Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ATP + citrulline + aspartate
AMP + diphosphate + 2-(Nomega-L-arginino)succinate
ATP + L-citrulline + 3-nitro-2-aminopropanoate
?
-
60% of the maximal activity with Asp
-
-
?
ATP + L-citrulline + L-Asp
?
ATP + L-citrulline + L-Asp
AMP + diphosphate + L-argininosuccinate
ATP + L-citrulline + L-aspartate
AMP + diphosphate + 2-(Nomega-L-arginino)succinate
ATP + L-citrulline + L-aspartate
AMP + diphosphate + L-argininosuccinate
ATP + L-citrulline + threo-beta-hydroxy-DL-Asp
?
-
-
-
-
?
ATP + L-citrulline + threo-beta-methyl-L-Asp
?
-
-
-
-
?
dATP + L-citrulline + L-Asp
dAMP + diphosphate + L-argininosuccinate
-
2.6% as active as ATP
-
-
?
additional information
?
-
ATP + citrulline + aspartate
AMP + diphosphate + 2-(Nomega-L-arginino)succinate
-
-
-
-
?
ATP + citrulline + aspartate
AMP + diphosphate + 2-(Nomega-L-arginino)succinate
-
-
-
-
?
ATP + citrulline + aspartate
AMP + diphosphate + 2-(Nomega-L-arginino)succinate
assay at pH 7.8, 37°C, reaction stopped by addition of molybdate buffer
-
-
?
ATP + citrulline + aspartate
AMP + diphosphate + 2-(Nomega-L-arginino)succinate
-
-
-
-
?
ATP + L-citrulline + L-Asp
?
-
urea-cycle enzyme
-
-
?
ATP + L-citrulline + L-Asp
?
-
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
-
-
?
ATP + L-citrulline + L-Asp
?
-
third reaction of urea cycle
-
-
?
ATP + L-citrulline + L-Asp
?
-
anabolic function in biosynthesis of Arg and catabolic function as the first enzyme of citrulline utilization as nitrogen source
-
-
?
ATP + L-citrulline + L-Asp
?
-
anabolic function in biosynthesis of Arg and catabolic function as the first enzyme of citrulline utilization as nitrogen source
-
-
?
ATP + L-citrulline + L-Asp
AMP + diphosphate + L-argininosuccinate
-
-
-
?
ATP + L-citrulline + L-Asp
AMP + diphosphate + L-argininosuccinate
-
-
-
?
ATP + L-citrulline + L-Asp
AMP + diphosphate + L-argininosuccinate
-
-
-
?
ATP + L-citrulline + L-Asp
AMP + diphosphate + L-argininosuccinate
-
-
-
?
ATP + L-citrulline + L-Asp
AMP + diphosphate + L-argininosuccinate
-
-
-
?
ATP + L-citrulline + L-Asp
AMP + diphosphate + L-argininosuccinate
-
r
-
?
ATP + L-citrulline + L-Asp
AMP + diphosphate + L-argininosuccinate
-
D-Asp is inactive as substrate
-
?
ATP + L-citrulline + L-Asp
AMP + diphosphate + L-argininosuccinate
-
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
-
-
?
ATP + L-citrulline + L-Asp
AMP + diphosphate + L-argininosuccinate
-
argininosuccinate synthase expression is required to maintain nitric oxide production and cell viability in aortic endothelial cells
-
-
?
ATP + L-citrulline + L-Asp
AMP + diphosphate + L-argininosuccinate
-
-
-
?
ATP + L-citrulline + L-Asp
AMP + diphosphate + L-argininosuccinate
-
-
-
?
ATP + L-citrulline + L-Asp
AMP + diphosphate + L-argininosuccinate
-
-
-
?
ATP + L-citrulline + L-Asp
AMP + diphosphate + L-argininosuccinate
-
-
-
?
ATP + L-citrulline + L-Asp
AMP + diphosphate + L-argininosuccinate
-
-
-
?
ATP + L-citrulline + L-Asp
AMP + diphosphate + L-argininosuccinate
-
-
-
?
ATP + L-citrulline + L-Asp
AMP + diphosphate + L-argininosuccinate
-
-
-
?
ATP + L-citrulline + L-Asp
AMP + diphosphate + L-argininosuccinate
-
-
-
?
