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Literature summary for 5.1.2.2 extracted from

  • Schafer, S.L.; Barrett, W.C.; Kallarakal, A.T.; Mitra, B.; Kozarich, J.W.; Gerlt, J.A.
    Mechanism of the reaction catalyzed by mandelate racemase: structure and mechanistic properties of the D270N mutant (1996), Biochemistry, 35, 5662-5669.
    View publication on PubMed
Search for more literature for 5.1.2.2

Protein Variants

Protein Variants Comment Organism
D270N structure of D270N with (S)-atrolactate bound in the active site reveals no geometric alterations when compared to the structure of the wild type enzyme complexed with (S)-atrolactate, with the exception that the side chain of His297 is tilted and displaced about 0.5A away from Asn270 and towards the (S)-atrolactate. The turnover number for both (R)-mandelate and (S)-mandelate are reduced 10000fold Pseudomonas putida

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.5
-
 (R)-mandelate D270N mutant Pseudomonas putida
2.1
-
 (S)-Mandelate D270N mutant Pseudomonas putida

Organism

Organism UniProt Comment Textmining
Pseudomonas putida P11444 wild type and mutant D270N
-

Reaction

Reaction Comment Organism Reaction ID
(S)-mandelate = (R)-mandelate His297 and Asp270 function together as a catalytic dyad Pseudomonas putida
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-mandelate
-
 Pseudomonas putida L-mandelate
-
 ?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
additional information
-
 additional information dependence of turnover number on pH Pseudomonas putida
0.018
-
 (R)-mandelate D270N mutant Pseudomonas putida
0.037
-
 (S)-Mandelate D270N mutant Pseudomonas putida
0.21
-
 (R)-mandelate mutant K166R Pseudomonas putida

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7 8.5 wild type enzyme Pseudomonas putida