1.1.3.2 (R)-lactate + 2,6-dichlorophenolindophenol no decarboxylation Gram-negative soil bacterium ? - ? 289450 1.1.3.2 (R)-lactate + 2,6-dichlorophenolindophenol no decarboxylation Gram-negative soil bacterium KY6 ? - ? 289450 1.1.3.2 (S)-2-hydroxy-2-phenylacetate + O2 - Aerococcus viridans phenylpyruvate + H2O2 - ? 442668 1.1.3.2 (S)-2-hydroxybutanoate + O2 - Aerococcus viridans 2-oxobutanoate + H2O2 - ? 442669 1.1.3.2 (S)-lactate + 2,6-dichlorophenolindophenol no decarboxylation Gram-negative soil bacterium pyruvate + ? - ? 289448 1.1.3.2 (S)-lactate + 2,6-dichlorophenolindophenol no decarboxylation Gram-negative soil bacterium KY6 pyruvate + ? - ? 289448 1.1.3.2 (S)-lactate + O2 - Yarrowia lipolytica pyruvate + H2O2 - ? 289436 1.1.3.2 (S)-lactate + O2 - Pediococcus sp. pyruvate + H2O2 - ? 289436 1.1.3.2 (S)-lactate + O2 - Aerococcus viridans pyruvate + H2O2 - ? 289436 1.1.3.2 (S)-lactate + O2 strict specificity to L-lactate. The enzyme does not oxidize fumarate, pyruvate, succinate, ascorbate, dihydroxyacetone, glycolate, D-lactate, D,L-2-hydroxybutyrate and D,L-alanine or D-serine Yarrowia lipolytica pyruvate + H2O2 - ? 289436 1.1.3.2 (S)-lactate + O2 - Yarrowia lipolytica VKM Y-47 pyruvate + H2O2 - ? 289436 1.1.3.2 (S)-lactate + O2 strict specificity to L-lactate. The enzyme does not oxidize fumarate, pyruvate, succinate, ascorbate, dihydroxyacetone, glycolate, D-lactate, D,L-2-hydroxybutyrate and D,L-alanine or D-serine Yarrowia lipolytica VKM Y-47 pyruvate + H2O2 - ? 289436 1.1.3.2 (S)-lactate + O2 - Aerococcus viridans ATCC 11563 pyruvate + H2O2 - ? 289436 1.1.3.2 (S)-lactate + O2 - Yarrowia lipolytica VKM Y-2378 pyruvate + H2O2 - ? 289436 1.1.3.2 (S)-lactate + O2 strict specificity to L-lactate. The enzyme does not oxidize fumarate, pyruvate, succinate, ascorbate, dihydroxyacetone, glycolate, D-lactate, D,L-2-hydroxybutyrate and D,L-alanine or D-serine Yarrowia lipolytica VKM Y-2378 pyruvate + H2O2 - ? 289436 1.1.3.2 (S)-lactate + O2 - Yarrowia lipolytica VKM Y-2373 pyruvate + H2O2 - ? 289436 1.1.3.2 (S)-lactate + O2 strict specificity to L-lactate. The enzyme does not oxidize fumarate, pyruvate, succinate, ascorbate, dihydroxyacetone, glycolate, D-lactate, D,L-2-hydroxybutyrate and D,L-alanine or D-serine Yarrowia lipolytica VKM Y-2373 pyruvate + H2O2 - ? 289436 1.1.3.2 (S)-lactate + O2 - Yarrowia lipolytica 655 pyruvate + H2O2 - ? 289436 1.1.3.2 (S)-lactate + O2 strict specificity to L-lactate. The enzyme does not oxidize fumarate, pyruvate, succinate, ascorbate, dihydroxyacetone, glycolate, D-lactate, D,L-2-hydroxybutyrate and D,L-alanine or D-serine Yarrowia lipolytica 655 pyruvate + H2O2 - ? 289436 1.1.3.2 (S)-lactate + O2 - Yarrowia lipolytica 672 pyruvate + H2O2 - ? 289436 1.1.3.2 (S)-lactate + O2 strict specificity to L-lactate. The enzyme does not oxidize fumarate, pyruvate, succinate, ascorbate, dihydroxyacetone, glycolate, D-lactate, D,L-2-hydroxybutyrate and D,L-alanine or D-serine Yarrowia lipolytica 672 pyruvate + H2O2 - ? 