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- Isupov, Michail N., et al. Show all 6 Authors
- FEBS letters 2014 v.588 pp. 1616-1622
- Escherichia coli; Rhodobacteraceae; active sites; carbon; crystal structure; hydrophobicity
- ... A putative haloalkane dehalogenase has been identified in a marine Rhodobacteraceae and subsequently cloned and over-expressed in Escherichia coli. The enzyme has highest activity towards the substrates 1,6-dichlorohexane, 1-bromooctane, 1,3-dibromopropane and 1-bromohexane. The crystal structures of the enzyme in the native and product bound forms reveal a large hydrophobic active site cavity. A ...