Article
Histidine residues 102 and 117 of MelC1 play different roles in the chaperone function for Streptomyces apotyrosinase.
Biochemical and biophysical research communications - 14 Sept 1995
Liaw L L, Lee Y H
Abstract excerpt
MelC1 regulates the copper incorporation and secretion of Streptomyces apotyrosinase (MelC2) via a transient, competent complex formation. His-102 and His-117 of the chaperone-like MelC1 are known to play important roles in this trans-activation activity of MelC1. In this study, we studied the si...
Topics
- Amino Acid Sequence
- Apoenzymes
- Bacterial Proteins
- Base Sequence
- Chaperonins
- Copper
- Genes, Bacterial
- Histidine
- Molecular Chaperones
- Molecular Sequence Data
- Monophenol Monooxygenase
- Mutagenesis, Site-Directed
- Oligodeoxyribonucleotides
- Phenotype
- Protein Processing, Post-Translational
- Recombinant Proteins
- Streptomyces
- Trans-Activators