نتایج جستجو برای: haloalkane dehalogenase

تعداد نتایج: 829  

Journal: :Plant physiology 2008
Gilda L Mena-Benitez Fernando Gandia-Herrero Stuart Graham Tony R Larson Simon J McQueen-Mason Christopher E French Elizabeth L Rylott Neil C Bruce

Plants are increasingly being employed to clean up environmental pollutants such as heavy metals; however, a major limitation of phytoremediation is the inability of plants to mineralize most organic pollutants. A key component of organic pollutants is halogenated aliphatic compounds that include 1,2-dichloroethane (1,2-DCA). Although plants lack the enzymatic activity required to metabolize th...

Journal: :Acta Crystallographica Section F Structural Biology and Crystallization Communications 2009

Journal: :Nature chemical biology 2009
Martina Pavlova Martin Klvana Zbynek Prokop Radka Chaloupkova Pavel Banas Michal Otyepka Rebecca C Wade Masataka Tsuda Yuji Nagata Jiri Damborsky

Engineering enzymes to degrade anthropogenic compounds efficiently is challenging. We obtained Rhodococcus rhodochrous haloalkane dehalogenase mutants with up to 32-fold higher activity than wild type toward the toxic, recalcitrant anthropogenic compound 1,2,3-trichloropropane (TCP) using a new strategy. We identified key residues in access tunnels connecting the buried active site with bulk so...

Journal: :European journal of biochemistry 1995
C Kennes F Pries G H Krooshof E Bokma J Kingma D B Janssen

Haloalkane dehalogenase catalyzes the hydrolytic cleavage of carbon-halogen bonds in short-chain haloalkanes. Two tryptophan residues of the enzyme (Trp125 and Trp175) form a halide-binding site in the active-site cavity, and were proposed to play a role in catalysis. The function of these residues was studied by replacing Trp125 with phenylalanine, glutamine or arginine and Trp175 by glutamine...

Journal: :ACS nano 2012
Daniel S Liu William S Phipps Ken H Loh Mark Howarth Alice Y Ting

We present a methodology for targeting quantum dots to specific proteins on living cells in two steps. In the first step, Escherichia coli lipoic acid ligase (LplA) site-specifically attaches 10-bromodecanoic acid onto a 13 amino acid recognition sequence that is genetically fused to a protein of interest. In the second step, quantum dots derivatized with HaloTag, a modified haloalkane dehaloge...

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