Article
Structure-function relationships within the peptide deformylase family. Evidence for a conserved architecture of the active site involving three conserved motifs and a metal ion.
Journal of molecular biology - 4 Apr 1997
Meinnel T, Lazennec C, Villoing S, Blanquet S
Abstract excerpt
Thermus thermophilus peptide deformylase was characterized. Its enzymatic properties as well as its organization in domains proved to share close resemblances with those of the Escherichia coli enzyme despite few sequence identities. In addition to the HEXXH signature sequence of the zinc metallo...
Topics
- Amidohydrolases
- Amino Acid Sequence
- Aminopeptidases
- Binding Sites
- Conserved Sequence
- Escherichia coli
- Geobacillus stearothermophilus
- Metalloendopeptidases
- Models, Molecular
- Molecular Sequence Data
- Mutation
- Sequence Alignment
- Sequence Homology, Amino Acid
- Structure-Activity Relationship
- Thermus thermophilus
- Zinc