the control, and the expression levels of the citrate and malate metabolic genes are increased under acid stress. The recombinant strain exhibits 11.0-, 2.0-, 1.9fold higher ASS activity, H+-ATPase activity and intracellular ATP level
physiological function
-
argininosuccinate synthase is important for Leishmania donovani to survive in stressed environments and can be exploited as anti-leishmanial drug target
-
Show AA Sequence and Transmembrane Helices (23365 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
185000
44815
45000
45400
-
4 * 45400, Western blot analysis, calculation from the amino acid sequence
46000
47000
48000
49000
44815
-
4 * 44815, recombinant tAsS, subunit/domain structure, amino acid sequence
44815
4 * 44815, recombinant tAsS, subunit/domain structure, amino acid sequence
45000
-
4 * 45000, two pairs of monomers crosslinked by disulfide bonds, SDS-PAGE in presence of reducing agent
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homotetramer
tetramer
homotetramer
-
each monomer of tetrameric EAS consits of a nucleotide binding domain and a novel catalytic/multimerization domain, subunit/domain structure, subunit interactions
homotetramer
-
4 * 45400, Western blot analysis, calculation from the amino acid sequence
tetramer
-
4 * 45000, two pairs of monomers crosslinked by disulfide bonds, SDS-PAGE in presence of reducing agent
tetramer
two dimers, dimeric and tetrameric interface structures, overview
tetramer
-
4 * 44815, recombinant tAsS, subunit/domain structure, amino acid sequence
tetramer
4 * 44815, recombinant tAsS, subunit/domain structure, amino acid sequence
tetramer
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
4 * 44815, recombinant tAsS, subunit/domain structure, amino acid sequence
-
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
nitrosylation
-
exposure of ASS to IL-1beta in Caco-2 cells induces the nitrosylation of the ASS protein
phosphoprotein
-
regulation of argininosuccinate synthase by dynamic phosphorylation through protein kinase A, the enzyme lacks a consensus Akt phosphorylation motif R-X-R-X-X-S/T
additional information
-
it is shown that IL-1beta inhibits the ASS activity through a post-translational mechanism since increase in both specific mRNA-level and protein amount can be detected after long-time exposure of Caco-2 cells to IL-1beta. The inhibiting effect of IL-1beta is linked to the production of nitric oxide (NO) induced by IL-1beta
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal strucures in complex with intact ATP and with ATP and citrulline, hanging drop vapour-diffusion technique, X-ray analysis
-
purified recombinant ASS1 by hanging-drop method, 0.001 ml of protein solution containing 17 mg/ml protein in 500 mM NaCl, 2 mM TCEP, 30 mM HEPES, pH 7.5, 10 mM aspartate, and 10 mM citrulline, is mixed with 0.001 ml of reservoir solution containing 16% w/v PEG 3350, 0.15 M dl-malic acid pH 7.0, X-ray diffraction structure determination and analysis at 2.4-2.5 A resolution
3-dimensional structure of free enzyme and of complexes with intact ATP, adenylyl imidodiphosphate, arginine or succinate, hanging drop method
-
structures of enzyme complexed with intact ATP and substrates citrulline and aspartate, complexed with AMP and argininosuccinate, and complexed with AMP-PNP, arginine, aspartate and Mg2+, vapor diffusion method, X-ray analysis
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A192V
-
mutant G280R has no ASS activity, mutants A192V, R272C, and R304W have low ASS activity and abnormal kinetics. A higher Km for citrulline than in wild-type enzyme is obtained with mutants A192V, R272C, and R304W
D296G
mutation of the argininosuccinate synthetase gene, found in patients
E191Q
mutation of the argininosuccinate synthetase gene, found in patients
G156del
mutation of the argininosuccinate synthetase gene, found in patients
G280R
-
mutant G280R has no ASS activity, mutants A192V, R272C, and R304W have low ASS activity and abnormal kinetics. A higher Km for citrulline than in wild-type enzyme is obtained with mutants A192V, R272C, and R304W
G324V
mutation of the argininosuccinate synthetase gene, found in patients
G347R
mutation of the argininosuccinate synthetase gene, found in patients
K277T
mutation of the argininosuccinate synthetase gene, found in patients
L160P
mutation of the argininosuccinate synthetase gene, found in patients
L206P
mutation of the argininosuccinate synthetase gene, found in patients
N158del
mutation of the argininosuccinate synthetase gene, found in patients
P96H
mutation of the argininosuccinate synthetase gene, found in patients
Q311del
mutation of the argininosuccinate synthetase gene, found in patients
Q401del
mutation of the argininosuccinate synthetase gene, found in patients
R127Q
mutation of the argininosuccinate synthetase gene, found in patients
R127W
mutation of the argininosuccinate synthetase gene, found in patients
R265C
mutation of the argininosuccinate synthetase gene, found in patients
R272C
-
mutant G280R has no ASS activity, mutants A192V, R272C, and R304W have low ASS activity and abnormal kinetics. A higher Km for citrulline than in wild-type enzyme is obtained with mutants A192V, R272C, and R304W
R304W
-
mutant G280R has no ASS activity, mutants A192V, R272C, and R304W have low ASS activity and abnormal kinetics. A higher Km for citrulline than in wild-type enzyme is obtained with mutants A192V, R272C, and R304W
R344del
mutation of the argininosuccinate synthetase gene, found in patients
S341F
mutation of the argininosuccinate synthetase gene, found in patients
S79P
mutation of the argininosuccinate synthetase gene, found in patients
T284I
mutation of the argininosuccinate synthetase gene, found in patients
Y291S
mutation of the argininosuccinate synthetase gene, found in patients
Y359D
mutation of the argininosuccinate synthetase gene, found in patients
additional information
additional information
an alignment with ASS proteins from other organisms reveals high similarity with fungal (6163%) and mammalian (5155%) ASS proteins
additional information
-
an alignment with ASS proteins from other organisms reveals high similarity with fungal (6163%) and mammalian (5155%) ASS proteins
additional information
enzyme overexpression induces a relocalization of HSCARG
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
45
-
