1887

Abstract

2-Oxoglutarate decarboxylase from the lactic acid bacterium was purified by precipitation with PEG and ion-exchange chromatography. The strictly thiamin-pyrophosphate-dependent enzyme decarboxylated 2-oxoglutarate to succinic semialdehyde. Oxalacetate was metabolized to a lesser extent. The measured values for 2-oxoglutarate and thiamin pyrophosphate were 1 m and 0·03 m respectively. The enzyme had a molecular mass in the range 65–70 kDa, did not consist of subunits and showed significant similarities to the corresponding mitochondrial enzyme of .

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/content/journal/micro/10.1099/00221287-136-8-1497
1990-08-01
2021-05-17
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