Literature summary for 6.3.4.5 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.

Search for more literature for 6.3.4.5

Cloned(Commentary)

Cloned (Comment)	Organism
expression of ASS1	Homo sapiens

Crystallization (Commentary)

Crystallization (Comment)	Organism
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

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

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	-	Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
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	-	?
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

Organism	UniProt	Comment	Textmining
Homo sapiens	P00966	ASS1	-

Purification (Commentary)

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

Substrates and Products (Substrate)

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

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

Synonyms

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

Cofactor

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

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Release 2023.1 (January 2023)