enzyme forms ASSI and II are stable, enzyme form ASSIII is very unstable
50
50
-
7 min, enzyme from normal liver and from patients with citrullinemia, in presence of 10 mM argininosuccinate, about 10% loss of activity
50
-
7 min, enzyme from patients with citrullinemia, in absence of argininosuccinate, 95% loss of activity
50
-
7 min, enzyme from normal liver, in absence of argininosuccinate, about 65% loss of activity
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
in presence of 5 mM argininosuccinate, the activities of the three forms of the enzyme are resistant to chymotrypsin
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 0.05 M citrulline, 0.05 M Asp, or 0.01 M argininosuccinate, stable for more than 1 year
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
affinity chromatography
analysis by native gel electrophoresis shows that argininosuccinate synthetase can bind bacterial lipopolysaccharide and lipid A
-
argininosuccinate synthetase is purified from mouse liver. Livers are excised from 20 male mice (C3H/He strain, age 7-8 weeks) and homogenized in 100 mM Tris-HCl (pH 7.5) containing 1 mM citrulline and 1 mM aspartic acid. Homogenate is centrifuged. After salting-out with (NH4)2SO4. The sample is subjected to anion-exchange chromatography on DE-52. Concentrated samples are loaded on a column of Sephacryl S-300 HR. The collected first peak fractions are dialyzed and subjected to anion-exchange chromatography on UNO S-1
-
recombinant His-tagged enzyme from Escherichia coli by nickel affinty chromatography
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed as a C-terminal fusion protein with maltose-binding protein in Escherichia coli
-
expression alone or together with FLAG-tagged HSCARG or with HSCARG siRNA in HeLa and HEK-293 cells, expression analysis, overview
expression analysis, the AS gene promoter contains a a near consensus PPARgamma response element, PPRE, overview
-
expression in Escherichia coli
expression in Escherichia coli as fusion protein with maltose binding protein
-
the gene encoding argininosuccinate synthetase of Porphyra yezoensis is obtained by PCR using an expressed sequence tag clone as a template, and subcloned into the yeast expression vector pYES2. The gene is expressed when the vector harboring PyARG1 is introduced into an ARG1-deficient strain of Saccharomyces cerevisiae, which results in complementation of the mutant phenotype. The transformed cells survive on a selective medium lacking arginine, and transcripts of PyARG1 are detected by RT-PCR. A quantitative comparison shows that the rescued mutant cells grow in the selective liquid medium with a minor reduction in growth rate relative to wild-type cells
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
argininosuccinate synthase 1 (ASS1), is directly transactivated by p53 in response to genotoxic stress, resulting in the rearrangement of arginine metabolism. x-Ray irradiation promotes the systemic induction of Ass1
Ass1 expression is upregulated significantly at implantation site on day 5 of pregnancy. Ass1 expression is induced by cAMP through PKA/p-Creb signaling pathway
downregulation of enzyme expression is associated with the development of platinum resistance to platinum-based drugs
-
hepatic argininosuccinate synthase expression is hormonally regulated, expression of endothelial and inflammatory cell argininosuccinate synthase is under control of cytokines
-
in liver, mRNA expression levels of Ass and Asl increase significantly during the induction phase of aestivation
in the brain, changes in Ass and asl mRNA expression levels during the three phases of aestivation can be related to the supply of arginine for NO synthesis in response to conditions that resemble ischaemia and ischaemia-reperfusion during the maintenance and arousal phase of aestivation, respectively
in the kidney, there is a significant decrease in ass mRNA expression level after 6 months of aestivation. In skeletal muscle, Ass mRNA expression decreases during aestivation
L-Arg at high concentration down-regulates Ass1 and Asl expression by negative feedback to maintain L-Arg homeostasis
overexpression of argininosuccinate synthase in primary ovarian, stomach and colorectal cancer cells results in platinum sensitive tumours
-
tumoural enzyme downregulation by hepatocellular carcinoma, malignant melanoma, malignant pleural mesothelioma, prostate and renal cancer
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
-
functioning of arginine related genes is required to deploy defense response against Pseudomonas syringae. Argininosuccinate lyase and argininosuccinate synthase expression is strongly induced upon infection with P. syringae. Silencing of argininosuccinate synthase or lyase leads to enhanced susceptibility to virulent as well as avirulent strains of P. syringae
analysis
method for high-throughput enrichment of temperature-sensitive ArgG variants with a fluorescent TIMER protein and flow cytometry
drug development
-
high levels of AS expression, which may be required for several arginine-dependent processes in cancer, including the production of nitric oxide, proline, pyrimidines and polyamines, is regulated by TNF-alpha and may provide an important molecular pathway linking inflammation and metabolism to ovarian tumorigenesis
medicine
molecular biology
report in which the function of a Porphyra yezoensis gene has been directly demonstrated by the rescue of a Saccharomyces cerevisiae mutant. This technique may provide new opportunities for further investigations into the functions of various genes in Porphyra yezoensis and other macroalgal species
synthesis
production of citrulline using a temperature-sensitive ArgG variant that enables precise and tunable control of cell growth by temperature changes. Production follows a 33°C growth-phase for biomass accumulation and a 39°C stationary-phase for citrulline production. 3 g/l citrulline are produced during 45 h cultivation in a 1-l bioreactor
medicine
-
neuronal and glial ASS expression is increased in brains of patients with Alzheimer disease
medicine
-
AS and GTP cyclohydrolase I are intimately associated with inflammatory arthritis, they may be important modulators of arthritis and may represent novel targets for modulation of disease activity
medicine
-
