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Literature summary extracted from

  • Hasson, M.S.; Schlichting, I.; Moulai, J.; Taylor, K.; Barrett, W.; Kenyon, G.L.; Babbitt, P.C.; Gerlt, J.A.; Petsko, G.A.; Ringe, D.
    Evolution of an enzyme active site: the structure of a new crystal form of muconate lactonizing enzyme compared with mandelate racemase and enolase (1998), Proc. Natl. Acad. Sci. USA, 95, 10396-10401.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
5.5.1.1 hanging drop vapor diffusion method, packing of the octameric enzyme in the crystal form is unusual, because the asymmetric unit contains three subunits Pseudomonas putida

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
5.5.1.1 additional information Pseudomonas putida the enzyme is a component of the beta-ketoadipate pathway ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
5.5.1.1 Pseudomonas putida
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
5.5.1.1 recombinant enzyme expressed in Escherichia coli JM105 Pseudomonas putida

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5.5.1.1 additional information the enzyme is a component of the beta-ketoadipate pathway Pseudomonas putida ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
5.5.1.1 MLE
-
 Pseudomonas putida