ATP + L-citrulline + L-Asp
AMP + diphosphate + L-argininosuccinate
-
IL-1beta stimulates argininosuccinate synthetase gene expression through NF-kappaB in Caco-2 cells
-
-
?
ATP + L-citrulline + L-Asp
AMP + diphosphate + L-argininosuccinate
-
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
-
-
?
ATP + L-citrulline + L-Asp
AMP + diphosphate + L-argininosuccinate
-
-
-
?
ATP + L-citrulline + L-Asp
AMP + diphosphate + L-argininosuccinate
-
-
-
?
ATP + L-citrulline + L-Asp
AMP + diphosphate + L-argininosuccinate
-
-
-
?
ATP + L-citrulline + L-Asp
AMP + diphosphate + L-argininosuccinate
-
-
-
?
ATP + L-citrulline + L-Asp
AMP + diphosphate + L-argininosuccinate
-
-
-
?
ATP + L-citrulline + L-Asp
AMP + diphosphate + L-argininosuccinate
-
-
-
?
ATP + L-citrulline + L-Asp
AMP + diphosphate + L-argininosuccinate
-
-
-
?
ATP + L-citrulline + L-Asp
AMP + diphosphate + L-argininosuccinate
-
-
-
?
ATP + L-citrulline + L-Asp
AMP + diphosphate + L-argininosuccinate
-
-
-
?
ATP + L-citrulline + L-Asp
AMP + diphosphate + L-argininosuccinate
-
-
-
?
ATP + L-citrulline + L-Asp
AMP + diphosphate + L-argininosuccinate
-
-
-
?
ATP + L-citrulline + L-Asp
AMP + diphosphate + L-argininosuccinate
-
r
-
?
ATP + L-citrulline + L-Asp
AMP + diphosphate + L-argininosuccinate
-
r
-
?
ATP + L-citrulline + L-Asp
AMP + diphosphate + L-argininosuccinate
-
r
-
?
ATP + L-citrulline + L-Asp
AMP + diphosphate + L-argininosuccinate
-
-
-
?
ATP + L-citrulline + L-aspartate
AMP + diphosphate + 2-(Nomega-L-arginino)succinate
-
-
-
-
?
ATP + L-citrulline + L-aspartate
AMP + diphosphate + 2-(Nomega-L-arginino)succinate
-
argininosuccinate synthase is essential for endothelial nitric oxide production, vascular NO production is regulated by dynamic argininosuccinate synthase phosphorylation
-
-
?
ATP + L-citrulline + L-aspartate
AMP + diphosphate + 2-(Nomega-L-arginino)succinate
-
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
-
-
?
ATP + L-citrulline + L-aspartate
AMP + diphosphate + 2-(Nomega-L-arginino)succinate
-
-
-
-
?
ATP + L-citrulline + L-aspartate
AMP + diphosphate + 2-(Nomega-L-arginino)succinate
-
-
-
?
ATP + L-citrulline + L-aspartate
AMP + diphosphate + 2-(Nomega-L-arginino)succinate
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
-
-
?
ATP + L-citrulline + L-aspartate
AMP + diphosphate + 2-(Nomega-L-arginino)succinate
rate-limiting enzyme in nitric oxide synthesis, negative feedback mechanism, overview
-
-
?
ATP + L-citrulline + L-aspartate
AMP + diphosphate + 2-(Nomega-L-arginino)succinate
-
the key enzyme in the urea cycle participates in many metabolic processes including arginine biosynthesis and the citrulline-nitric oxide cycle
-
-
?
ATP + L-citrulline + L-aspartate
AMP + diphosphate + 2-(Nomega-L-arginino)succinate
substrate binding structures, overview
-
-
?
ATP + L-citrulline + L-aspartate
AMP + diphosphate + 2-(Nomega-L-arginino)succinate
-
-
-
?
ATP + L-citrulline + L-aspartate
AMP + diphosphate + 2-(Nomega-L-arginino)succinate
-
-
-
-
?
ATP + L-citrulline + L-aspartate
AMP + diphosphate + 2-(Nomega-L-arginino)succinate
the enzyme plays an important role as the rate-limiting step required for converting L-citrulline to argininosuccinate to provide arginine
-
-
?
