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Article

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

European journal of biochemistry - 15 Jun 1994

Veitch N C, Tams J W, Vind J, Dalbøge H, Welinder K G

Abstract excerpt

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 undertaken for comparison with the fungal enzyme and in order to establish a meaningful basis for solution studies of...

Topics

Amino Acid Sequence
Asparagine
Binding Sites
Coprinus
Glutamine
Heme
Magnetic Resonance Spectroscopy
Molecular Sequence Data
Mutagenesis, Site-Directed
Mutation
Peroxidase

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Phenylalanine

Recombinant Proteins

Substrate Specificity

Source

Identifiers

PMID: 8026500
DOI: 10.1111/j.1432-1033.1994.tb18939.x

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-8026500-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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