The lactic acid oxidase of the mycobacteria

F. B. Cousins

Biochemical Journal · 1956 · 11 citations · 11 references

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Abstract

Although most of the mycobacteria can oxidize lactate, the rate of oxidation varies considerably from one species to another (see An aerobic dehydrogenase catalysing the overall re- action (1) was originally extracted from Mycobacterium phlei The enzyme was specific for the oxidation of L-lactate and did not oxidize pyruvate or acetate. CH3. CH(OH) . C02H + 02 = CH3 . CO2H + C02 + H20. (1) Anaerobically, with methylene blue as hydrogen acceptor, the crude enzyme preparation oxidized lactate to pyruvate. Since partially purified enzyme preparations contained flavin-adenine dinucleotide (FAD), it seemed that the enzyme might be a flavoprotein (F) operating as follows: CHR3. CH(OH) . CO2H + F =CH3.CO.CO2H+FH2, (2) FH2+02=F+H202,

References

11