289436 1.1.3.2 (S)-lactate + O2 - Yarrowia lipolytica 667 pyruvate + H2O2 - ? 289436 1.1.3.2 (S)-lactate + O2 strict specificity to L-lactate. The enzyme does not oxidize fumarate, pyruvate, succinate, ascorbate, dihydroxyacetone, glycolate, D-lactate, D,L-2-hydroxybutyrate and D,L-alanine or D-serine Yarrowia lipolytica 667 pyruvate + H2O2 - ? 289436 1.1.3.2 (S)-lactate + O2 - Yarrowia lipolytica 668 pyruvate + H2O2 - ? 289436 1.1.3.2 (S)-lactate + O2 strict specificity to L-lactate. The enzyme does not oxidize fumarate, pyruvate, succinate, ascorbate, dihydroxyacetone, glycolate, D-lactate, D,L-2-hydroxybutyrate and D,L-alanine or D-serine Yarrowia lipolytica 668 pyruvate + H2O2 - ? 289436 1.1.3.2 (S)-lactate + O2 - Yarrowia lipolytica 585 pyruvate + H2O2 - ? 289436 1.1.3.2 (S)-lactate + O2 strict specificity to L-lactate. The enzyme does not oxidize fumarate, pyruvate, succinate, ascorbate, dihydroxyacetone, glycolate, D-lactate, D,L-2-hydroxybutyrate and D,L-alanine or D-serine Yarrowia lipolytica 585 pyruvate + H2O2 - ? 289436 1.1.3.2 (S)-lactate + O2 - Yarrowia lipolytica 645 pyruvate + H2O2 - ? 289436 1.1.3.2 (S)-lactate + O2 strict specificity to L-lactate. The enzyme does not oxidize fumarate, pyruvate, succinate, ascorbate, dihydroxyacetone, glycolate, D-lactate, D,L-2-hydroxybutyrate and D,L-alanine or D-serine Yarrowia lipolytica 645 pyruvate + H2O2 - ? 289436 1.1.3.2 (S)-lactate + O2 - Yarrowia lipolytica 646 pyruvate + H2O2 - ? 289436 1.1.3.2 (S)-lactate + O2 strict specificity to L-lactate. The enzyme does not oxidize fumarate, pyruvate, succinate, ascorbate, dihydroxyacetone, glycolate, D-lactate, D,L-2-hydroxybutyrate and D,L-alanine or D-serine Yarrowia lipolytica 646 pyruvate + H2O2 - ? 289436 1.1.3.2 (S)-mandelic acid + O2 - Aerococcus viridans phenylpyruvate + H2O2 - ? 442674 1.1.3.2 2-hydroxy-2-(4-chlorophenyl)acetate + O2 - Aerococcus viridans (4-chlorophenyl)pyruvate + H2O2 - ? 442796 1.1.3.2 2-hydroxy-2-(4-hydroxyphenyl)acetate + O2 - Aerococcus viridans (4-hydroxyphenyl)pyruvate + H2O2 - ? 442797 1.1.3.2 2-hydroxy-2-(4-methoxyphenyl)acetate + O2 - Aerococcus viridans (4-methoxyphenyl)pyruvate + H2O2 - ? 442798 1.1.3.2 2-hydroxy-2-(4-methylphenyl)acetate + O2 - Aerococcus viridans (4-methylphenyl)pyruvate + H2O2 - ? 442799 1.1.3.2 2-hydroxy-2-(4-nitrophenyl)acetate + O2 - Aerococcus viridans (4-nitrophenyl)pyruvate + H2O2 - ? 442800 1.1.3.2 2-hydroxy-2-phenylacetate + O2 - Aerococcus viridans phenylpyruvate + H2O2 - ? 442801 1.1.3.2 2-hydroxybutanoate + O2 - Aerococcus viridans 2-oxobutanoate + H2O2 - ? 442803 1.1.3.2 2-hydroxypentanoate + O2 - Aerococcus viridans 2-oxopentanoate + H2O2 - ? 442806 1.1.3.2 glycerate + O2 - Aerococcus viridans hydroxypyruvate + H2O2 - ? 443607 1.1.3.2 glycerate + O2 5.9% of the activity with L-lactate Nostoc sp. PCC 7120 = FACHB-418 hydroxypyruvate + H2O2 - ? 