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Mutation of Conserved Residues Increases in Vitro Activity of the Formylglycine-Generating Enzyme.
Journal article

Mutation of Conserved Residues Increases in Vitro Activity of the Formylglycine-Generating Enzyme.

  • Knop M Department of Chemistry, University of Basel, St. Johanns-Ring 19, 4056, Basel, Switzerland.
  • Lemnaru R Department of Chemistry, University of Basel, St. Johanns-Ring 19, 4056, Basel, Switzerland.
  • Seebeck FP Department of Chemistry, University of Basel, St. Johanns-Ring 19, 4056, Basel, Switzerland.
  • 2017-06-13
Published in:
  • Chembiochem : a European journal of chemical biology. - 2017
copper
formylglycine
mutagenesis
posttranslational modification
protein engineering
Actinobacteria
Amino Acid Motifs
Amino Acid Sequence
Bacterial Proteins
Catalytic Domain
Enzymes
Escherichia coli
Glycine
Humans
Kinetics
Mutagenesis, Site-Directed
Recombinant Proteins
Sequence Alignment
English The formylglycine-generating enzyme (FGE) recognizes proteins with a specific cysteine-containing six-amino-acid motif and converts this cysteine residue into formylglycine. The resulting aldehyde function provides a unique handle for selective protein labeling. We have identified two mutations in FGE from Thermomonospora curvata that increase this catalytic efficiency more than 40-fold. The resulting activity and stability, as well as its ease of recombinant production, make this FGE variant a practical reagent for in vitro protein engineering.
Language
  • English
Open access status
closed
Identifiers
Persistent URL
https://sonar.ch/global/documents/42578
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