Biochemical Journal · 1956 · 11 citations · 11 references
Life SciencesBiochemistryMicrobiologyEnzymologyMedical MicrobiologyMicrobial MetabolismAnaerobic BacteriologyLactic Acid Bacteria
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,
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A new method for preparing flavin-adenine dinucleotide
L. G. Whitby · Biochemical Journal · 1953 · 480 citations · Full text
A wet-crushing mill for micro-organisms
V. H. Booth, D. E. Green · Biochemical Journal · 1938 · 70 citations · Full text
THE INTERMEDIARY METABOLISM OF THE MYCOBACTERIA
N. L. Edson · Bacteriological Reviews · 1951 · 67 citations · Full text