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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粪链球菌丙酮酸脱氢酶多酶复合物二氢硫辛酰胺乙酰转移酶链中的两个硫辛酰结构域
影响因子：
3.5
作者：
A. Allen;R. Perham
通讯作者：
R. Perham
来自 Azotobacter vinelandii 的硫辛酰胺脱氢酶。
DOI：
--
发表时间：
1988
期刊：
European Journal of Biochemistry
影响因子：
--
作者：
A. Westphal;A. Kok
通讯作者：
A. Kok
大肠杆菌K12的硫辛酸酰胺脱氢酶基因的核苷酸序列。
DOI：
--
发表时间：
1983
期刊：
European Journal of Biochemistry
影响因子：
--
作者：
P. Stephens;H. Lewis;M. Darlison;J. Guest
通讯作者：
J. Guest
链球菌 NADH 过氧化物酶和 NADH 氧化酶：结构和机制方面
DOI：
10.1515/9783110855425-122
发表时间：
1991
期刊：
The Journal of pediatrics
影响因子：
--
作者：
A. Claiborne;S. A. Ahmed;P. Ross;H. Miller
通讯作者：
H. Miller
来自粪链球菌 10C1 的 NADH 过氧化物酶的结构以 2.16 A 分辨率进行精炼。
影响因子：
5.6
作者：
Stehle,T;Ahmed,SA;Claiborne,A;Schulz,GE
通讯作者：
Schulz,GE