Photochemical regulation of the activity of an endonuclease BamHI using an azobenzene moiety incorporated site-selectively into the dimer interface.
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.
Nakayama
Koji
K
Institute of Scientific and Industrial Research, Osaka University, 8-1 Mihogaoka, Ibaraki, Osaka 567-0074, Japan.
Endo
Masayuki
M
Majima
Tetsuro
T
D015245:Deoxyribonuclease BamHI / Q000737:chemistry* / Q000378:metabolism / Q000528:radiation effects*; D019281:Dimerization; D015394:Molecular Structure; D016297:Mutagenesis, Site-Directed; D010649:Phenylalanine / Q000031:analogs & derivatives* / Q000737:chemistry; D010777:Photochemistry; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D013237:Stereoisomerism; D013379:Substrate Specificity; D014466:Ultraviolet Rays
C506099:azophenylalanine; D010649:Phenylalanine; D015245:Deoxyribonuclease BamHI