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Photochemical regulation of the activity of an endonuclease BamHI using an azobenzene moiety incorporated site-selectively into the dimer interface.
- Source :
-
Chemical communications (Cambridge, England) [Chem Commun (Camb)] 2004 Nov 07 (21), pp. 2386-7. Date of Electronic Publication: 2004 Sep 20. - Publication Year :
- 2004
-
Abstract
- Endonuclease BamHI mutants having an azophenylalanine residue in the dimer interface (azoAla-BamHI) were synthesized; while the activity was almost suppressed using trans-azoAla-BamHI, the cis-isomer generated with photoirradiation recovered its intrinsic activity.
- Subjects :
- Deoxyribonuclease BamHI metabolism
Dimerization
Molecular Structure
Phenylalanine chemistry
Photochemistry
Protein Conformation
Protein Structure, Tertiary
Stereoisomerism
Substrate Specificity
Ultraviolet Rays
Deoxyribonuclease BamHI chemistry
Deoxyribonuclease BamHI radiation effects
Mutagenesis, Site-Directed
Phenylalanine analogs & derivatives
Subjects
Details
- Language :
- English
- ISSN :
- 1359-7345
- Issue :
- 21
- Database :
- MEDLINE
- Journal :
- Chemical communications (Cambridge, England)
- Publication Type :
- Academic Journal
- Accession number :
- 15514778
- Full Text :
- https://doi.org/10.1039/b409844g