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EC Number
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
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
structure-function relationship, roles of Cys106, Ala75, Ala74, and the isoalloxazine ring of FMN
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