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Literature summary extracted from

  • Neidhart, D.J.; Kenyon, G.L.; Gerlt, J.A.; Petsko, G.A.
    Mandelate racemase and muconate lactonizing enzyme are mechanistically distinct and structurally homologous (1990), Nature, 347, 692-694.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
5.1.2.2 X-ray crystal structure of mandelate racemase solved at 2.5 A resolution, reveals that the sescondary, tertiary and quarternary structures of mandelate racemase and muconate lactonizing enzyme are remarkably similar Pseudomonas putida
5.5.1.1 X-ray crystal structure compared with that of mandelate racemase Pseudomonas putida

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
5.5.1.1 Mn2+ divalent metal ion is required, Mn2+ is preferred Pseudomonas putida

Organism

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

Reaction

EC Number Reaction Comment Organism Reaction ID
5.5.1.1 (+)-muconolactone = cis,cis-muconate reaction may proceed through formation of an intermediate carbanion located alpha to a carboxyl group, subsequent protonation of this putative carbanion, the carbanion is generated by attack of the remote carboxylate group on a double bond Pseudomonas putida
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5.1.2.2 D-mandelate
-
 Pseudomonas putida L-mandelate
-
 ?
5.5.1.1 cis,cis-Muconate
-
 Pseudomonas putida (+)-Muconolactone
-
 ?