EC Number | Cloned (Comment) | Organism |
---|---|---|
6.3.4.5 | expression in Escherichia coli BB101 | Escherichia coli |
EC Number | Crystallization (Comment) | Organism |
---|---|---|
6.3.4.5 | crystal strucures in complex with intact ATP and with ATP and citrulline, hanging drop vapour-diffusion technique, X-ray analysis | Escherichia coli |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
6.3.4.5 | ATP + L-citrulline + L-aspartate | Escherichia coli | penultimate step in the biosnthesis of arginine, rate-limiting enzyme of both the urea and arginine-citrulline cycles | AMP + diphosphate + L-argininosuccinate | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
6.3.4.5 | Escherichia coli | - |
- |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
6.3.4.5 | recombinant EAS | Escherichia coli |
EC Number | Reaction | Comment | Organism | Reaction ID |
---|---|---|---|---|
6.3.4.5 | ATP + L-citrulline + L-aspartate = AMP + diphosphate + 2-(Nomega-L-arginino)succinate | detailed catalytic mechanism | Escherichia coli |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
6.3.4.5 | ATP + L-citrulline + L-aspartate | 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 | Escherichia coli | AMP + diphosphate + L-argininosuccinate | - |
r | |
6.3.4.5 | ATP + L-citrulline + L-aspartate | penultimate step in the biosnthesis of arginine, rate-limiting enzyme of both the urea and arginine-citrulline cycles | Escherichia coli | AMP + diphosphate + L-argininosuccinate | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
6.3.4.5 | homotetramer | each monomer of tetrameric EAS consits of a nucleotide binding domain and a novel catalytic/multimerization domain, subunit/domain structure, subunit interactions | Escherichia coli |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
6.3.4.5 | Argininosuccinate synthetase | - |
Escherichia coli |
6.3.4.5 | AS | - |
Escherichia coli |
6.3.4.5 | EAS | - |
Escherichia coli |