A review on non-stereospecific haloalkanoic acid dehalogenases

Haloalkanoic acid dehalogenases remove halides from organic haloacids and have potential as bioremediation agents. DehE from Rhizobium sp. RC1, DehI from Pseudomonas putida PP3 and D,LDEX 113 from Pseudomonas sp. 113 are non-stereospecific dehalogenases that invert the configurations of D- and L- c...

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Main Authors:	Tengku Abdul Hamid, Tengku Haziyamin, Abdul Hamid, Azzmer Azzar, Huyop, Huyop
Format:	Article
Language:	English
Published:	Academic Journals 2011
Subjects:	Q Science (General)
Online Access:	http://irep.iium.edu.my/4938/ http://irep.iium.edu.my/4938/ http://irep.iium.edu.my/4938/1/Review_Tg-Frul.pdf

id	iium-4938
recordtype	eprints
spelling	iium-49382012-02-28T05:40:31Z http://irep.iium.edu.my/4938/ A review on non-stereospecific haloalkanoic acid dehalogenases Tengku Abdul Hamid, Tengku Haziyamin Abdul Hamid, Azzmer Azzar Huyop, Huyop Q Science (General) Haloalkanoic acid dehalogenases remove halides from organic haloacids and have potential as bioremediation agents. DehE from Rhizobium sp. RC1, DehI from Pseudomonas putida PP3 and D,LDEX 113 from Pseudomonas sp. 113 are non-stereospecific dehalogenases that invert the configurations of D- and L- carbons bound to a halogen. The kinetics of DehE has been partially characterized and brominated compounds have greater specificity constant values than do the corresponding chlorinated compounds. The sequence of DehE is similar to that of DehI; therefore, the two enzymes may have similar structures and functions. The three-dimensional structure of DehI is known and its reaction mechanism was inferred from its structure and a mutagenesis study of D,L-DEX 113. Aspartate residues at positions 189 and 194 in DehI and D,L-DEX 113 were predicted to be involved in catalysis. These residues activate a water molecule that directly attacks the chiral carbon. Because DehE and DehI are sequentially related, delineating the structure of DehE is important to ascertain if the catalytic residues and reaction mechanism are the same for both enzymes. A structural prediction, sequence-homology modeling and a site-directed mutagenesis study of DehE might help achieve this goal. Academic Journals 2011-08-29 Article PeerReviewed application/pdf en http://irep.iium.edu.my/4938/1/Review_Tg-Frul.pdf Tengku Abdul Hamid, Tengku Haziyamin and Abdul Hamid, Azzmer Azzar and Huyop, Huyop (2011) A review on non-stereospecific haloalkanoic acid dehalogenases. African Journal of Biotechnology, 10 (48). pp. 9725-9736. ISSN ISSN 1684–5315 http://www.academicjournals.org/AJB/
repository_type	Digital Repository
institution_category	Local University
institution	International Islamic University Malaysia
building	IIUM Repository
collection	Online Access
language	English
topic	Q Science (General)
spellingShingle	Q Science (General) Tengku Abdul Hamid, Tengku Haziyamin Abdul Hamid, Azzmer Azzar Huyop, Huyop A review on non-stereospecific haloalkanoic acid dehalogenases
description	Haloalkanoic acid dehalogenases remove halides from organic haloacids and have potential as bioremediation agents. DehE from Rhizobium sp. RC1, DehI from Pseudomonas putida PP3 and D,LDEX 113 from Pseudomonas sp. 113 are non-stereospecific dehalogenases that invert the configurations of D- and L- carbons bound to a halogen. The kinetics of DehE has been partially characterized and brominated compounds have greater specificity constant values than do the corresponding chlorinated compounds. The sequence of DehE is similar to that of DehI; therefore, the two enzymes may have similar structures and functions. The three-dimensional structure of DehI is known and its reaction mechanism was inferred from its structure and a mutagenesis study of D,L-DEX 113. Aspartate residues at positions 189 and 194 in DehI and D,L-DEX 113 were predicted to be involved in catalysis. These residues activate a water molecule that directly attacks the chiral carbon. Because DehE and DehI are sequentially related, delineating the structure of DehE is important to ascertain if the catalytic residues and reaction mechanism are the same for both enzymes. A structural prediction, sequence-homology modeling and a site-directed mutagenesis study of DehE might help achieve this goal.
format	Article
author	Tengku Abdul Hamid, Tengku Haziyamin Abdul Hamid, Azzmer Azzar Huyop, Huyop
author_facet	Tengku Abdul Hamid, Tengku Haziyamin Abdul Hamid, Azzmer Azzar Huyop, Huyop
author_sort	Tengku Abdul Hamid, Tengku Haziyamin
title	A review on non-stereospecific haloalkanoic acid dehalogenases
title_short	A review on non-stereospecific haloalkanoic acid dehalogenases
title_full	A review on non-stereospecific haloalkanoic acid dehalogenases
title_fullStr	A review on non-stereospecific haloalkanoic acid dehalogenases
title_full_unstemmed	A review on non-stereospecific haloalkanoic acid dehalogenases
title_sort	review on non-stereospecific haloalkanoic acid dehalogenases
publisher	Academic Journals
publishDate	2011
url	http://irep.iium.edu.my/4938/ http://irep.iium.edu.my/4938/ http://irep.iium.edu.my/4938/1/Review_Tg-Frul.pdf
first_indexed	2023-09-18T20:13:22Z
last_indexed	2023-09-18T20:13:22Z
_version_	1777407625503178752

A review on non-stereospecific haloalkanoic acid dehalogenases

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