RT Journal Article SR Electronic(1) A1 Kapol, Rainer A1 Radler, FerdinandYR 1990 T1 Purification and characterization of 2-oxoglutarate decarboxylase of Leuconostoc oenos JF Microbiology, VO 136 IS 8 SP 1497 OP 1499 DO https://doi.org/10.1099/00221287-136-8-1497 PB Microbiology Society, SN 1465-2080, AB 2-Oxoglutarate decarboxylase from the lactic acid bacterium Leuconostoc oenos 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 K m values for 2-oxoglutarate and thiamin pyrophosphate were 1 mm and 0·03 mm 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 Euglena gracilis., UL https://www.microbiologyresearch.org/content/journal/micro/10.1099/00221287-136-8-1497