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Literature summary extracted from

  • Britton, K.L.; Abeysinghe, I.S.B.; Baker, P.J.; Barynin, V.; Diehl, P.; Langridge, S.J.; McFadden, B.A.; Sedelnikova, S.E.; Stillman, T.J.; Weeradechapon, K.; Rice, D.W.
    The structure and domain organization of Escherichia coli isocitrate lyase (2001), Acta Crystallogr. Sect. D, D57, 1209-1218.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
4.1.3.1 hanging drop vapor diffusion method Escherichia coli

Protein Variants

EC Number Protein Variants Comment Organism
4.1.3.1 A219C similar catalytic properties as the wild-type enzyme Escherichia coli

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
4.1.3.1 cytoplasm
-
 Escherichia coli 5737
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.1.3.1 isocitrate Escherichia coli first step in glyoxylate-bypass pathway succinate + glyoxylate
-
 ?

Organism

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

Purification (Commentary)

EC Number Purification (Comment) Organism
4.1.3.1
-
 Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.3.1 isocitrate
-
 Escherichia coli succinate + glyoxylate
-
 ?
4.1.3.1 isocitrate first step in glyoxylate-bypass pathway Escherichia coli succinate + glyoxylate
-
 ?

Subunits

EC Number Subunits Comment Organism
4.1.3.1 tetramer monomers are identical, crystallization experiments Escherichia coli