ATP + L-citrulline + L-aspartate
AMP + diphosphate + 2-(Nomega-L-arginino)succinate
-
-
-
?
ATP + L-citrulline + L-aspartate
AMP + diphosphate + 2-(Nomega-L-arginino)succinate
the enzyme plays an important role as the rate-limiting step required for converting L-citrulline to argininosuccinate to provide arginine
-
-
?
ATP + L-citrulline + L-aspartate
AMP + diphosphate + 2-(Nomega-L-arginino)succinate
-
-
-
-
?
ATP + L-citrulline + L-aspartate
AMP + diphosphate + 2-(Nomega-L-arginino)succinate
-
rate-limiting enzyme of the urea cycle
-
-
?
ATP + L-citrulline + L-aspartate
AMP + diphosphate + 2-(Nomega-L-arginino)succinate
-
-
-
-
?
ATP + L-citrulline + L-aspartate
AMP + diphosphate + 2-(Nomega-L-arginino)succinate
-
-
-
-
?
ATP + L-citrulline + L-aspartate
AMP + diphosphate + 2-(Nomega-L-arginino)succinate
-
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
-
-
?
ATP + L-citrulline + L-aspartate
AMP + diphosphate + 2-(Nomega-L-arginino)succinate
-
-
-
-
?
ATP + L-citrulline + L-aspartate
AMP + diphosphate + 2-(Nomega-L-arginino)succinate
-
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
-
-
?
ATP + L-citrulline + L-aspartate
AMP + diphosphate + L-argininosuccinate
-
catalyzes the coupling reaction between citrulline and arginine to form argininosuccinic acid
-
?
ATP + L-citrulline + L-aspartate
AMP + diphosphate + L-argininosuccinate
-
the rate-limiting enzyme for converting citrulline to arginine
-
?
ATP + L-citrulline + L-aspartate
AMP + diphosphate + L-argininosuccinate
-
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
-
r
ATP + L-citrulline + L-aspartate
AMP + diphosphate + L-argininosuccinate
-
ATP-dependent ligation of citrulline and aspartate
-
r
ATP + L-citrulline + L-aspartate
AMP + diphosphate + L-argininosuccinate
-
penultimate step in the biosnthesis of arginine, rate-limiting enzyme of both the urea and arginine-citrulline cycles
-
?
ATP + L-citrulline + L-aspartate
AMP + diphosphate + L-argininosuccinate
-
-
-
?
ATP + L-citrulline + L-aspartate
AMP + diphosphate + L-argininosuccinate
-
catalyzes the coupling reaction between citrulline and arginine to form argininosuccinic acid
-
?
ATP + L-citrulline + L-aspartate
AMP + diphosphate + L-argininosuccinate
-
the rate-limiting enzyme for converting citrulline to arginine
-
?
ATP + L-citrulline + L-aspartate
AMP + diphosphate + L-argininosuccinate
-
-
-
-
?
ATP + L-citrulline + L-aspartate
AMP + diphosphate + L-argininosuccinate
-
catalyzes the coupling reaction between citrulline and arginine to form argininosuccinic acid
-
?
ATP + L-citrulline + L-aspartate
AMP + diphosphate + L-argininosuccinate
-
the rate-limiting enzyme for converting citrulline to arginine
-
?
ATP + L-citrulline + L-aspartate
AMP + diphosphate + L-argininosuccinate
-
-
-
?
ATP + L-citrulline + L-aspartate
AMP + diphosphate + L-argininosuccinate
-
-
-
?
ATP + L-citrulline + L-aspartate
AMP + diphosphate + L-argininosuccinate
-
mediates transformation of L-citrulline to L-arginine in the ureum cycle in hepatocytes, first step in L-citrulline recycling pathway
-
?
ATP + L-citrulline + L-aspartate
AMP + diphosphate + L-argininosuccinate
-
-
-
-
?
ATP + L-citrulline + L-aspartate
AMP + diphosphate + L-argininosuccinate
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
-
r
ATP + L-citrulline + L-aspartate
AMP + diphosphate + L-argininosuccinate
-
ATP-dependent condensation of citrulline with aspartate, no conformational change upon binding of substrates, mechanism via citrullyl-AMP intermediate, active site structure
-
r
ATP + L-citrulline + L-aspartate
AMP + diphosphate + L-argininosuccinate
-
second step of urea cycle
-
?
