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Literature summary for 4.3.2.1 extracted from

  • Bhaumik, P.; Koski, M.K.; Bergmann, U.; Wierenga, R.K.
    Structure determination and refinement at 2.44 A resolution of argininosuccinate lyase from Escherichia coli (2004), Acta Crystallogr. Sect. D, 60, 1964-1970.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
-
Escherichia coli

Crystallization (Commentary)

Crystallization (Comment) Organism
crystallized from a highly concentrated sample of purified recombinant alpha-methylacyl-CoA-racemase with arginosuccinate lyase as a minor impurity, growing at room temperature in mother liquid consisting of 1.26 M ammonium phosphate pH 7.0, small bipyramidal crystals, molecular replacement at 2.44 A resolution Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
omega-N-(L-arginino)succinate Escherichia coli
-
L-arginine + fumarate
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
omega-N-(L-arginino)succinate
-
Escherichia coli L-arginine + fumarate
-
?

Subunits

Subunits Comment Organism
tetramer
-
Escherichia coli