citrulline-arginine recycling enzyme, intervention in the supply of arginine may represent a new therapeutic approach to the treatment of NO-mediated neurodegenerative damage in the brain
medicine
-
a case of late-onset CTLN1 (citrullinemia) in a patient is described by biochemical analyses and ASS gene mutation confirmation. This is the first report of a Korean patient with late-onset CTLN1 confirmed by ASS gene mutation identification
medicine
-
the downregulation of tumor necrosis factor-alpha is an added insult to endothelial function because of its important role in NO production and in endothelial viability
medicine
-
transient ischemia induces changes in nitric oxide synthase, argininosuccinate synthetase and argininsuccinate lyase co-expression in the rat striatal neurons. At 24 h after reperfusion in the animals with a longer survival and better motor-sensory performances there is an increase in these neuronal populations. It is hypothesized that the elevated expression of argininosuccinate synthetase and argininsuccinate lyase protects ischemic striatal neurons from tissue damages by maintaining a correct NO production
medicine
-
argininosuccinate synthetase is inhibited by endotoxin, implying that bacterial products might potentially regulate the arginine metabolism in the host and perturb NO synthesis
medicine
argininosuccinate synthase Ass contributes to ethanol plus Fas/CD95 agonistic antibody Jo2-mediated liver injury. NOS2 induction, 3-nitrotyrosine adducts formation and elevated nitrites, nitrates and S-nitrosothiols are higher in livers from wild-type mice than from Ass+/- mice
medicine
argininosuccinate synthase ASS1 is significantly downregulated in the urine of 30 depressed subjects while remaining unchanged in the plasma. ASS1 displays strong efficacy in distinguishing major depressive disorder subjects from healthy controls
medicine
unclassified hepatocellular carcinomas display specific up-regulation of the arginine synthesis pathway associated with overexpression of argininosuccinate synthase (ASS1) and arginosuccinate lyase. All the unclassified hepatocellular carcinomas tested could be identified by ASS1 immunohistochemistry, and 64.7% of these carcinomas presented clinical bleeding manifestations. The significance of ASS1 also encompasses certain hemorrhagic cases, particularly inflammatory hepatocellular carcinomas
medicine
argininosuccinate synthase 1 is upregulated in primary human colorectal tumors and pharmacological inhibition or genetic ablation of ASS1 impairs colorectal cancer pathogenicity. ASS1 inhibition leads to reductions in the levels of oncogenic metabolite fumarate, leading to impairments in glycolytic metabolism that supports colorectal cancer cell pathogenicity
medicine
ASS1 expression is upregulated and correlates with APC mutations in human colorectal adenomas and carcinomas. Epithelial Ass1 is not required for intestinal epithelial regeneration after irradiation, and epithelial expression of Ass1 is not required for intestinal tumorigenesis
medicine
ASS1 expression is upregulated and correlates with APC mutations in human colorectal adenomas and carcinomas. Epithelial Ass1 is not required for intestinal epithelial regeneration after irradiation, and epithelial expression of Ass1 is not required for intestinal tumorigenesis. Epithelial Ass1 does not affect intestinal tumorigenesis in mice fed an arginine-free diet
medicine
ASS1 is highly expressed in gastric cancer and positively correlated with gastric cancer aggressiveness and poor outcome. Depletion of ASS1 leads to inhibition of tumor growth and decreases cell invasion via induction of autophagy-lysosome machinery, resulting in degradation of active beta-catenin, Snail, and Twist. Ectopic expression of ASS1 in gastric cancer cells reverse protects cancer cells from chemotherapy drug-induced apoptosis via activation of the AKT-mammalian target of rapamycin signaling pathway
medicine
ASS1 expression is highly correlated with glioma-associated oncogene GLI1 expression. In hepatocellular adenoma, ASS1 overexpression is significantly associated with sonic hedgehog hepatocellular adenoma compared to other molecular subgroups. GLI1 expression silencing induces a downregulation of ASS1 in PLC/PFR5 and SNU878 cell lines. ASS1 expression belongs to the periportal expression program that is maintained in sonic hedgehog hepatocellular adenoma but down-regulated in all the other hepatocellular adenoma subtypes. ASS1 mRNA expression is not associated with specific clinical features
medicine
Kaposi's sarcoma-associated herpesvirus infection accelerates nitrogen efflux by upregulating the expression of argininosuccinate synthase ASS1. Kaposi's sarcoma-associated herpesvirus utilizes multiple microRNAs to upregulate ASS1 expression. Depletion of either ASS1 or inducible nitric oxide synthase suppresses growth proliferation, abolishes colony formation in soft agar, and decreases NO generation. ASS1 expression facilitates Kaposi's sarcoma-associated herpesvirus-mediated activation of the STAT3 pathway, critical for virus-induced transformation
medicine
in hepatocellular carcinoma patients, ASS1 expression is significantly decreased and down-regulation of ASS1 was closely correlated with poor prognosis. DNA methylation leads to the down-regulation of ASS1 in hepatocellular carcinoma. Stable silencing of ASS1 promotes migration and invasion of hepatocellular carcinoma cells, and overexpression of ASS1 inhibits metastasis of hepatocellular carcinoma cells in vivo and in vitro. ASS1-knockdown increases the phosphorylation level of S727 STAT3
medicine
ASS1 expression is low in most hepatocellular carcinoma samples. High levels of ASS1 are associated with favorable overall survival of patients. Bidirectional interactions between ASS1 and ER stress responses in hepatocellular carcinoma-derived multicellular tumor spheroids can limit hepatocellular carcinoma progression. ASS1 overexpression effectively inhibits tumor growth and enhances the efficacy of in vitro and in vivo anti-hepatocellular carcinomacombination chemotherapy via activation of the PERK/eIF2alpha/ATF4/CHOP axis
medicine
ASS1 functions as a tumor suppressor in breast cancer, and the pesticide spinosyn A and its derivative LM-2I suppress breast tumor cell proliferation and growth by binding to and activating ASS1
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REF.