ATP + L-citrulline + L-aspartate
AMP + diphosphate + L-argininosuccinate
seventh step of the arginine biosynthesis, second step of the urea cycle
-
?
ATP + L-citrulline + L-aspartate
AMP + diphosphate + L-argininosuccinate
-
ATP-dependent condensation of citrulline with aspartate, no conformational change upon binding of substrates, mechanism via citrullyl-AMP intermediate, active site structure
-
r
ATP + L-citrulline + L-aspartate
AMP + diphosphate + L-argininosuccinate
-
second step of urea cycle
-
?
ATP + L-citrulline + L-aspartate
AMP + diphosphate + L-argininosuccinate
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
-
r
ATP + L-citrulline + L-aspartate
AMP + diphosphate + L-argininosuccinate
seventh step of the arginine biosynthesis, second step of the urea cycle
-
?
additional information
?
-
-
urea cycle
-
?
additional information
?
-
-
citrullinemia is an autosomal recessive disease caused by a deficiency of argininosuccinate synthetase
-
-
?
additional information
?
-
-
adult-type citrullinemia with neuro-psychiatric symptoms of late onset, 24-28 years old, caused by argininosuccinate synthetase abnormalities
-
-
?
additional information
?
-
-
rate-limiting enzyme in the metabolic pathway leading from L-citrulline to L-arginine, urea cycle
-
?
additional information
?
-
-
factors like diets, hormones and pro-inflammatory stimuli regulate ASS gene expression primarily at the transcription level
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
pancreatic cancer cell lines deficient in argininosuccinate synthetase are sensitive to arginine deprivation by arginine deiminase
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
?
additional information
?
-
-
urea cycle, enzyme of citrulline-arginine recycling, which is important for high output production of NO in activated microglial cells, inducible enzyme
-
?
additional information
?
-
-
ASS binds to and inactivates lipopolysaccharide and lipid A, overview
-
-
?
additional information
?
-
-
involved in the recycling of L-citrulline to L-arginine
-
?
additional information
?
-
-
urea cycle, enzyme of citrulline-arginine recycling, which is important for high output production of NO in activated microglial cells, inducible enzyme
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ATP + L-citrulline + L-Asp
?
ATP + L-citrulline + L-Asp
AMP + diphosphate + L-argininosuccinate
ATP + L-citrulline + L-aspartate
AMP + diphosphate + 2-(Nomega-L-arginino)succinate
ATP + L-citrulline + L-aspartate
AMP + diphosphate + L-argininosuccinate
additional information
?
-
ATP + L-citrulline + L-Asp
?
-
urea-cycle enzyme
-
-
?
ATP + L-citrulline + L-Asp
?
-
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
-
-
?
ATP + L-citrulline + L-Asp
?
-
third reaction of urea cycle
-
-
?
ATP + L-citrulline + L-Asp
?
-
anabolic function in biosynthesis of Arg and catabolic function as the first enzyme of citrulline utilization as nitrogen source
-
-
?
ATP + L-citrulline + L-Asp
?
-
anabolic function in biosynthesis of Arg and catabolic function as the first enzyme of citrulline utilization as nitrogen source
-
-
?
ATP + L-citrulline + L-Asp
AMP + diphosphate + L-argininosuccinate
-
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
-
-
?
ATP + L-citrulline + L-Asp
AMP + diphosphate + L-argininosuccinate
-
argininosuccinate synthase expression is required to maintain nitric oxide production and cell viability in aortic endothelial cells
-
-
?
ATP + L-citrulline + L-Asp
AMP + diphosphate + L-argininosuccinate
-
IL-1beta stimulates argininosuccinate synthetase gene expression through NF-kappaB in Caco-2 cells
-
-
?
ATP + L-citrulline + L-Asp
AMP + diphosphate + L-argininosuccinate
-
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
-
-
?
ATP + L-citrulline + L-aspartate
AMP + diphosphate + 2-(Nomega-L-arginino)succinate
-
argininosuccinate synthase is essential for endothelial nitric oxide production, vascular NO production is regulated by dynamic argininosuccinate synthase phosphorylation
-
-
?
