Site-directed mutagenesis of the FAD-binding histidine of 6-hydroxy-D-nicotine oxidase
Author:
Publisher
Wiley
Subject
Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1016/0014-5793(89)81792-2/fullpdf
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2. Covalently Bound Flavin in d-6-Hydroxynicotine Oxidase from Arthrobacter oxidans. Identification of the 8alpha-(N-3-Histidyl)-riboflavin-Linkage between FAD and Apoenzyme
3. Covalent flavinylation of 6-hydroxy-D-nicotine oxidase involves an energy-requiring process
4. Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mpl8 and pUC19 vectors
5. Covalent flavinylation of 6-hydroxy-D-nicotine oxidase analyzed by partial deletions of the gene
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