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TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Shargool, P.D.
Purification of argininosuccinate synthetase from cotyledons of germinating peas
Phytochemistry
10
2029-2032
1971
Lathyrus oleraceus
-
brenda
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Enzymes of arginine and urea synthesis
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39
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1973
Bos taurus
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Rattus norvegicus
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Rattus norvegicus
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Rochovansky, O.; Kodowaki, H.; Ratner, S.
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Bos taurus
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Studies on liver argininosuccinate synthetase in a patient with citrullinemia and in normal subjects
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85
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1979
Homo sapiens
brenda
Hilger, F.; Simon, J.P.; Stalon, V.
Yeast argininosuccinate synthetase. Purification, structural and kinetic properties
Eur. J. Biochem.
94
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1979
Saccharomyces cerevisiae, Saccharomyces cerevisiae 1278b
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Studies on rat liver argininosuccinate synthetase. Inhibition by various amino acids
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85
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Rattus norvegicus
brenda
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Isolation and characterization of argininosuccinate synthetase from human liver
Biochemistry
18
5353-5356
1979
Homo sapiens
brenda
Takada, S.; Kusumi, T.; Saheki, T.; Tsuda, M.; Katsunuma, T.
Studies of rat liver argininosuccinate synthetase. The presence of three forms, and their physicochemical, catalytic, and immunochemical properties
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86
1353-1359
1979
Rattus norvegicus
brenda
Kimball, M.E.; Jacoby, L.B.
Purification and properties of argininosuccinate synthetase from normal and canavanine-resistant human lymphoblasts
Biochemistry
19
705-709
1980
Homo sapiens
brenda
Saheki, T.; Tsuda, M.; Takada, S.; Kusumi, K.; Katsunuma, T.
Role of argininosuccinate synthetase in the regulation of urea synthesis in the rat and argininosuccinate synthetase-associated metabolic disorder in man
Adv. Enzyme Regul.
18
221-238
1986
Rattus norvegicus, Homo sapiens
brenda
Ratner, S.
Argininosuccinate synthetase of bovine liver: chemical and physical properties
Proc. Natl. Acad. Sci. USA
79
5197-5199
1982
Bos taurus
brenda
Saheki, T.; Sase, M.; Nakano, K.; Azuma, F.; Katsunuma, T.
Some properties of argininosuccinate synthetase purified from human liver and a comparison with the rat liver enzyme
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93
1531-1537
1983
Rattus norvegicus, Homo sapiens
brenda
Raushell, F.M.; Seiglie, J.L.
Kinetic mechanism of argininosuccinate synthetase
Arch. Biochem. Biophys.
225
979-985
1983
Bos taurus
brenda
Raushel, F.M.
Nitro analogs of substrates for argininosuccinate synthetase and argininosuccinate lyase
Arch. Biochem. Biophys.
232
520-525
1984
Bos taurus
brenda
Kumar, S.; Lennane, J.; Ratner, S.
Argininosuccinate synthetase: essential role of cysteine and arginine residues in relation to structure and mechanism of ATP activation
Proc. Natl. Acad. Sci. USA
82
6745-6749
1985
Bos taurus
brenda
Isayama, H.; Nakamura, H.; Kanemura, H.; Kobayashi, K.; Emson, P.C.; Kawabuchi, M.; Tashiro, N.
Distribution and co-localization of nitric oxide synthetase and argininosuccinate synthetase in the cat hypothalamus
Arch. Histol. Cytol.
60
477-492
1997
Felis catus
brenda
Demarquoy, J.; Fairand, A.; Gautier, C.; Vaillant, T.
Regulation of argininosuccinate synthetase level by corticosteroid and pancreatic hormones during perinatal period
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143
47-51
1995
Rattus norvegicus
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Demonstration of argininosuccinate synthetase activity associated with mitochondrial membrane: characterization and hormonal regulation
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136
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1994
Rattus norvegicus
brenda
Patejunas, G.; Bradley, A.; Beaudet, A.L.; O'Brien, W.E.
Generation of a mouse model for citrullinemia by targeted disruption of the argininosuccinate synthetase gene
Somat. Cell Mol. Genet.
20
55-60
1994
Mus musculus
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Immunohistochemical localization of argininosuccinate synthetase in the rat brain in relation to nitric oxide synthase-containg neurons
Neuroscience
51
773-789
1992
Rattus norvegicus
brenda
Isahiki, Y.; Noda, T.; Kobayashi, K.; Sase, M.; Saheki, T.; Titani, K.
Identification of essential arginine residue(s) for Mg-ATP binding of human argininosuccinate synthetase
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2
283-287
1989
Homo sapiens
brenda
Wakui, H.; Komatsuda, A.; Itoh, H.; Kobayashi, R.; Nakamoto, Y.; Miura, A.B.
Renal argininosuccinate synthetase: purification, immunohistochemical localization, and elastin-binding property
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15
1-9
1992
Sus scrofa
brenda
Yu, Y.; Terada, K.; Nagasaki, A.; Takiguchi, M.; Mori, M.
Preparation of recombinant argininosuccinate synthetase and arguininosuccinate lyase: expression of the enzymes in rat tissues
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117
952-957
1995
Rattus norvegicus
brenda
Shaheen, N.; Kobayashi, K.; Terazono, H.; Fukushige, T.; Horiuchi, M.; Saheki, T.