ATP + L-citrulline + L-aspartate
AMP + diphosphate + 2-(Nomega-L-arginino)succinate
-
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
-
-
?
ATP + L-citrulline + L-aspartate
AMP + diphosphate + 2-(Nomega-L-arginino)succinate
-
-
-
-
?
ATP + L-citrulline + L-aspartate
AMP + diphosphate + 2-(Nomega-L-arginino)succinate
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
-
-
?
ATP + L-citrulline + L-aspartate
AMP + diphosphate + 2-(Nomega-L-arginino)succinate
rate-limiting enzyme in nitric oxide synthesis, negative feedback mechanism, overview
-
-
?
ATP + L-citrulline + L-aspartate
AMP + diphosphate + 2-(Nomega-L-arginino)succinate
-
the key enzyme in the urea cycle participates in many metabolic processes including arginine biosynthesis and the citrulline-nitric oxide cycle
-
-
?
ATP + L-citrulline + L-aspartate
AMP + diphosphate + 2-(Nomega-L-arginino)succinate
-
-
-
?
ATP + L-citrulline + L-aspartate
AMP + diphosphate + 2-(Nomega-L-arginino)succinate
the enzyme plays an important role as the rate-limiting step required for converting L-citrulline to argininosuccinate to provide arginine
-
-
?
ATP + L-citrulline + L-aspartate
AMP + diphosphate + 2-(Nomega-L-arginino)succinate
the enzyme plays an important role as the rate-limiting step required for converting L-citrulline to argininosuccinate to provide arginine
-
-
?
ATP + L-citrulline + L-aspartate
AMP + diphosphate + 2-(Nomega-L-arginino)succinate
-
rate-limiting enzyme of the urea cycle
-
-
?
ATP + L-citrulline + L-aspartate
AMP + diphosphate + 2-(Nomega-L-arginino)succinate
-
-
-
-
?
ATP + L-citrulline + L-aspartate
AMP + diphosphate + 2-(Nomega-L-arginino)succinate
-
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
-
-
?
ATP + L-citrulline + L-aspartate
AMP + diphosphate + 2-(Nomega-L-arginino)succinate
-
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
-
-
?
ATP + L-citrulline + L-aspartate
AMP + diphosphate + L-argininosuccinate
-
the rate-limiting enzyme for converting citrulline to arginine
-
?
ATP + L-citrulline + L-aspartate
AMP + diphosphate + L-argininosuccinate
-
penultimate step in the biosnthesis of arginine, rate-limiting enzyme of both the urea and arginine-citrulline cycles
-
?
ATP + L-citrulline + L-aspartate
AMP + diphosphate + L-argininosuccinate
-
the rate-limiting enzyme for converting citrulline to arginine
-
?
ATP + L-citrulline + L-aspartate
AMP + diphosphate + L-argininosuccinate
-
the rate-limiting enzyme for converting citrulline to arginine
-
?
ATP + L-citrulline + L-aspartate
AMP + diphosphate + L-argininosuccinate
-
mediates transformation of L-citrulline to L-arginine in the ureum cycle in hepatocytes, first step in L-citrulline recycling pathway
-
?
ATP + L-citrulline + L-aspartate
AMP + diphosphate + L-argininosuccinate
-
second step of urea cycle
-
?
ATP + L-citrulline + L-aspartate
AMP + diphosphate + L-argininosuccinate
seventh step of the arginine biosynthesis, second step of the urea cycle
-
?
ATP + L-citrulline + L-aspartate
AMP + diphosphate + L-argininosuccinate
-
second step of urea cycle
-
?
ATP + L-citrulline + L-aspartate
AMP + diphosphate + L-argininosuccinate
seventh step of the arginine biosynthesis, second step of the urea cycle
-
?
additional information
?
-
-
urea cycle
-
?
additional information
?
-
-
citrullinemia is an autosomal recessive disease caused by a deficiency of argininosuccinate synthetase
-
-
?
additional information
?
-
-
adult-type citrullinemia with neuro-psychiatric symptoms of late onset, 24-28 years old, caused by argininosuccinate synthetase abnormalities
-
-
?
additional information
?
