The Structure Identifying of Coenzyme Oxidase NAD(P)H Based on Bioinformatics
Abstract: Coenzyme regeneration is the key to promote large-scale industrial application of oxidoreductase. Coenzyme oxidase (NOX) is an ideal candidate for industrial enzymes regeneration of NADH and NADPH. Based on sequence alignment tools and other bioinformatics methods, we analyze the amino acid sequence and high-level structural characteristics of NOX proteins, laying the foundation for future researches on the identification and transformation of coenzyme oxidase. Based on bioinformatics approaches, ClustalX 2.0, PyMOL 1.0 and other related software were used, and the nicotinamide coenzyme oxidase NOXs (the infer type or the known type) from Enterococcus faecalis, Lactococcus lactis, Methanocaldococcus jannaschii, Mycoplasma genitalium, Mycoplasma pneumoniae, Streptococcus pyogenes are compared for sequence alignment and homology modeling. The catalytically active sites, conservative characteristics of the active site amino acid residues and reaction mechanism were analyzed. Cofactors and important amino acid residues around them were identified. A lot of comparison analyses showed that NOX catalytic active sites presented important residues—Cys42 and cofactor FAD, and highly conserved residues—His10, Leu40 or Ser40 and Gly43 around them. The results can be used to guide future enzyme screening, modification and transformation of enzyme structure at the molecular level.
文章引用: 王世珍 , 王雅丽 , 李红春 , 李 昊 , 方柏山 (2014) 基于生物信息学对NAD(P)H辅酶氧化酶的结构识别。 生物物理学， 2， 30-37. doi: 10.12677/BIPHY.2014.23004
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