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Literature summary extracted from

  • Gu, J.; Yu, H.
    The role of residue S139 of mandelate racemase: synergistic effect of S139 and E317 on transition state stabilization (2012), J. Biomol. Struct. Dyn., 30, 585-593.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
5.1.2.2 S139A site-directed mutagenesis, the mutation leads to a significant reduction of catalytic efficiency by about 45fold and 60fold in R to S and S to R directions Pseudomonas putida

Natural Substrates/ Products (Substrates)

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

Organism

EC Number Organism UniProt Comment Textmining
5.1.2.2 Pseudomonas putida P11444
-
-

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
-
?

General Information

EC Number General Information Comment Organism
5.1.2.2 additional information significance of Ser139 in mandelate racemization, the active site residue S139 forms a hydrogen bond with one carboxyl oxygen of the substrate mandelate, residues S139 and E317 of mandelate racemase have a synergistic effect on transition state stabilization, overview Pseudomonas putida