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Literature summary extracted from

  • Choi, W.J.; Lee, K.Y.; Kang, S.H.; Lee, S.B.
    Biocatalytic enantioconvergent separation of racemic mandelic acid (2007), Sep. Purif. Technol., 53, 178-182.
No PubMed abstract available

Application

EC Number Application Comment Organism
5.1.2.2 biotechnology the demonstrated application of a membrane bioreactor will be a useful method for large-scale dynamic kinetic resulution (DKR) of mandelic acid and for possible other bioconversions in organic media Pseudomonas putida

Cloned(Commentary)

EC Number Cloned (Comment) Organism
5.1.2.2 expressed ind Escherichia coli Pseudomonas putida

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
5.1.2.2 0.548
-
(S)-Mandelate
-
Pseudomonas putida

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
5.1.2.2 42000
-
SDS-PAGE Pseudomonas putida

Organism

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

Reaction

EC Number Reaction Comment Organism Reaction ID
5.1.2.2 (S)-mandelate = (R)-mandelate one pot enantioconvergent synthesis of R-mandelic acid ester from racemic mandelic acid is achieved by a novel aqueous/organic two-phase system with two-enzyme process consisting of (1) lipase-catalyzed enantioselective esterification of racemic mandelic acid in organic solvent and (2) in situ racemization of unreacted isomer, S-mandelic acid in aqueous phase by recombinant mandelate racemase Pseudomonas putida

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5.1.2.2 (S)-mandelate
-
Pseudomonas putida (R)-mandelate
-
?

Synonyms

EC Number Synonyms Comment Organism
5.1.2.2 mandelate racemase
-
Pseudomonas putida

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
5.1.2.2 650
-
(S)-Mandelate
-
Pseudomonas putida