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Literature summary for 1.1.3.2 extracted from

  • Yorita, K.; Misaki, H.; Palfey, B.A.; Massey, V.
    On the interpretation of quantitative structure-function activity relationship data for lactate oxidase (2000), Proc. Natl. Acad. Sci. USA, 97, 2480-2485 .
    View publication on PubMedView publication on EuropePMC

Organism

Organism UniProt Comment Textmining
Aerococcus viridans Q44467
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-hydroxy-2-phenylacetate + O2
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Aerococcus viridans phenylpyruvate + H2O2
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L-lactate + O2
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Aerococcus viridans pyruvate + H2O2
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additional information a two-step equilibrium precedes the chemical reaction step, in which the second equilibrium step provides an upper limit to the rate with which the particular substrate or ligand is positioned with the flavin in the correct fashion. Results indicate development of significant negative charge in the transition states of the reactions. For reduction by substrate, the results are consistent either with a hydride transfer mechanism or with the carbanion mechanism, in which the substrate alpha-proton is abstracted by an enzyme base protected from exchange with solvent Aerococcus viridans ?
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Cofactor

Cofactor Comment Organism Structure
FMN removal of FMN and reconstitution of the apoprotein with 12 FMN derivatives with various substituents at the flavin 6- and 8-positions show an increase in the reduction rate constant with increasing redox potential, except that, with lactate, a limiting rate constant is obtained with flavins of high potential Aerococcus viridans