Cloned (Comment) | Organism |
---|---|
expression of ASS1 | Homo sapiens |
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 | Comment | Organism |
---|---|---|
additional information | clinical mutations, phenotypes, overview | Homo sapiens |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | - |
Homo sapiens |
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 | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | P00966 | ASS1 | - |
Purification (Comment) | Organism |
---|---|
recombinant ASS1 by His affinity chromatography and gel filtration | Homo sapiens |
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 | Comment | Organism |
---|---|---|
tetramer | two dimers, dimeric and tetrameric interface structures, overview | Homo sapiens |
Synonyms | Comment | Organism |
---|---|---|
Argininosuccinate synthetase | - |
Homo sapiens |
ASS | - |
Homo sapiens |
Citrulline-aspartate ligase | - |
Homo sapiens |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
ATP | binding structure, conformational change upon ATP binding | Homo sapiens |