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.

引用

页码：1497 / 1499

页数：3

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