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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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(a,b) comparison of tertiary structures of GH46 chitosanases from Bacillus circulans MH-K1 (CHIS_BACCI) and Microbacterium sp. OU01 (E1AXU1_9PSED). Structure drawings were derived from PDB files 1QGI and 4OLT; (c,d) major lobe loop length polymorphism shown on chitosanases from Cluster A (SACTE_5457 from Streptomyces sp. SirexAA-E) and B (KSE_40930_csn3 from Kitasatospora setae). Drawings derived from PDB file 4ILY and a homology-based model build on 3D-JIGSAW server [48]; (e,f) minor lobe loop length polymorphism shown on chitosanases from Bacillus circulans MH-K1 (CHIS_BACCI) and Streptomyces sp. N174 (CsnN174). Drawings derived from PDB files 1QGI and 1CHK. The longer loop in CHIS-BACCI allows for the accommodation of an N-acetyl group of the chitosan substrate at +1 subsite of chitosanase [41]. α-Helices are paint in violet, β-sheets in yellow and loops in green.
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marinedrugs-13-06566-f003: (a,b) comparison of tertiary structures of GH46 chitosanases from Bacillus circulans MH-K1 (CHIS_BACCI) and Microbacterium sp. OU01 (E1AXU1_9PSED). Structure drawings were derived from PDB files 1QGI and 4OLT; (c,d) major lobe loop length polymorphism shown on chitosanases from Cluster A (SACTE_5457 from Streptomyces sp. SirexAA-E) and B (KSE_40930_csn3 from Kitasatospora setae). Drawings derived from PDB file 4ILY and a homology-based model build on 3D-JIGSAW server [48]; (e,f) minor lobe loop length polymorphism shown on chitosanases from Bacillus circulans MH-K1 (CHIS_BACCI) and Streptomyces sp. N174 (CsnN174). Drawings derived from PDB files 1QGI and 1CHK. The longer loop in CHIS-BACCI allows for the accommodation of an N-acetyl group of the chitosan substrate at +1 subsite of chitosanase [41]. α-Helices are paint in violet, β-sheets in yellow and loops in green.

Mentions: The tertiary structure of GH46 chitosanases is similar to those of lysozymes (GH22, GH23, GH24) and non-processive chitinases (GH19) [47]. The CAZy database groups into “clans” the families of proteins “sharing a fold and catalytic machinery”. Accordingly, GH46 proteins belong to clan GH-I together with families GH24 and GH80 [24,25]. They are mostly α-helical proteins, composed of two lobes, a major lobe and a minor lobe, separated by a substrate-binding cleft (Figure 3). Residues that function could be inferred from crystallography or site-directed mutagenesis are listed in Table 1. Secondary structures derived from crystallography are also shown in the sequence alignment in Figure S2.


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

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

(a,b) comparison of tertiary structures of GH46 chitosanases from Bacillus circulans MH-K1 (CHIS_BACCI) and Microbacterium sp. OU01 (E1AXU1_9PSED). Structure drawings were derived from PDB files 1QGI and 4OLT; (c,d) major lobe loop length polymorphism shown on chitosanases from Cluster A (SACTE_5457 from Streptomyces sp. SirexAA-E) and B (KSE_40930_csn3 from Kitasatospora setae). Drawings derived from PDB file 4ILY and a homology-based model build on 3D-JIGSAW server [48]; (e,f) minor lobe loop length polymorphism shown on chitosanases from Bacillus circulans MH-K1 (CHIS_BACCI) and Streptomyces sp. N174 (CsnN174). Drawings derived from PDB files 1QGI and 1CHK. The longer loop in CHIS-BACCI allows for the accommodation of an N-acetyl group of the chitosan substrate at +1 subsite of chitosanase [41]. α-Helices are paint in violet, β-sheets in yellow and loops in green.
© Copyright Policy
Related In: Results  -  Collection

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

marinedrugs-13-06566-f003: (a,b) comparison of tertiary structures of GH46 chitosanases from Bacillus circulans MH-K1 (CHIS_BACCI) and Microbacterium sp. OU01 (E1AXU1_9PSED). Structure drawings were derived from PDB files 1QGI and 4OLT; (c,d) major lobe loop length polymorphism shown on chitosanases from Cluster A (SACTE_5457 from Streptomyces sp. SirexAA-E) and B (KSE_40930_csn3 from Kitasatospora setae). Drawings derived from PDB file 4ILY and a homology-based model build on 3D-JIGSAW server [48]; (e,f) minor lobe loop length polymorphism shown on chitosanases from Bacillus circulans MH-K1 (CHIS_BACCI) and Streptomyces sp. N174 (CsnN174). Drawings derived from PDB files 1QGI and 1CHK. The longer loop in CHIS-BACCI allows for the accommodation of an N-acetyl group of the chitosan substrate at +1 subsite of chitosanase [41]. α-Helices are paint in violet, β-sheets in yellow and loops in green.
Mentions: The tertiary structure of GH46 chitosanases is similar to those of lysozymes (GH22, GH23, GH24) and non-processive chitinases (GH19) [47]. The CAZy database groups into “clans” the families of proteins “sharing a fold and catalytic machinery”. Accordingly, GH46 proteins belong to clan GH-I together with families GH24 and GH80 [24,25]. They are mostly α-helical proteins, composed of two lobes, a major lobe and a minor lobe, separated by a substrate-binding cleft (Figure 3). Residues that function could be inferred from crystallography or site-directed mutagenesis are listed in Table 1. Secondary structures derived from crystallography are also shown in the sequence alignment in Figure S2.

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
Related in: MedlinePlus