Two malate dehydrogenases in Methanobacterium thermoautotrophicum

被引:30
作者
Thompson, H
Tersteegen, A
Thauer, RK
Hedderich, R
机构
[1] Max Planck Inst Terr Mikrobiol, D-35043 Marburg, Germany
[2] Univ Marburg, Mikrobiol Lab, Fachbereich Biol, D-35032 Marburg, Germany
关键词
Methanobacterium thermoautotrophicum; methanogenic archaea; malate dehydrogenase; transhydrogenase; lactate dehydrogenase;
D O I
10.1007/s002030050612
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
Methanobacterium thermoautotrophicum (strain Marburg) was found to contain two malate dehydrogenases, which were partially purified and characterized. One was specific for NAD(+) and catalyzed the dehydrogenation of malate at approximately one-third of the rate of oxalacetate reduction, and the other could equally well use NAD(+) and NADP(+) as coenzyme and catalyzed essentially only the reduction of oxalacetate. Via the N-terminal amino acid sequences, the encoding genes were identified in the genome of M. thermoautotrophicum (strain Delta H). Comparison of the deduced amino acid sequences revealed that the two malate dehydrogenases are phylogenetically only distantly related. The NAD(+)-specific malate dehydrogenase showed high sequence similarity to L-malate dehydrogenase from Methanothermus fervidus, and the NAD(P)(+)-using malate dehyrogenase showed high sequence similarity to L-lactate dehydrogenase from Thermotoga maritima and L-malate dehydrogenase from Bacillus subtilis. A function of the two malate dehydrogenases in NADPH:NAD(+) transhydrogenation is discussed.
引用
收藏
页码:38 / 42
页数:5
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