Universiti Teknologi Malaysia Institutional Repository

Interactions of non-natural halogenated substrates with D-specific dehalogenase (DehD) mutants using in silico studies

Sudi, Ismaila Yada and Shamsir, Mohd. Shahir and Jamaluddin, Haryati and Abdul Wahab, Roswanira and Huyop, Fahrul (2014) Interactions of non-natural halogenated substrates with D-specific dehalogenase (DehD) mutants using in silico studies. Biotechnology and Biotechnological Equipment, 28 (5). pp. 949-957. ISSN 1310-2818


Official URL: http://dx.doi.org/10.1080/13102818.2014.960663


The D-2-haloacid dehalogenase of D-specific dehalogenase (DehD) from Rhizobium sp. RC1 catalyses the hydrolytic dehalogenation of D-haloalkanoic acids, inverting the substrate-product configuration and thereby forming the corresponding L-hydroxyalkanoic acids. Our investigations were focused on DehD mutants: R134A and Y135A. We examined the possible interactions between these mutants with haloalkanoic acids and characterized the key catalytic residues in the wild-type dehalogenase, to design dehalogenase enzyme(s) with improved potential for dehalogenation of a wider range of substrates. Three natural substrates of wild-type DehD, specifically, monochloroacetate, monobromoacetate and D,L-2,3-dichloropropionate, and eight other non-natural haloalkanoic acids substrates of DehD, namely, L-2-chloropropionate; L-2-bromopropionate; 2,2-dichloropropionate; dichloroacetate; dibromoacetate; trichloroacetate; tribromoacetate; and 3-chloropropionate, were docked into the active site of the DehD mutants R134A and Y135A, which produced altered catalytic functions. The mutants interacted strongly with substrates that wild-type DehD does not interact with or degrade. The interaction was particularly enhanced with 3-chloropropionate, in addition to monobromoacetate, monochloroacetate and D,L-2,3-dichloropropionate. In summary, DehD variants R134A and Y135A demonstrated increased propensity for binding haloalkanoic acid and were non-stereospecific towards halogenated substrates. The improved characteristics in these mutants suggest that their functionality could be further exploited and harnessed in bioremediations and biotechnological applications

Item Type:Article
Uncontrolled Keywords:dehalogenases, docking, haloalkanoic acids, hydrogen-bond distance, interacting residues
Subjects:Q Science > QH Natural history
Divisions:Biosciences and Medical Engineering
ID Code:53216
Deposited By: Siti Nor Hashidah Zakaria
Deposited On:01 Feb 2016 11:53
Last Modified:19 Jul 2018 15:26

Repository Staff Only: item control page