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Halina R. Novak, Christopher Sayer, Michail N. Isupov, Konrad Paszkiewicz, Dorothee Gotz, Andrew Mearns Spragg and Jennifer A. Littlechild Marine Rhodobacteraceae l-haloacid dehalogenase contains a novel His/Glu dyad that could activate the catalytic water FEBS Journal 280

Article first published online: 8 MAR 2013 | DOI: 10.1111/febs.12177

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The structures of the native, reaction intermediate and substrate-bound forms of a marine Rhodobacteraceae L-haloacid dehalogenase have been determined. The enzyme active site has significant differences from previously studied L-haloacid dehalogenases. It has a His/Glu dyad positioned for deprotonation of the catalytic water similar to that found in the haloalkane dehalogenases thereby representing a new type of L-haloacid dehalogenase

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