Characterization of human wild-type and mutant argininosuccinate synthetase proteins expressed in bacterial cells
Enzyme Protein
95
251-264
1994
Homo sapiens
brenda
Lemke, C.; Yeung, M.; Howell, P.L.
Expression, purification, crystallization and preliminary X-ray analysis of Escherichia coli argininosuccinate synthetase
Acta Crystallogr. Sect. D
55
2028-2030
1999
Escherichia coli
-
brenda
Shen, L.J.; Lin, W.C.; Beloussow, K.; Shen, W.C.
Resistance to the anti-proliferative activity of recombinant arginine deiminase in cell culture correlates with the endogenous enzyme, argininosuccinate synthetase
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191
165-170
2003
Homo sapiens, Mus musculus, Canis lupus familiaris
brenda
Van Geldre, L.A.; Timmermans, J.P.; Lefebvre, R.A.
L-citrulline recycling by argininosuccinate synthetase and lyase in rat gastric fundus
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455
149-160
2002
Rattus norvegicus
brenda
Lemke, C.T.; Howell, P.L.
Substrate induced conformational changes in argininosuccinate synthetase
J. Biol. Chem.
277
13074-13081
2002
Escherichia coli
brenda
Goto, M.; Nakajima, Y.; Hirotsu, K.
Crystal structure of argininosuccinate synthetase from Thermus thermophilus HB8. Structural basis for the catalytic action
J. Biol. Chem.
277
15890-15896
2002
Thermus thermophilus, Thermus thermophilus HB8 / ATCC 27634 / DSM 579
brenda
Goto, M.; Omi, R.; Miyahara, I.; Sugahara, M.; Hirotsu, K.
Structures of argininosuccinate synthetase in enzyme-ATP substrates and enzyme-AMP product forms. Stereochemistry of the catalytic reaction
J. Biol. Chem.
278
22964-22971
2003
Thermus thermophilus (P59846), Thermus thermophilus, Thermus thermophilus HB8 / ATCC 27634 / DSM 579 (P59846)
brenda
Heneka, M.T.; Wiesinger, H.; Dumitrescu-Ozimek, L.; Riederer, P.; Feinstein, D.L.; Klockgether, T.
Neuronal and glial coexpression of argininosuccinate synthetase and inducible nitric oxide synthase in Alzheimer disease
J. Neuropathol. Exp. Neurol.
60
906-916
2001
Homo sapiens
brenda
Hukkanen, M.; Platts, L.A.M.; Haralambous, S.; Ainola, M.; Konttinen, Y.T.; Kollias, G.; Polak, J.M.
Induction of inducible nitric oxide synthase, argininosuccinate synthase, and GTP cyclohydrolase I in arthritic joints of human tumor necrosis factor-alpha transgenic mice
J. Rheumatol.
30
652-659
2003
Mus musculus
brenda
Kawahara, K.; Gotoh, T.; Oyadomari, S.; Kajizono, M.; Kuniyasu, A.; Ohsawa, K.; Imai, Y.; Kohsaka, S.; Nakayama, H.; Mori, M.
Co-induction of argininosuccinate synthetase, cationic amino acid transporter-2, and nitric oxide synthase in activated murine microglial cells
Mol. Brain Res.
90
165-173
2001
Rattus norvegicus, Mus musculus
brenda
Hammermann, R.; Bliesener, N.; Mossner, J.; Klasen, S.; Wiesinger, H.; Wessler, I.; Racke, K.
Inability of rat alveolar macrophages to recycle L-citrulline to L-arginine despite induction of argininosuccinate synthetase mRNA and protein, and inhibition of nitric oxide synthesis by exogenous L-citrulline
Naunyn Schmiedebergs Arch. Pharmacol.
358
601-607
1998
Rattus norvegicus
brenda
Brasse-Lagnel, C.; Lavoinne, A.; Fairand, A.; Vavasseur, K.; Husson, A.
IL-1beta stimulates argininosuccinate synthetase gene expression through NF-kappaB in Caco-2 cells
Biochimie
87
403-409
2005
Homo sapiens
brenda
Goodwin, B.L.; Solomonson, L.P.; Eichler, D.C.
Argininosuccinate synthase expression is required to maintain nitric oxide production and cell viability in aortic endothelial cells
J. Biol. Chem.
279
18353-18360
2004
Bos taurus
brenda
Hao, G.; Xie, L.; Gross, S.S.
Argininosuccinate synthetase is reversibly inactivated by S-nitrosylation in vitro and in vivo
J. Biol. Chem.
279
36192-36200
2004
Homo sapiens
brenda
Pendleton, L.C.; Goodwin, B.L.; Solomonson, L.P.; Eichler, D.C.
Regulation of endothelial argininosuccinate synthase expression and NO production by an upstream open reading frame
J. Biol. Chem.
280
24252-24260
2005
Bos taurus
brenda
Goodwin, B.L.; Pendleton, L.C.; Levy, M.M.; Solomonson, L.P.; Eichler, D.C.
Tumor necrosis factor-alpha reduces argininosuccinate synthase expression and nitric oxide production in aortic endothelial cells
Am. J. Physiol. Heart Circ. Physiol.
293
H1115-H1121
2007
Bos taurus
brenda
Brasse-Lagnel, C.; Lavoinne, A.; Fairand, A.; Vavasseur, K.; Deniel, N.; Husson, A.
Biphasic effect of IL-1beta on the activity of argininosuccinate synthetase in Caco-2 cells. Involvement of nitric oxide production
Biochimie
88
607-612
2006
Homo sapiens
brenda
Bizzoco, E.; Vannucchi, M.G.; Faussone-Pellegrini, M.S.
Transient ischemia increases neuronal nitric oxide synthase, argininosuccinate synthetase and argininosuccinate lyase co-expression in rat striatal neurons
Exp. Neurol.
