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J. Biol. Chem., Vol. 269, Issue 26, 17490-17494, 07, 1994
F Pries, AJ van den Wijngaard, R Bos, M Pentenga and DB Janssen
The first step in the utilization of the xenobiotic chlorinated hydrocarbon
1,2-dichloroethane by Xanthobacter autotrophicus is catalyzed by haloalkane
dehalogenase (Dh1A). The enzyme hydrolyses 1- haloalkanes to the
corresponding alcohols. This allows the organism to grow also on
short-chain (C2-C4) 1-chloro-n-alkanes. We have expressed Dh1A in a strain
of Pseudomonas that grows on long-chain alcohols and have selected 12
independent mutants that utilize 1-chlorohexane. Six different mutant
enzymes with improved Km or Vmax values with 1- chlorohexane were obtained.
The sequences of the mutated dh1A genes showed that several mutants had the
same 11-amino acid deletion, two mutants carried a different point
mutation, and three mutants had different tandem repeats. All mutations
occurred in a region encoding the N-terminal part of the cap domain of
Dh1A, and it is concluded that this part of the protein is involved in the
evolution of activity toward xenobiotic substrates.
The role of spontaneous cap domain mutations in haloalkane dehalogenase specificity and evolution
Department of Biochemistry, University of Groningen, The Netherlands.
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