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Literature summary for 1.1.3.2 extracted from

  • Stoisser, T.; Klimacek, M.; Wilson, D.K.; Nidetzky, B.
    Speeding up the product release a second-sphere contribution from Tyr191 to the reactivity of L-lactate oxidase revealed in crystallographic and kinetic studies of site-directed variants (2015), FEBS J., 282, 4130-4140 .
    View publication on PubMed
Search for more literature for 1.1.3.2

Crystallization (Commentary)

Crystallization (Comment) Organism
1.9 A crystal structure, Y191F variant bound with FMN and pyruvate. Mutation has a strictly locally disruptive effect Aerococcus viridans

Protein Variants

Protein Variants Comment Organism
Y191A 28fold decrease in release of pyruvate, , binding of L-lactate is strongly affected Aerococcus viridans
Y191F 4.7fold decrease in release of pyruvate Aerococcus viridans
Y191L 19fold decrease in release of pyruvate, binding of L-lactate is strongly affected Aerococcus viridans

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.08
-
 (S)-lactate mutant Y191F, pH 6.5, 20°C Aerococcus viridans
0.5
-
 (S)-lactate wild-type, pH 6.5, 20°C Aerococcus viridans
1.5
-
 (S)-lactate mutant Y191L, pH 6.5, 20°C Aerococcus viridans
46
-
 (S)-lactate mutant Y191A, pH 6.5, 20°C Aerococcus viridans

Organism

Organism UniProt Comment Textmining
Aerococcus viridans Q44467
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(S)-lactate + O2
-
 Aerococcus viridans pyruvate + H2O2
-
 ?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
5
-
 (S)-lactate mutant Y191A, pH 6.5, 20°C Aerococcus viridans
7.5
-
 (S)-lactate mutant Y191L, pH 6.5, 20°C Aerococcus viridans
22
-
 (S)-lactate mutant Y191F, pH 6.5, 20°C Aerococcus viridans
88
-
 (S)-lactate wild-type, pH 6.5, 20°C Aerococcus viridans