204
252-259
2007
Rattus norvegicus
brenda
Szlosarek, P.W.; Grimshaw, M.J.; Wilbanks, G.D.; Hagemann, T.; Wilson, J.L.; Burke, F.; Stamp, G.; Balkwill, F.R.
Aberrant regulation of argininosuccinate synthetase by TNF-alpha in human epithelial ovarian cancer
Int. J. Cancer
121
6-11
2007
Homo sapiens
brenda
Kim, I.S.; Ki, C.S.; Kim, J.W.; Lee, M.; Jin, D.K.; Lee, S.Y.
Characterization of late-onset citrullinemia 1 in a Korean patient: confirmation by argininosuccinate synthetase gene mutation analysis
J. Biochem. Mol. Biol.
39
400-405
2006
Homo sapiens
brenda
Satoh, M.; Iwahori, T.; Sugawara, N.; Yamazaki, M.
Liver argininosuccinate synthase binds to bacterial lipopolysaccharides and lipid A and inactivates their biological activities
J. Endotoxin Res.
12
21-38
2006
Mus musculus
brenda
Endo, H.; Ootsuka, S.; Fukuda, S.; Kitade, Y.; Saga, N.
Functional complementation of an arginine auxotrophic yeast mutant by an argininosuccinate synthetase from Porphyra yezoensis (Rhodophyta)
J. Phycol.
42
1066-1071
2006
Pyropia yezoensis (Q0KKQ0)
-
brenda
Wagemaker, M.J.; Eastwood, D.C.; van der Drift, C.; Jetten, M.S.; Burton, K.; Van Griensven, L.J.; Op den Camp, H.J.
Argininosuccinate synthetase and argininosuccinate lyase: two ornithine cycle enzymes from Agaricus bisporus
Mycol. Res.
111
493-502
2007
Agaricus bisporus (Q2Z0F6), Agaricus bisporus
brenda
Cruz, C.; Egsgaard, H.; Trujillo, C.; Ambus, P.; Requena, N.; Martins-Loucao, M.A.; Jakobsen, I.
Enzymatic evidence for the key role of arginine in nitrogen translocation by arbuscular mycorrhizal fungi
Plant Physiol.
144
782-792
2007
Rhizophagus intraradices, Daucus carota
brenda
Karlberg, T.; Collins, R.; van den Berg, S.; Flores, A.; Hammarstroem, M.; Hoegbom, M.; Holmberg Schiavone, L.; Uppenberg, J.
Structure of human argininosuccinate synthetase
Acta Crystallogr. Sect. D
64
279-286
2008
Homo sapiens (P00966), Homo sapiens
brenda
Goodwin, B.L.; Corbin, K.D.; Pendleton, L.C.; Levy, M.M.; Solomonson, L.P.; Eichler, D.C.
Troglitazone up-regulates vascular endothelial argininosuccinate synthase
Biochem. Biophys. Res. Commun.
370
254-258
2008
Bos taurus
brenda
Corbin, K.D.; Pendleton, L.C.; Solomonson, L.P.; Eichler, D.C.
Phosphorylation of argininosuccinate synthase by protein kinase A
Biochem. Biophys. Res. Commun.
377
1042-1046
2008
Bos taurus
brenda
Guei, T.R.; Liu, M.C.; Yang, C.P.; Su, T.S.
Identification of a liver-specific cAMP response element in the human argininosuccinate synthetase gene
Biochem. Biophys. Res. Commun.
377
257-261
2008
Homo sapiens
brenda
Satoh, M.; Ando, S.; Shinoda, T.; Yamazaki, M.
Clearance of bacterial lipopolysaccharides and lipid A by the liver and the role of argininosuccinate synthase
Innate Immun.
14
51-60
2008
Mus musculus
brenda
Bowles, T.L.; Kim, R.; Galante, J.; Parsons, C.M.; Virudachalam, S.; Kung, H.J.; Bold, R.J.
Pancreatic cancer cell lines deficient in argininosuccinate synthetase are sensitive to arginine deprivation by arginine deiminase
Int. J. Cancer
123
1950-1955
2008
Homo sapiens
brenda
Zhao, Y.; Zhang, J.; Li, H.; Li, Y.; Ren, J.; Luo, M.; Zheng, X.
An NADPH sensor protein (HSCARG) down-regulates nitric oxide synthesis by association with argininosuccinate synthetase and is essential for epithelial cell viability
J. Biol. Chem.
283
11004-11013
2008
Homo sapiens (P00966)
brenda
Larovere, L.E.; Angaroni, C.J.; Antonozzi, S.L.; Bezard, M.B.; Shimohama, M.; de Kremer, R.D.
Citrullinemia type I, classical variant. Identification of ASS-p~G390R (c.1168G>A) mutation in families of a limited geographic area of Argentina: a possible population cluster
Clin. Biochem.
42
1166-1168
2009
Homo sapiens (P00966), Homo sapiens
brenda
Ibarra-Gonzalez, I.; Fernandez-Lainez, C.; Vela-Amieva, M.
Clinical and biochemical characteristics of patients with urea cycle disorders in a developing country
Clin. Biochem.
43
461-466
2010
Homo sapiens
brenda
El Fadili, K.; Drummelsmith, J.; Roy, G.; Jardim, A.; Ouellette, M.
Down regulation of KMP-11 in Leishmania infantum axenic antimony resistant amastigotes as revealed by a proteomic screen
Exp. Parasitol.
123
51-57
2009
Leishmania infantum (A4I066), Leishmania infantum
brenda
Engel, K.; Hhne, W.; Hberle, J.
Mutations and polymorphisms in the human argininosuccinate synthetase (ASS1) gene
Hum. Mutat.
