However, transitions were observed at +160mV and –240mV, which are likely due to the presence FMN in the FAD-binding site. Redox measurements were hindered in Y459H by the instability of the protein. Diminished FAD-binding specificity, caused by both Y459H and V492E mutations, resulted ...
FAD-binding 例句 释义: 全部 更多例句筛选 1. Cloning and Expression of Inducible Nitric Oxide Synthase FAD-Binding Domain and Its Binding Activity to FAD 诱生型一氧化氮合酶FAD结合区的克隆、表达和活性鉴定 www.ilib.cn隐私声明 法律声明 广告 反馈 © 2025 Microsoft...
Erv2p is an FAD-dependent sulfhydryl oxidase that can promote disulfide bond formation during protein biosynthesis in the yeast endoplasmic reticulum. The structure of Erv2p, determined by X-ray crystallography to 1.5 Å resolution, reveals a helix-ric
(1989) Site-directed mutagenesis of the FAD-binding histidine of 6-Hydroxy-D-nicotine oxidase. Conse- quences on flavinylation and enzyme activity. FEBS Lett. 257: 86-88.Ludwig Mauch,Veronika Bichler and Roderich Brandsch.Site-directed mutagenesis of the FAD-binding histidine of 6-hydroxy-D-...
Keywords:sequencemotif;Rossmannfold;hydrogenbond;FAD-binding; NAD(P)-binding*Correspondingauthor Introduction GXXXGisanaminoacidsequencemotifthat stabilizeshelix–helixinteractionsinbothmem- braneandsolubleproteins.TheGXXXGsequence motifhasbeenfoundintransmembranea-helices, ...
Interestingly, the mutant generated by changing the first glycine of the proposed FAD-binding domain (GxGxxG) to alanine revealed catalytic activities, but was lower than those seen with the unmodified form. The conversion of the first glycine to alanine markedly increased and decreased the K m ...
Cytochrome b-245 appears to bind both the haem and FAD, in a molar ratio of 2:1. The e.p.r. signal of the purified cytochrome was weak and had an asymmetric g(z) peak at g = 3.31. The purified cytochrome could be partially reflavinated (about 20%) in the presence of lipid. ...
The results provide direct evidence for the structure of the N-terminal modification of the protein and for the existence of the FAD and NADP binding domains of Gly-X-Gly-X-X-Gly.References (22) R.E. Tynes et al. Arch. Biochem. Biophys (1985) L.L. Poulsen et al. J. Biol. Chem...
(2014), Bacterial NDH-2 protomer (in grey ribbon) viewed from the side displaying the binding regions of FAD, (putative) aqueous NADH (yellow) and lipophilic quinone (orange). The membrane- anchoring region is highlighted in magenta. For further details readers are referred to the article by...
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