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Literature summary for 1.1.99.31 extracted from

  • Lehoux, I.E.; Mitra, B.
    (S)-Mandelate dehydrogenase from Pseudomonas putida: mutations of the catalytic base histidine-274 and chemical rescue of activity (1999), Biochemistry, 38, 9948-9955.
    View publication on PubMed
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Protein Variants

Protein Variants Comment Organism
H274A inactive mutant, activity can partially be restored by the addition of exogenous imidazole Pseudomonas putida
H274D inactive mutant Pseudomonas putida
H274G inactive mutant, activity can be restored by the addition of exogenous imidazole Pseudomonas putida

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
13
-
 (S)-Mandelate mutant enzyme H274G, in presence of 20 mM imidazole Pseudomonas putida

Organism

Organism UniProt Comment Textmining
Pseudomonas putida
-
-
-

Purification (Commentary)

Purification (Comment) Organism
mutant enzymes H274G, H274A and H274N Pseudomonas putida

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(R,S)-p-chloromandelate + acceptor
-
 Pseudomonas putida ?
-
 ?
(S)-mandelate + acceptor
-
 Pseudomonas putida 2-oxo-2-phenylacetate + reduced acceptor
-
 ?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.03
-
 (R,S)-p-chloromandelate mutant enzyme H274G, in presence of 20 mM imidazole Pseudomonas putida
0.09
-
 (S)-Mandelate mutant enzyme H274G, in presence of 20 mM imidazole Pseudomonas putida