Novak_2014_FEBS.Lett_588_1616

Reference

Title : Biochemical and structural characterisation of a haloalkane dehalogenase from a marine Rhodobacteraceae - Novak_2014_FEBS.Lett_588_1616
Author(s) : Novak HR , Sayer C , Isupov MN , Gotz D , Spragg AM , Littlechild JA
Ref : FEBS Letters , 588 :1616 , 2014
Abstract :

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.

PubMedSearch : Novak_2014_FEBS.Lett_588_1616
PubMedID: 24613925
Gene_locus related to this paper: 9rhob-KF032932

Citations formats

Novak HR, Sayer C, Isupov MN, Gotz D, Spragg AM, Littlechild JA (2014)
Biochemical and structural characterisation of a haloalkane dehalogenase from a marine Rhodobacteraceae
FEBS Letters 588 :1616

Novak HR, Sayer C, Isupov MN, Gotz D, Spragg AM, Littlechild JA (2014)
FEBS Letters 588 :1616