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Literature summary extracted from

  • Karlberg, T.; Collins, R.; van den Berg, S.; Flores, A.; Hammarstroem, M.; Hoegbom, M.; Holmberg Schiavone, L.; Uppenberg, J.
    Structure of human argininosuccinate synthetase (2008), Acta Crystallogr. Sect. D, 64, 279-286.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
6.3.4.5 expression of ASS1 Homo sapiens

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
6.3.4.5 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 Homo sapiens

Protein Variants

EC Number Protein Variants Comment Organism
6.3.4.5 additional information clinical mutations, phenotypes, overview Homo sapiens

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
6.3.4.5 Mg2+
-
 Homo sapiens

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
6.3.4.5 ATP + L-citrulline + L-aspartate Homo sapiens 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 AMP + diphosphate + 2-(Nomega-L-arginino)succinate
-
 ?
6.3.4.5 additional information Homo sapiens 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 ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
6.3.4.5 Homo sapiens P00966 ASS1
-

Purification (Commentary)

EC Number Purification (Comment) Organism
6.3.4.5 recombinant ASS1 by His affinity chromatography and gel filtration Homo sapiens

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.3.4.5 ATP + L-citrulline + L-aspartate 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 Homo sapiens AMP + diphosphate + 2-(Nomega-L-arginino)succinate
-
 ?
6.3.4.5 ATP + L-citrulline + L-aspartate substrate binding structures, overview Homo sapiens AMP + diphosphate + 2-(Nomega-L-arginino)succinate
-
 ?
6.3.4.5 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 Homo sapiens ?
-
 ?

Subunits

EC Number Subunits Comment Organism
6.3.4.5 tetramer two dimers, dimeric and tetrameric interface structures, overview Homo sapiens

Synonyms

EC Number Synonyms Comment Organism
6.3.4.5 Argininosuccinate synthetase
-
 Homo sapiens
6.3.4.5 ASS
-
 Homo sapiens
6.3.4.5 Citrulline-aspartate ligase
-
 Homo sapiens

Cofactor

EC Number Cofactor Comment Organism Structure
6.3.4.5 ATP binding structure, conformational change upon ATP binding Homo sapiens