-
-
rate-limiting enzyme in the metabolic pathway leading from L-citrulline to L-arginine, urea cycle
-
?
additional information
?
-
-
factors like diets, hormones and pro-inflammatory stimuli regulate ASS gene expression primarily at the transcription level
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
pancreatic cancer cell lines deficient in argininosuccinate synthetase are sensitive to arginine deprivation by arginine deiminase
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
?
additional information
?
-
-
urea cycle, enzyme of citrulline-arginine recycling, which is important for high output production of NO in activated microglial cells, inducible enzyme
-
?
additional information
?
-
-
ASS binds to and inactivates lipopolysaccharide and lipid A, overview
-
-
?
additional information
?
-
-
involved in the recycling of L-citrulline to L-arginine
-
?
additional information
?
-
-
urea cycle, enzyme of citrulline-arginine recycling, which is important for high output production of NO in activated microglial cells, inducible enzyme
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Shargool, P.D.
Purification of argininosuccinate synthetase from cotyledons of germinating peas
Phytochemistry
10
2029-2032
1971
Pisum sativum
-
brenda
Ratner, S.
Enzymes of arginine and urea synthesis
Adv. Enzymol. Relat. Areas Mol. Biol.
39
1-90
1973
Bos taurus
brenda
Saheki, T.; Kusumi, T.; Takada, S.; Katsunuma, T.; Katunuma, N.
Crystallization and some properties of argininosuccinate synthetase from rat liver
FEBS Lett.
58
314-317
1975
Rattus norvegicus
brenda
Saheki, T.; Kusumi, T.; Takada, S.; Katsunuma, T.
Studies of rat liver argininosuccinate synthetase. I. Physicochemical, catalytic, and immunochemical properties
J. Biochem.
81
687-696
1977
Rattus norvegicus
brenda
Rochovansky, O.; Kodowaki, H.; Ratner, S.
Biosynthesis of urea. Molecular and regulatory properties of crystalline argininosuccinate synthetase
J. Biol. Chem.
252
5287-5294
1977
Bos taurus
brenda
Matsuda, Y.; Tsuji, A.; Katunuma, N.; Hayashi, M.; Takahashi, Y.
Studies on liver argininosuccinate synthetase in a patient with citrullinemia and in normal subjects
J. Biochem.
85
191-195
1979
Homo sapiens
brenda
Hilger, F.; Simon, J.P.; Stalon, V.
Yeast argininosuccinate synthetase. Purification, structural and kinetic properties
Eur. J. Biochem.
94
153-163
1979
Saccharomyces cerevisiae, Saccharomyces cerevisiae 1278b
brenda
Takada, S.; Saheki, T.; Igarashi, Y.; Katsunuma, T.
Studies on rat liver argininosuccinate synthetase. Inhibition by various amino acids
J. Biochem.
85
1309-1314
1979
Rattus norvegicus
brenda
O'Brien, W.E.
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
J. Biochem.
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
Homo sapiens, Rattus norvegicus
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
J. Biochem.
93
1531-1537
1983
Homo sapiens, Rattus norvegicus
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
Mol. Cell. Biochem.
143
47-51
1995
Rattus norvegicus
brenda
Demarquoy, J.; Fairand, A.; Gautier, C.; Vaillant, R.
Demonstration of argininosuccinate synthetase activity associated with mitochondrial membrane: characterization and hormonal regulation
Mol. Cell. Biochem.
136
145-155
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
brenda
Arnt-Ramos, L.R.; O'Brien, W.E.; Vincent, S.R.
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
Protein Seq. Data Anal.
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
Renal Physiol. Biochem.
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
J. Biochem.
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
Cancer Lett.
191
165-170
2003
Canis lupus familiaris, Homo sapiens, Mus musculus
brenda
Van Geldre, L.A.; Timmermans, J.P.; Lefebvre, R.A.
L-citrulline recycling by argininosuccinate synthetase and lyase in rat gastric fundus
Eur. J. Pharmacol.
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
Mus musculus, Rattus norvegicus
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
Neopyropia 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
Daucus carota, Rhizophagus intraradices
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
Homo sapiens, Mus musculus (P16460)
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
Mus musculus, Homo sapiens (P00966)
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
Pyrococcus furiosus, Saccharolobus solfataricus, 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