Molecular phylogeny, 3D-structural insights, docking and mechanisms of action of plant beta-galactosidases
Beta-galactosidase (BGAL) is an exoglycosidase that catalyses the hydrolysis of terminal β-linked galactose residues. To better understand the molecular characteristics and structural insights of mango BGAL (MiBGAL), we performed the sequence analyses, reconstruction of the evolutionary tree, homolo...
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| Format: | Article |
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Inderscience Enterprises Ltd.
2016
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| Online Access: | http://ir.unimas.my/id/eprint/12659/ |
| _version_ | 1848837245542334464 |
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| author | Md. Anowar, Hossain Hairul Azman, Roslan Md. Rezaul, Karim Yoshinobu, Kimura |
| author_facet | Md. Anowar, Hossain Hairul Azman, Roslan Md. Rezaul, Karim Yoshinobu, Kimura |
| author_sort | Md. Anowar, Hossain |
| building | UNIMAS Institutional Repository |
| collection | Online Access |
| description | Beta-galactosidase (BGAL) is an exoglycosidase that catalyses the hydrolysis of terminal β-linked galactose residues. To better understand the molecular characteristics and structural insights of mango BGAL (MiBGAL), we performed the sequence analyses, reconstruction of the evolutionary tree, homology modelling and molecular docking. BGALs are widely distributed enzymes that evolved from a common bacterial ancestor. Plant BGALs (pBGALs) belong to glycosyl hydrolase-35(GH35) family and had close similarities with fungi BGALs. Three conserved motifs and GH35 putative active site with a consensus sequence G-G-P-[LIVM](2)-x(2)-Q-x-E-N-E-[FY] were identified in 67 BGAL sequences. Modelled 3D structure of MiBGAL is composed of a catalytic TIM barrel domain (domain-I) and three other β-domains, II, III & IV. Structural studies identified the residues Glu182 and Glu251 as the proton donor and nucleophile, respectively in pBGALs that could function through retaining mechanism. p-nitrophenyl-β-D-galactopyranoside and 2-[4-(2-hydroxyethyl)piperazin-1-yl]ethanesulfonic acid could be potential substrate and inhibitor, respectively among the docked-ligands for both tomato BGAL4 and MiBGAL. |
| first_indexed | 2025-11-15T06:36:36Z |
| format | Article |
| id | unimas-12659 |
| institution | Universiti Malaysia Sarawak |
| institution_category | Local University |
| last_indexed | 2025-11-15T06:36:36Z |
| publishDate | 2016 |
| publisher | Inderscience Enterprises Ltd. |
| recordtype | eprints |
| repository_type | Digital Repository |
| spelling | unimas-126592016-08-07T19:23:49Z http://ir.unimas.my/id/eprint/12659/ Molecular phylogeny, 3D-structural insights, docking and mechanisms of action of plant beta-galactosidases Md. Anowar, Hossain Hairul Azman, Roslan Md. Rezaul, Karim Yoshinobu, Kimura GE Environmental Sciences SB Plant culture Beta-galactosidase (BGAL) is an exoglycosidase that catalyses the hydrolysis of terminal β-linked galactose residues. To better understand the molecular characteristics and structural insights of mango BGAL (MiBGAL), we performed the sequence analyses, reconstruction of the evolutionary tree, homology modelling and molecular docking. BGALs are widely distributed enzymes that evolved from a common bacterial ancestor. Plant BGALs (pBGALs) belong to glycosyl hydrolase-35(GH35) family and had close similarities with fungi BGALs. Three conserved motifs and GH35 putative active site with a consensus sequence G-G-P-[LIVM](2)-x(2)-Q-x-E-N-E-[FY] were identified in 67 BGAL sequences. Modelled 3D structure of MiBGAL is composed of a catalytic TIM barrel domain (domain-I) and three other β-domains, II, III & IV. Structural studies identified the residues Glu182 and Glu251 as the proton donor and nucleophile, respectively in pBGALs that could function through retaining mechanism. p-nitrophenyl-β-D-galactopyranoside and 2-[4-(2-hydroxyethyl)piperazin-1-yl]ethanesulfonic acid could be potential substrate and inhibitor, respectively among the docked-ligands for both tomato BGAL4 and MiBGAL. Inderscience Enterprises Ltd. 2016 Article PeerReviewed Md. Anowar, Hossain and Hairul Azman, Roslan and Md. Rezaul, Karim and Yoshinobu, Kimura (2016) Molecular phylogeny, 3D-structural insights, docking and mechanisms of action of plant beta-galactosidases. International Journal of Bioinformatics Research and Applications, 12 (2). pp. 149-179. ISSN 1744-5493 http://www.inderscienceonline.com/doi/pdf/10.1504/IJBRA.2016.077125 DOI: 10.1504/IJBRA.2016.077125 |
| spellingShingle | GE Environmental Sciences SB Plant culture Md. Anowar, Hossain Hairul Azman, Roslan Md. Rezaul, Karim Yoshinobu, Kimura Molecular phylogeny, 3D-structural insights, docking and mechanisms of action of plant beta-galactosidases |
| title | Molecular phylogeny, 3D-structural insights, docking and mechanisms of action of plant beta-galactosidases |
| title_full | Molecular phylogeny, 3D-structural insights, docking and mechanisms of action of plant beta-galactosidases |
| title_fullStr | Molecular phylogeny, 3D-structural insights, docking and mechanisms of action of plant beta-galactosidases |
| title_full_unstemmed | Molecular phylogeny, 3D-structural insights, docking and mechanisms of action of plant beta-galactosidases |
| title_short | Molecular phylogeny, 3D-structural insights, docking and mechanisms of action of plant beta-galactosidases |
| title_sort | molecular phylogeny, 3d-structural insights, docking and mechanisms of action of plant beta-galactosidases |
| topic | GE Environmental Sciences SB Plant culture |
| url | http://ir.unimas.my/id/eprint/12659/ http://ir.unimas.my/id/eprint/12659/ http://ir.unimas.my/id/eprint/12659/ |