1.14.14.3	additional information	analysis of subunit interface structure and role in the conformational stability of the heterodimeric enzyme, the beta-sunbunit can self-associate to form a stable but inactive homodimer, unfolding in a four-state mechanism	657927	
1.14.14.3	additional information	functional roles of conserved residues in the protease-labile, unstructured loop of the alpha-subunit, formed by residues 257-291, the loop undergoed conformational changes during catalysis, overview	657923	
1.14.14.3	additional information	luciferase is composed of two homologous subunits designated alpha and beta, both of which assume the TIM barrel fold. Although the beta-subunit is required for activity, the catalytic site resides exclusively on the alpha-subunit. The most substantial compositional difference between subunits corresponds to a highly conserved stretch of residues between positions 260 and 290 unique to the alpha chains of luminous bacteria. In the luciferase/FMN complex, the asymmetric unit contains two beta/alpha-heterodimers	711486	
1.14.14.3	additional information	structure-function relationship, roles of Cys106, Ala75, Ala74, and the isoalloxazine ring of FMN	657939