Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.1.3.2 extracted from

  • Stoisser, T.; Rainer, D.; Leitgeb, S.; Wilson, D.K.; Nidetzky, B.
    The Ala95-to-Gly substitution in Aerococcus viridans l-lactate oxidase revisited - structural consequences at the catalytic site and effect on reactivity with O2 and other electron acceptors (2015), FEBS J., 282, 562-578 .
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Aerococcus viridans

Crystallization (Commentary)

Crystallization (Comment) Organism
mutant A95G in complex with pyruvate, to 1.65 A resolution. Mutation leads to increased steric volume available in the active site Aerococcus viridans

Protein Variants

Protein Variants Comment Organism
A95G mutant is 3fold more reactive towards 2,6-dichlorophenol-indophenol than O2, whereas wildtype is 14fold more reactive towards O2 than 2,6-dichlorophenol-indophenol. Substituted 1,4-benzoquinones are up to 5fold better electron acceptors for reaction with L-lactate-reduced A95G variant than wild-type Aerococcus viridans

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information detailed analysis of reductive and oxidative half-reaction Aerococcus viridans

Organism

Organism UniProt Comment Textmining
Aerococcus viridans Q44467
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(S)-2-hydroxybutanoate + O2
-
Aerococcus viridans 2-oxobutanoate + H2O2
-
?
(S)-lactate + O2
-
Aerococcus viridans pyruvate + H2O2
-
?
(S)-mandelic acid + O2
-
Aerococcus viridans phenylpyruvate + H2O2
-
?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
140
-
(S)-lactate mutant A95G, pH 6.5, 20°C Aerococcus viridans
140
-
(S)-lactate wild-type, pH 6.5, 20°C Aerococcus viridans