Molecular cloning and analysis of the gene encoding the NADH oxidase from Streptococcus faecalis 10C1. Comparison with NADH peroxidase and the flavoprotein disulfide reductases.
Molecular cloning and analysis of the gene encoding the NADH oxidase from Streptococcus faecalis 10C1. Comparison with NADH peroxidase and the flavoprotein disulfide reductases.
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粪链球菌 10C1 NADH 氧化酶编码基因的分子克隆和分析。
DOI：
10.1016/0022-2836(92)90215-6
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发表时间：
1992
影响因子：
5.6
通讯作者：
Claiborne,A
中科院分区：
文献类型：
--
作者：
Ross,RP;Claiborne,A
The gene encoding the streptococcal flavoprotein NADH oxidase (NOXase), which catalyzes the four-electron reduction of O2→ 2H2O, has been cloned and sequenced from the genome ofStreptococcus (Enterococcus) faecalis10C1 (ATCC 11700). The deduced NOXase protein sequence corresponds to a molecular mass of 48.9 kDa and contains three previously sequenced cysteinyl peptides obtained with the purified enzyme. InEscherichia coli, the expressednoxgene produced a catalytically active product, which retained its immunoreactivity to affinity-purified NOXase antisera. Alignment of the NOXase protein sequence with that of streptococcal NADH peroxidase (NPXase) revealed that the proteins are 44% identical. Among the most highly conserved segments is a sequence containing Cys42; this residue is known to exist as a stabilized cysteine-sulfenic acid (Cys-SOH) in NPXase and serves as the non-flavin redox center. In addition, three previously identified NPXase segments, known to be involved in FAD and NAD(P)-binding in other pyridine nucleotide-linked flavoprotein oxidoreductases, are strongly conserved in NOXase. Overall, the extensive homology observed between NOXase and NPXase suggests that the monomer chain fold of the oxidase closely resembles that of the peroxidase. Both sequences share limited but significant homology to those of glutathione reductase and other members of the flavoprotein disulfide reductase family. These and other considerations suggest that these two unusual streptococcal flavoproteins constitute a distinct class of FAD-dependent oxidoreductases, the flavoprotein peroxide reductases, easily contrasted with enzymes such as glutathione reductase and thioredoxin reductase.
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影响因子：
3.5
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通讯作者：
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DOI：
--
发表时间：
1988
期刊：
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影响因子：
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通讯作者：
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DOI：
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发表时间：
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期刊：
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影响因子：
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作者：
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DOI：
10.1515/9783110855425-122
发表时间：
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期刊：
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影响因子：
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作者：
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通讯作者：
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DOI：
--
发表时间：
1990
期刊：
The Journal of biological chemistry
影响因子：
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作者：
Miller,H;Poole,LB;Claiborne,A
通讯作者：
Claiborne,A