PURIFICATION AND CHARACTERIZATION OF 2-OXOGLUTARATE DECARBOXYLASE OF LEUCONOSTOC-OENOS

被引:3
作者
KAPOL, R [1 ]
RADLER, F [1 ]
机构
[1] UNIV MAINZ, INST MIKROBIOL & WEINFORSCH, POSTFACH 3980, W-6500 MAINZ, GERMANY
来源
JOURNAL OF GENERAL MICROBIOLOGY | 1990年 / 136卷
关键词
D O I
10.1099/00221287-136-8-1497
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
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.
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页码:1497 / 1499
页数:3
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