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In silico and empirical approaches toward understanding the structural adaptation of the alkaline-stable lipase KV1 from Acinetobacter haemolyticus

Interests in Acinetobacter haemolyticus lipases are showing an increasing trend concomitant with growth of the enzyme industry and the widening search for novel enzymes and applications. Here, we present a structural model that reveals the key catalytic residues of lipase KV1 from A. haemolyticus. H...

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Main Authors: Batumalaie, K., Edbeib, M. F., Mahat, N. A., Huyop, F., Wahab, R. A.
Format: Article
Published: Taylor and Francis Ltd. 2018
Subjects:
QD Chemistry
Online Access:http://eprints.utm.my/id/eprint/77185/
http://dx.doi.org/10.1080/07391102.2017.1377635
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spelling my.utm.771852020-06-02T05:30:19Z http://eprints.utm.my/id/eprint/77185/ In silico and empirical approaches toward understanding the structural adaptation of the alkaline-stable lipase KV1 from Acinetobacter haemolyticus Batumalaie, K. Edbeib, M. F. Mahat, N. A. Huyop, F. Wahab, R. A. QD Chemistry Interests in Acinetobacter haemolyticus lipases are showing an increasing trend concomitant with growth of the enzyme industry and the widening search for novel enzymes and applications. Here, we present a structural model that reveals the key catalytic residues of lipase KV1 from A. haemolyticus. Homology modeling of the lipase structure was based on the structure of a carboxylesterase from the archaeon Archaeoglobus fulgidus as the template, which has a sequence that is 58% identical to that of lipase KV1. The lipase KV1 model is comprised of a single compact domain consisting of seven parallel and one anti-parallel β-strand surrounded by nine α-helices. Three structurally conserved active-site residues, Ser165, Asp259, and His289, and a tunnel through which substrates access the binding site were identified. Docking of the substrates tributyrin and palmitic acid into the pH 8 modeled lipase KV1 active sites revealed an aromatic platform responsible for the substrate recognition and preference toward tributyrin. The resulting binding modes from the docking simulation correlated well with the experimentally determined hydrolysis pattern, for which pH 8 and tributyrin being the optimum pH and preferred substrate. The results reported herein provide useful insights into future structure-based tailoring of lipase KV1 to modulate its catalytic activity. Taylor and Francis Ltd. 2018-09-28 Article PeerReviewed Batumalaie, K. and Edbeib, M. F. and Mahat, N. A. and Huyop, F. and Wahab, R. A. (2018) In silico and empirical approaches toward understanding the structural adaptation of the alkaline-stable lipase KV1 from Acinetobacter haemolyticus. Journal of Biomolecular Structure and Dynamics, 36 (12). pp. 3077-3093. ISSN 0739-1102 http://dx.doi.org/10.1080/07391102.2017.1377635 DOI:10.1080/07391102.2017.1377635
institution Universiti Teknologi Malaysia
building UTM Library
collection Institutional Repository
continent Asia
country Malaysia
content_provider Universiti Teknologi Malaysia
content_source UTM Institutional Repository
url_provider http://eprints.utm.my/
topic QD Chemistry
spellingShingle QD Chemistry
Batumalaie, K.
Edbeib, M. F.
Mahat, N. A.
Huyop, F.
Wahab, R. A.
In silico and empirical approaches toward understanding the structural adaptation of the alkaline-stable lipase KV1 from Acinetobacter haemolyticus
description Interests in Acinetobacter haemolyticus lipases are showing an increasing trend concomitant with growth of the enzyme industry and the widening search for novel enzymes and applications. Here, we present a structural model that reveals the key catalytic residues of lipase KV1 from A. haemolyticus. Homology modeling of the lipase structure was based on the structure of a carboxylesterase from the archaeon Archaeoglobus fulgidus as the template, which has a sequence that is 58% identical to that of lipase KV1. The lipase KV1 model is comprised of a single compact domain consisting of seven parallel and one anti-parallel β-strand surrounded by nine α-helices. Three structurally conserved active-site residues, Ser165, Asp259, and His289, and a tunnel through which substrates access the binding site were identified. Docking of the substrates tributyrin and palmitic acid into the pH 8 modeled lipase KV1 active sites revealed an aromatic platform responsible for the substrate recognition and preference toward tributyrin. The resulting binding modes from the docking simulation correlated well with the experimentally determined hydrolysis pattern, for which pH 8 and tributyrin being the optimum pH and preferred substrate. The results reported herein provide useful insights into future structure-based tailoring of lipase KV1 to modulate its catalytic activity.
format Article
author Batumalaie, K.
Edbeib, M. F.
Mahat, N. A.
Huyop, F.
Wahab, R. A.
author_facet Batumalaie, K.
Edbeib, M. F.
Mahat, N. A.
Huyop, F.
Wahab, R. A.
author_sort Batumalaie, K.
title In silico and empirical approaches toward understanding the structural adaptation of the alkaline-stable lipase KV1 from Acinetobacter haemolyticus
title_short In silico and empirical approaches toward understanding the structural adaptation of the alkaline-stable lipase KV1 from Acinetobacter haemolyticus
title_full In silico and empirical approaches toward understanding the structural adaptation of the alkaline-stable lipase KV1 from Acinetobacter haemolyticus
title_fullStr In silico and empirical approaches toward understanding the structural adaptation of the alkaline-stable lipase KV1 from Acinetobacter haemolyticus
title_full_unstemmed In silico and empirical approaches toward understanding the structural adaptation of the alkaline-stable lipase KV1 from Acinetobacter haemolyticus
title_sort in silico and empirical approaches toward understanding the structural adaptation of the alkaline-stable lipase kv1 from acinetobacter haemolyticus
publisher Taylor and Francis Ltd.
publishDate 2018
url http://eprints.utm.my/id/eprint/77185/
http://dx.doi.org/10.1080/07391102.2017.1377635
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score 13.211869

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