30
300-307
2009
Homo sapiens (P00966), Homo sapiens
brenda
Nicholson, L.J.; Smith, P.R.; Hiller, L.; Szlosarek, P.W.; Kimberley, C.; Sehouli, J.; Koensgen, D.; Mustea, A.; Schmid, P.; Crook, T.
Epigenetic silencing of argininosuccinate synthetase confers resistance to platinum-induced cell death but collateral sensitivity to arginine auxotrophy in ovarian cancer
Int. J. Cancer
125
1454-1463
2009
Homo sapiens
brenda
Delage, B.; Fennell, D.A.; Nicholson, L.; McNeish, I.; Lemoine, N.R.; Crook, T.; Szlosarek, P.W.
Arginine deprivation and argininosuccinate synthetase expression in the treatment of cancer
Int. J. Cancer
126
2762-2772
2010
Homo sapiens
brenda
Guerreiro, J.R.; Lameu, C.; Oliveira, E.F.; Klitzke, C.F.; Melo, R.L.; Linares, E.; Augusto, O.; Fox, J.W.; Lebrun, I.; Serrano, S.M.; Camargo, A.C.
Argininosuccinate synthetase is a functional target for a snake venom anti-hypertensive peptide: role in arginine and nitric oxide production
J. Biol. Chem.
284
20022-20033
2009
Mus musculus (P16460), Homo sapiens
brenda
Nagasaka, H.; Tsukahara, H.; Yorifuji, T.; Miida, T.; Murayama, K.; Tsuruoka, T.; Takatani, T.; Kanazawa, M.; Kobayashi, K.; Okano, Y.; Takayanagi, M.
Evaluation of endogenous nitric oxide synthesis in congenital urea cycle enzyme defects
Metab. Clin. Exp.
58
278-282
2009
Homo sapiens
brenda
Prima, V.; Wang, A.; Molina, G.; Wang, K.K.; Svetlov, S.I.
Inhibition of LPS toxicity by hepatic argininosuccinate synthase (ASS): Novel roles for ASS in innate immune responses to bacterial infection
Int. Immunopharmacol.
11
1180-1188
2011
Homo sapiens (P00966), Mus musculus
brenda
Mun, G.I.; Kim, I.S.; Lee, B.H.; Boo, Y.C.
Endothelial argininosuccinate synthetase 1 regulates nitric oxide production and monocyte adhesion under static and laminar shear stress conditions
J. Biol. Chem.
286
2536-2542
2011
Homo sapiens (P00966), Homo sapiens
brenda
Van de Casteele, M.; Demarez, M.; Legrain, C.; Glansdorff, N.; Pierard, A.
Pathways of arginine biosynthesis in extreme thermophilic archaeo- and eubacteria
J. Gen. Microbiol.
136
1177-1183
1990
Saccharolobus solfataricus, Pyrococcus furiosus, Saccharolobus solfataricus P1
-
brenda
Lakhal-Naouar, I.; Jardim, A.; Strasser, R.; Luo, S.; Kozakai, Y.; Nakhasi, H.L.; Duncan, R.C.
Leishmania donovani argininosuccinate synthase is an active enzyme associated with parasite pathogenesis
PLoS Negl. Trop. Dis.
6
e1849
2012
Leishmania donovani (H9BG20), Leishmania donovani
brenda
Bateman, L.A.; Ku, W.M.; Heslin, M.J.; Contreras, C.M.; Skibola, C.F.; Nomura, D.K.
Argininosuccinate synthase 1 is a metabolic regulator of colorectal cancer pathogenicity
ACS Chem. Biol.
12
905-911
2017
Homo sapiens (P00966), Homo sapiens
brenda
Lu, Y.; Ward, S.; Nieto, N.
Ethanol plus the Jo2 fas agonistic antibody-induced liver injury is attenuated in mice with partial ablation of argininosuccinate synthase
Alcoholism
38
649-656
2014
Mus musculus (P16460)
brenda
Wu, D.; Peng, Y.; Zhou, J.; Yang, Y.T.; Rao, C.L.; Bai, S.J.; Zhou, X.Y.; Chen, J.; Liao, L.; Liang, Z.H.; Yang, D.Y.; Xie, P.
Identification and validation of argininosuccinate synthase as a candidate urinary biomarker for major depressive disorder
Clin. Chim. Acta
451
142-148
2015
Homo sapiens (P00966)
brenda
Henriet, E.; Abou Hammoud, A.; Dupuy, J.W.; Dartigues, B.; Ezzoukry, Z.; Dugot-Senant, N.; Leste-Lasserre, T.; Pallares-Lupon, N.; Nikolski, M.; Le Bail, B.; Blanc, J.F.; Balabaud, C.; Bioulac-Sage, P.; Raymond, A.A.; Saltel, F.
Argininosuccinate synthase 1 (ASS1) A marker of unclassified hepatocellular adenoma and high bleeding risk
Hepatology
66
2016-2028
2017
Homo sapiens (P00966)
brenda
Chng, Y.R.; Ong, J.L.; Ching, B.; Chen, X.L.; Wong, W.P.; Chew, S.F.; Ip, Y.K.
Molecular characterization of argininosuccinate synthase and argininosuccinate lyase from the liver of the African lungfish Protopterus annectens, and their mRNA expression levels in the liver, kidney, brain and skeletal muscle during aestivation
J. Comp. Physiol. B
184
835-853
2014
Protopterus annectens (S4V5K7), Protopterus annectens
brenda
Huang, Z.; Wang, T.S.; Zhao, Y.C.; Zuo, R.J.; Deng, W.B.; Chi, Y.J.; Yang, Z.M.
Cyclic adenosine monophosphate-induced argininosuccinate synthase 1 expression is essential during mouse decidualization
Mol. Cell. Endocrinol.
