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...
(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-...
The structure of Erv2p, determined by X-ray crystallography to 1.5 Å resolution, reveals a helix-rich dimer with no global resemblance to other known FAD-binding proteins or thiol oxidoreductases. Two pairs of cysteine residues are required for Erv2p activity. The first (Cys-Gly-Glu-Cys) ...
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 ...
GXXXG and GXXXA Motifs Stabilize FAD and NAD(P)-binding Rossmann Folds Through Cα–HO Hydrogen Bonds and van der Waals Interactions Kleiger,G. and Eisenberg,D. (2002) GXXXG and GXXXA motifs stabilize FAD and NAD(P)-binding Rossmann folds through C(alpha)-H * * * O hydrogen... ...
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...
FAD or NAD(P)-binding Rossmannfold. The Rossmann fold is one of the three most highly representedfolds in the Protein Data Bank (PDB). A subset of the proteins that adoptthe Rossmann fold also bind to nucleotide cofactors such as FAD andNAD(P) and function as oxidoreductases. These ...
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