The formylmethanofuran dehydrogenase isoenzymes in Methanobacterium wolfei and Methanobacterium thermoautotrophicum:: induction of the molybdenum isoenzyme by molybdate and constitutive synthesis of the tungsten isoenzyme

The formylmethanofuran dehydrogenase isoenzymes in Methanobacterium wolfei and Methanobacterium thermoautotrophicum:: induction of the molybdenum isoenzyme by molybdate and constitutive synthesis of the tungsten isoenzyme
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DOI:
10.1007/s002030050658
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发表时间:
1998-10-01
影响因子:
2.8
通讯作者:
Thauer, RK
Thauer, RK
中科院分区:
生物学4区
文献类型:
--
作者:
Hochheimer, A;Hedderich, R;Thauer, RK

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甲酰甲烷呋喃脱氢酶催化产甲烷古菌中二氧化碳生成甲烷的第一步。沃尔菲甲烷杆菌和自养甲烷杆菌含有两种同工酶,一种是含钨同工酶(Fwd),另一种是含钼同工酶(Fmd)。我们在这里报道,在这两种嗜热生物中,编码基因都组织在高度保守的fwdHFGDACB钨操纵子和fmdECB钼操纵子中。在这两种生物中,钨同工酶被发现是结构性转录的,而钼操纵子的转录是由钼酸盐诱导的。钨酸盐对钼酸盐诱导的影响不显著。
Formylmethanofuran dehydrogenase catalyzes the first step in methane formation from CO2 in methanogenic archaea. Methanobacterium wolfei and Methanobacterium thermoautotrophicum have been shown to contain two isoenzymes, a tungsten-containing isoenzyme (Fwd) and a molybdenum-containing isoenzyme (Fmd). We report here that in both thermophilic organisms the encoding genes are organized in a highly conserved fwdHFGDACB tungsten operon and in an fmdECB molybdenum operon. In both organisms, the tungsten isoenzyme was found to be constitutively transcribed, whereas the transcription of the molybdenum operon was induced by molybdate. Induction by molybdate was not significantly affected by tungstate.