NMR studies of recombinant Coprinus peroxidase and three site-directed mutants. Implications for peroxidase substrate binding

Proton nuclear magnetic resonance spectroscopy has been used to characterise and compare wild-type fungal and recombinant Coprinus cinereus peroxidase (CIP) and three mutants in which Gly156 and/or Asn157 was replaced by Phe. Analysis of one- and two-dimensional NMR spectra of recombinant CIP was un...

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Veröffentlicht in:	European journal of biochemistry 1994, Vol.222 (3), p.909-918
Hauptverfasser:	Veitch, N.C, Tams, J.W, Vind, J, Dalboge, H, Welinder, K.G
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence amino acid sequences Asparagine - chemistry binding Binding Sites Coprinus Coprinus - enzymology Coprinus cinereus Glutamine - chemistry Heme - chemistry Magnetic Resonance Spectroscopy Molecular Sequence Data Mutagenesis, Site-Directed mutants Mutation peroxidase Peroxidase - chemistry Peroxidase - genetics phenylalanine Phenylalanine - chemistry Recombinant Proteins - chemistry spectral analysis Substrate Specificity
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