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Literature summary 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)

EC Number Cloned (Comment) Organism
4.3.2.1
-
Escherichia coli

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
4.3.2.1 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)

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

Organism

EC Number Organism UniProt Comment Textmining
4.3.2.1 Escherichia coli
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.3.2.1
-
Escherichia coli

Substrates and Products (Substrate)

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

Subunits

EC Number Subunits Comment Organism
4.3.2.1 tetramer
-
Escherichia coli