388
20-31
2014
Mus musculus (P16460), Mus musculus
brenda
Miyamoto, T.; Lo, P.H.Y.; Saichi, N.; Ueda, K.; Hirata, M.; Tanikawa, C.; Matsuda, K.
Argininosuccinate synthase 1 is an intrinsic Akt repressor transactivated by p53
Sci. Adv.
3
e1603204
2017
Mus musculus (P16460)
brenda
Sardar, A.; Jardim, A.; Ghosh, A.; Mandal, A.; Das, S.; Saini, S.; Abhishek, K.; Singh, R.; Verma, S.; Kumar, A.; Das, P.
Genetic manipulation of Leishmania donovani to explore the involvement of argininosuccinate synthase in oxidative stress management
PLoS Negl. Trop. Dis.
10
e0004308
2016
Leishmania donovani (H9BG20), Leishmania donovani, Leishmania donovani AG83 (H9BG20)
brenda
Tao, X.; Zuo, Q.; Ruan, H.; Wang, H.; Jin, H.; Cheng, Z.; Lv, Y.; Qin, W.; Wang, C.
Argininosuccinate synthase 1 suppresses cancer cell invasion by inhibiting STAT3 pathway in hepatocellular carcinoma
Acta Biochim. Biophys. Sin. (Shanghai)
51
263-276
2019
Homo sapiens (P00966)
brenda
Anwar, S.; Ali, M.; Abbas, A.; Wieczorek, K.
Arabidopsis argininosuccinate lyase and argininosuccinate synthase are important for resistance against Pseudomonas syringae
Adv. Life Sci.
7
20-26
2019
Arabidopsis thaliana
-
brenda
van der Meer, J.H.M.; de Boer, R.J.; Meijer, B.J.; Smit, W.L.; Vermeulen, J.L.M.; Meisner, S.; van Roest, M.; Koelink, P.J.; Dekker, E.; Hakvoort, T.B.M.; Koster, J.; Hawinkels, L.J.A.C.; Heijmans, J.; Struijs, E.A.; Boermeester, M.A.; van den Brink, G.R.; Muncan, V.
Epithelial argininosuccinate synthetase is dispensable for intestinal regeneration and tumorigenesis
Cell Death Dis.
12
897
2021
Homo sapiens (P00966), Mus musculus (P16460)
brenda
Tsai, C.Y.; Chi, H.C.; Chi, L.M.; Yang, H.Y.; Tsai, M.M.; Lee, K.F.; Huang, H.W.; Chou, L.F.; Cheng, A.J.; Yang, C.W.; Wang, C.S.; Lin, K.H.
Argininosuccinate synthetase 1 contributes to gastric cancer invasion and progression by modulating autophagy
FASEB J.
32
2601-2614
2018
Homo sapiens (P00966)
brenda
Zhao, H.; Liu, L.; Peng, S.; Yuan, L.; Li, H.; Wang, H.
Heterologous expression of argininosuccinate synthase from Oenococcus oeni enhances the acid resistance of Lactobacillus plantarum
Front. Microbiol.
10
1393
2019
Oenococcus oeni (A0A483BCS6)
brenda
Nault, J.C.; Couchy, G.; Caruso, S.; Meunier, L.; Caruana, L.; Letouze, E.; Rebouissou, S.; Paradis, V.; Calderaro, J.; Zucman-Rossi, J.
Argininosuccinate synthase 1 and periportal gene expression in sonic hedgehog hepatocellular adenomas
Hepatology
68
964-976
2018
Homo sapiens (P00966)
brenda
Kim, S.; Lee, M.; Song, Y.; Lee, S.; Choi, I.; Park, I.; Kim, J.; Kim, J.; Kim, K.; Seo, H.
Argininosuccinate synthase 1 suppresses tumor progression through activation of PERK/eIF2alpha/ATF4/CHOP axis in hepatocellular carcinoma
J. Exp. Clin. Cancer Res.
40
127
2021
Homo sapiens (P00966)
brenda
Li, T.; Zhu, Y.; Cheng, F.; Lu, C.; Jung, J.; Gao, S.
Oncogenic Kaposis sarcoma-associated herpesvirus upregulates argininosuccinate synthase 1, a rate-limiting enzyme of the citrulline-nitric oxide cycle, to activate the STAT3 pathway and promote growth transformation
J. Virol.
93
e01599-18
2019
Rattus norvegicus (P09034)
brenda
Schramm, T.; Lempp, M.; Beuter, D.; Sierra, S.G.; Glatter, T.; Link, H.
High-throughput enrichment of temperature-sensitive argininosuccinate synthetase for two-stage citrulline production in E. coli
Metab. Eng.
60
14-24
2020
Escherichia coli (P0A6E4)
brenda
Zou, Z.; Hu, X.; Luo, T.; Ming, Z.; Chen, X.; Xia, L.; Luo, W.; Li, J.; Xu, N.; Chen, L.; Cao, D.; Wen, M.; Kong, F.; Peng, K.; Xie, Y.; Li, X.; Ma, D.; Yang, C.; Chen, C.; Yi, W.; Liu, O.; Liu, S.; Luo, J.; Luo, Z.
Naturally-occurring spinosyn A and its derivatives function as argininosuccinate synthase activator and tumor inhibitor
Nat. Commun.
12
2263
2021
Homo sapiens (P00966)
brenda
Querobino, S.M.; Ribeiro, C.A.J.; Alberto-Silva, C.
Bradykinin-potentiating PEPTIDE-10C, an argininosuccinate synthetase activator, protects against H2O2-induced oxidative stress in SH-SY5Y neuroblastoma cells
Peptides
103
90-97
2018
Homo sapiens (P00966)
brenda
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