443607 1.1.3.2 glycolate + 2,6-dichlorophenolindophenol no decarboxylation Gram-negative soil bacterium ? - ? 289453 1.1.3.2 glycolate + 2,6-dichlorophenolindophenol no decarboxylation Gram-negative soil bacterium KY6 ? - ? 289453 1.1.3.2 glyoxylate + O2 15.3% of the activity with L-lactate Nostoc sp. PCC 7120 = FACHB-418 oxalate + H2O2 - ? 289439 1.1.3.2 L-2-hydroxyisocaproate + 2,6-dichlorophenolindophenol no decarboxylation Gram-negative soil bacterium ? - ? 289452 1.1.3.2 L-2-hydroxyisocaproate + 2,6-dichlorophenolindophenol no decarboxylation Gram-negative soil bacterium KY6 ? - ? 289452 1.1.3.2 L-alpha-hydroxy-beta-methylvalerate + O2 - Aerococcus viridans 3-methyl-2-oxopentanoate + H2O2 - ? 443672 1.1.3.2 L-lactate + O2 - Aerococcus viridans pyruvate + H2O2 - ? 257487 1.1.3.2 L-lactate + O2 - Nostoc sp. PCC 7120 = FACHB-418 pyruvate + H2O2 - ? 257487 1.1.3.2 L-lactate + O2 - Chlamydomonas reinhardtii pyruvate + H2O2 - ? 257487 1.1.3.2 L-malic acid + 2,6-dichlorophenolindophenol no decarboxylation Gram-negative soil bacterium ? - ? 289454 1.1.3.2 lactate + 2,6-dichlorophenolindophenol no decarboxylation Gram-negative soil bacterium ? - ? 289451 1.1.3.2 lactate + 2,6-dichlorophenolindophenol no decarboxylation Gram-negative soil bacterium KY6 ? - ? 289451 1.1.3.2 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 ? - ? 89 1.1.3.2 additional information contrary to lactate monooxygenase, with lactate oxidase the complex of reduced flavin enzyme and pyruvate dissociates rapidly, with the result that it is the free reduced flavin form of the enzyme that reacts with O2, to give the observed products, pyruvate and H2O2 Aerococcus viridans ? - ? 89 1.1.3.2 additional information enzyme is highly specific for L-lactate. No substrates: D-lactate, glycolate and DL-2-hydroxybutanoate Aerococcus viridans ? - ? 89 1.1.3.2 additional information mechanism with little development of charge in the transition state, such as a transfer of hydride to the flavin N(5) position or a synchronous mechanism in which the alpha-C-H is formally abstracted as a H+ while the resulting charge is simultaneously neutralized by another event Aerococcus viridans ? - ? 89 1.1.3.2 additional information no substrate: D-lactate. Poor substrate: glycolate Nostoc sp. PCC 7120 = FACHB-418 ? - ? 89 1.1.3.2 additional information no substrate: D-lactate. Poor substrate: glycolate Chlamydomonas reinhardtii ? - ? 89 1.1.3.2 additional information redox potential difference is a dominant factor in determing rate of reduction. The enzyme reconstituted with a series of flavins modified at 6 or 8 position of the isoalloxazine ring shows a close linear relationship between reduction rate constant and redox potential in the ranges of -250 mV to -100 mV when L-lactate is used as substrate. The reconstituted enzyme shows a close linear relationship in the ranges of -150 mV to +100 mV when L-mandelate is used as substrate Aerococcus viridans ? - ? 89