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Protein engineering and molecular modelling of firefly luciferase SE Prebble2; Rachel L Price*1; B Lingard1; PJ White1; LC Tisi3 (1) Detection, DERA Porton Down, Salisbury, Wiltshire, SP4 0JQ, UK; (2) School of Biosciences, University of Kent at Canterbury, Canterbury, Kent, CT2 7NJ, UK; (3) Institute of Biotechnology, Tennis Court Road, Cambridge, CB2 1QT, UK      *(rlprice@dera.gov.uk) Firefly luciferase has great potential as a bioluminescent label, exhibiting greater specificity, sensitivity and localisation compared with other labels used in immunoassays and nucleic acid detection techniques. The Km (ATP) and thermal stability of the native enzyme have been altered using protein engineering, introducing amino acid substitutions by genetic modification. Characterisation of the resultant mutant enzymes and modelling using SYBYL modelling software (Tripos Ltd.) have provided some insight into structure-function relationships. A binding cleft for coenzyme A is proposed. [Poster: price.rachel.24152]

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