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Chitosanases from Family 46 of Glycoside Hydrolases: From Proteins to Phenotypes.

Viens P, Lacombe-Harvey MÈ, Brzezinski R - Mar Drugs (2015)

Bottom Line: Chitosanases, enzymes that catalyze the endo-hydrolysis of glycolytic links in chitosan, are the subject of numerous studies as biotechnological tools to generate low molecular weight chitosan (LMWC) or chitosan oligosaccharides (CHOS) from native, high molecular weight chitosan.Glycoside hydrolases belonging to family GH46 are among the best-studied chitosanases, with four crystallography-derived structures available and more than forty enzymes studied at the biochemical level.This review is focused on the taxonomic distribution of GH46 proteins, their multi-modular character, the structure-function relationships and their biological functions in the host organisms.

View Article: PubMed Central - PubMed

Affiliation: Biologie, Faculté des Sciences, Université de Sherbrooke, 2500, boul. de l'Université, Sherbrooke, QC J1K 2R1, Canada. Pascal.Viens@USherbrooke.ca.

ABSTRACT
Chitosanases, enzymes that catalyze the endo-hydrolysis of glycolytic links in chitosan, are the subject of numerous studies as biotechnological tools to generate low molecular weight chitosan (LMWC) or chitosan oligosaccharides (CHOS) from native, high molecular weight chitosan. Glycoside hydrolases belonging to family GH46 are among the best-studied chitosanases, with four crystallography-derived structures available and more than forty enzymes studied at the biochemical level. They were also subjected to numerous site-directed mutagenesis studies, unraveling the molecular mechanisms of hydrolysis. This review is focused on the taxonomic distribution of GH46 proteins, their multi-modular character, the structure-function relationships and their biological functions in the host organisms.

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Phylogenetic tree of 58 primary sequences of GH46 proteins. The tree has been drawn with TreeDyn program version 198.3 [28] based on an alignment performed with Clustal Omega [26]. Asterisks (*) indicate the proteins with known 3D structure. Proteins for which a SEC-type signal peptide has been detected are highlighted in blue, while those with putative TAT-type signal peptides [29,30] are highlighted in red.
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marinedrugs-13-06566-f001: Phylogenetic tree of 58 primary sequences of GH46 proteins. The tree has been drawn with TreeDyn program version 198.3 [28] based on an alignment performed with Clustal Omega [26]. Asterisks (*) indicate the proteins with known 3D structure. Proteins for which a SEC-type signal peptide has been detected are highlighted in blue, while those with putative TAT-type signal peptides [29,30] are highlighted in red.

Mentions: GH46 proteins are essentially present in eubacterial organisms. To analyze the phylogenetic distribution of GH46 members, we performed an alignment of a subset of 58 primary sequences, including all the sequences of biochemically and structurally studied enzymes but excluding groups of very similar sequences from closely related microorganisms (mostly originating from whole genome sequencing projects). The full-length sequences in Fasta format are shown in Figure S1. All the sequences were first analyzed for the occurrence of a signal peptide at the N-terminus and, when present, these segments of low sequence conservation were subtracted from the set submitted to the alignment program. Sequences were aligned with Clustal Omega at default settings [26]. The resulting alignment (Figure S2) is considered as reliable, as it shows the conservation of all the residues for which importance for chitosanase function has been demonstrated by site-directed mutagenesis or crystallography. Most secondary structures revealed by crystallography are also aligned. The alignment was used to derive the phylogenetic tree (Figure 1), which corroborates a more extensive tree based on 148 sequences, published previously [27].


Chitosanases from Family 46 of Glycoside Hydrolases: From Proteins to Phenotypes.

Viens P, Lacombe-Harvey MÈ, Brzezinski R - Mar Drugs (2015)

Phylogenetic tree of 58 primary sequences of GH46 proteins. The tree has been drawn with TreeDyn program version 198.3 [28] based on an alignment performed with Clustal Omega [26]. Asterisks (*) indicate the proteins with known 3D structure. Proteins for which a SEC-type signal peptide has been detected are highlighted in blue, while those with putative TAT-type signal peptides [29,30] are highlighted in red.
© Copyright Policy
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4663542&req=5

marinedrugs-13-06566-f001: Phylogenetic tree of 58 primary sequences of GH46 proteins. The tree has been drawn with TreeDyn program version 198.3 [28] based on an alignment performed with Clustal Omega [26]. Asterisks (*) indicate the proteins with known 3D structure. Proteins for which a SEC-type signal peptide has been detected are highlighted in blue, while those with putative TAT-type signal peptides [29,30] are highlighted in red.
Mentions: GH46 proteins are essentially present in eubacterial organisms. To analyze the phylogenetic distribution of GH46 members, we performed an alignment of a subset of 58 primary sequences, including all the sequences of biochemically and structurally studied enzymes but excluding groups of very similar sequences from closely related microorganisms (mostly originating from whole genome sequencing projects). The full-length sequences in Fasta format are shown in Figure S1. All the sequences were first analyzed for the occurrence of a signal peptide at the N-terminus and, when present, these segments of low sequence conservation were subtracted from the set submitted to the alignment program. Sequences were aligned with Clustal Omega at default settings [26]. The resulting alignment (Figure S2) is considered as reliable, as it shows the conservation of all the residues for which importance for chitosanase function has been demonstrated by site-directed mutagenesis or crystallography. Most secondary structures revealed by crystallography are also aligned. The alignment was used to derive the phylogenetic tree (Figure 1), which corroborates a more extensive tree based on 148 sequences, published previously [27].

Bottom Line: Chitosanases, enzymes that catalyze the endo-hydrolysis of glycolytic links in chitosan, are the subject of numerous studies as biotechnological tools to generate low molecular weight chitosan (LMWC) or chitosan oligosaccharides (CHOS) from native, high molecular weight chitosan.Glycoside hydrolases belonging to family GH46 are among the best-studied chitosanases, with four crystallography-derived structures available and more than forty enzymes studied at the biochemical level.This review is focused on the taxonomic distribution of GH46 proteins, their multi-modular character, the structure-function relationships and their biological functions in the host organisms.

View Article: PubMed Central - PubMed

Affiliation: Biologie, Faculté des Sciences, Université de Sherbrooke, 2500, boul. de l'Université, Sherbrooke, QC J1K 2R1, Canada. Pascal.Viens@USherbrooke.ca.

ABSTRACT
Chitosanases, enzymes that catalyze the endo-hydrolysis of glycolytic links in chitosan, are the subject of numerous studies as biotechnological tools to generate low molecular weight chitosan (LMWC) or chitosan oligosaccharides (CHOS) from native, high molecular weight chitosan. Glycoside hydrolases belonging to family GH46 are among the best-studied chitosanases, with four crystallography-derived structures available and more than forty enzymes studied at the biochemical level. They were also subjected to numerous site-directed mutagenesis studies, unraveling the molecular mechanisms of hydrolysis. This review is focused on the taxonomic distribution of GH46 proteins, their multi-modular character, the structure-function relationships and their biological functions in the host organisms.

Show MeSH