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Biochemical and structural characterisation of a haloalkane dehalogenase from a marine Rhodobacteraceae
Author(s) -
Novak Halina R.,
Sayer Christopher,
Isupov Michail N.,
Gotz Dorothee,
Spragg Andrew Mearns,
Littlechild Jennifer A.
Publication year - 2014
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2014.02.056
Subject(s) - dehalogenase , enzyme , active site , chemistry , stereochemistry , substrate (aquarium) , biochemistry , binding site , biology , ecology
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 deeper substrate binding pocket defines the enzyme preference towards substrates with longer carbon chains. Arg136 at the bottom of the substrate pocket is positioned to bind the distal halogen group of extended di‐halogenated substrates.