title: Photochemical regulation of the activity of an endonuclease BamHI using an azobenzene moiety incorporated site-selectively into the dimer interface.
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.
authors.affiliation: Institute of Scientific and Industrial Research, Osaka University, 8-1 Mihogaoka, Ibaraki, Osaka 567-0074, Japan.
authors.forename: Koji
authors.initials: K
authors.lastname: Nakayama
authors.forename: Masayuki
authors.initials: M
authors.lastname: Endo
authors.forename: Tetsuro
authors.initials: T
authors.lastname: Majima
mesh_terms: 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
chemical_list: C506099:azophenylalanine; D010649:Phenylalanine; D015245:Deoxyribonuclease BamHI