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Literature summary for 6.3.4.5 extracted from

  • Lemke, C.T.; Howell, P.L.
    Substrate induced conformational changes in argininosuccinate synthetase (2002), J. Biol. Chem., 277, 13074-13081.
    View publication on PubMed
Search for more literature for 6.3.4.5

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli BB101 Escherichia coli

Crystallization (Commentary)

Crystallization (Comment) Organism
crystal strucures in complex with intact ATP and with ATP and citrulline, hanging drop vapour-diffusion technique, X-ray analysis Escherichia coli

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant EAS Escherichia coli

Reaction

Reaction Comment Organism Reaction ID
ATP + L-citrulline + L-aspartate = AMP + diphosphate + 2-(Nomega-L-arginino)succinate detailed catalytic mechanism Escherichia coli
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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
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
-
 ?

Subunits

Subunits Comment Organism
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

Synonyms

Synonyms Comment Organism
Argininosuccinate synthetase
-
 Escherichia coli
AS
-
 Escherichia coli
EAS
-
 Escherichia coli