The Structural Basis of Substrate Recognition in an exo-β-d-Glucosaminidase Involved in Chitosan Hydrolysis

Bueren, A. Lammerts van; Ghinet, Mariana Gabriela; Gregg, K.; Fleury, Alain; Brzeziński, Ryszard; Boraston, A.B.

doi:10.1016/j.jmb.2008.10.031

Cited by 36 publications

(28 citation statements)

References 41 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…ThMan2A is structurally related to b-D-glucosaminidase (rmsd of 3.0 A, as computed by DALI [24] for PDB structure 2VZO [25]), b-glucuronidase (rmsd of 3.7 A for PDB structure 3HN3; not published), and b-galactosidase (rmsd of 4.3…”

Section: Structural Comparison With Gh Family 2 Membersmentioning

confidence: 99%

“…Structural comparisons of ThMan2A with other members of GH family 2 reveal interesting patterns in the macromolecular architecture of this GH family. ThMan2A is structurally related to b-D-glucosaminidase (rmsd of 3.0 A, as computed by DALI [24] for PDB structure 2VZO [25]), b-glucuronidase (rmsd of 3.7 A for PDB structure 3HN3; not published), and b-galactosidase (rmsd of 4.3…”

Section: Structural Comparison With Gh Family 2 Membersmentioning

confidence: 99%

“…A for PDB structure 1F4A [26]). Despite the low sequence identity (only 21%, covering 43% of the ThMan2A sequence), ThMan2A and Amycolatopsis orientalis D-glucosaminidase [25] (PDB ID: 2VZO) share the same domain organization, with four small domains folded as small b-sandwiches surrounding the central a/b-barrel that contains the active site. A secondary structure-based superposition reveals an rmsd of only 2.7…”

Section: Structural Comparison With Gh Family 2 Membersmentioning

confidence: 99%

See 2 more Smart Citations

Insights into the structure and function of fungal β‐mannosidases from glycoside hydrolase family 2 based on multiple crystal structures of the Trichoderma harzianum enzyme

et al. 2014

View full text Add to dashboard Cite

Hemicellulose is an important part of the plant cell wall biomass, and is relevant to cellulosic ethanol technologies. b-Mannosidases are enzymes capable of cleaving nonreducing residues of b-D-mannose from b-D-mannosides and hemicellulose mannose-containing polysaccharides, such as mannans and galactomannans. b-Mannosidases are distributed between glycoside hydrolase (GH) families 1, 2, and 5, and only a handful of the enzymes have been structurally characterized to date. The only published X-ray structure of a GH family 2 mannosidase is that of the bacterial Bacteroides thetaiotaomicron enzyme. No structures of eukaryotic mannosidases of this family are currently available. To fill this gap, we set out to solve the structure of Trichoderma harzianum GH family 2 b-mannosidase and to refine it to 1.9-A resolution. Structural comparisons of the T. harzianum GH2 b-mannosidase highlight similarities in its structural architecture with other members of GH family 2, reveal the molecular mechanism of b-mannoside binding and recognition, and shed light on its putative galactomannan-binding site. DatabaseCoordinates and observed structure factor amplitudes have been deposited with the Protein Data Bank (4CVU and 4UOJ). The T. harzianum b-mannosidase 2A nucleotide sequence has GenBank accession number BankIt1712036 GeneMark.hmm KJ624918. AbbreviationsBtMan2A, Bacteroides thetaiotaomicron glycosyl hydrolase family 2 b-mannosidase; CBM, carbohydrate-binding module; CmMan5A, Cellvibrio mixtus glycosyl hydrolase family 5 b-mannosidase; GH, glycosyl hydrolase; GM, b-galactomannan; Man 2 , mannobiose; Man 3 , mannotriose; Man 4 , mannotetraose; PDB, Protein Data Bank; ThMan2A, Trichoderma harzianum glycosyl hydrolase family 2 b-mannosidase.

show abstract

Section: Structural Comparison With Gh Family 2 Membersmentioning

confidence: 99%

Section: Structural Comparison With Gh Family 2 Membersmentioning

confidence: 99%

Section: Structural Comparison With Gh Family 2 Membersmentioning

confidence: 99%

See 1 more Smart Citation

Insights into the structure and function of fungal β‐mannosidases from glycoside hydrolase family 2 based on multiple crystal structures of the Trichoderma harzianum enzyme

et al. 2014

View full text Add to dashboard Cite

show abstract

“…Chitosanases from family GH5 and GH8 also tend to have β-1, 4-glucanase activity. In contrast, chitosanases of family GH46, GH75, and GH80 are more specific in substrate, which is limited to chitosan (Bueren et al 2009). Most bacteria can be induced by exogenous chitosan to expression chitosanase and thus play an important role in degradation of this polysaccharide.…”

Section: Introductionmentioning

confidence: 99%

Cloning and overexpression of a new chitosanase gene from Penicillium sp. D-1

et al. 2012

View full text Add to dashboard Cite

A chitosanase gene, csn, was cloned from Penicillium sp. D-1 by inverse PCR. The cDNA sequence analysis revealed that csn had no intron. The deduced CSN protein consists of 250 amino acids including a 20-amino acid signal peptide, and shared 83.6% identity with the family 75 chitosanase from Talaromyces stipitatus (B8M2R4). The mature protein was overexpressed in Escherichia coli and purified with the affinity chromatography of Ni2+-NTA. The novel recombinant chitosanase showed maximal catalytic activity at pH 4.0 and 48°C. Moreover, the activity of CSN was stable over a broad pH range of 3.0-8.0, and the enzymatic activity was significantly enhanced by Mg2+ and Mn2+. The CSN could effectively hydrolyze colloidal chitosan and chitosan, while could not hydrolyze chitin and carboxymethylcellulose (CMC). Due to the particular acidophily, CSN has the potential application in the recycling of chitosan wastes.The GenBank/EMBL/DDBJ accession numbers for the 18S rRNA gene and chitosanase gene of strain D-1 are JF950269 and JF950270, respectively.

show abstract

“…The studies were further extended to understand the catalytic mechanism, crystallization, and recombinant system for easy production. [36][37][38] Thereafter, most of the reports were from fungi such as Trichoderma reesei, 39 Aspergillus fumigatus, 40 Penicillium funiculosum, 41 and Aspergillus oryzae. 42 Ike et al 43 cloned and characterized the GlcNase-encoding gene (gls93) from T. reesei.…”

Section: Chitin and Chitosanmentioning

confidence: 99%

Chitinolytic enzymes: An appraisal as a product of commercial potential

Chavan

Deshpande

2013

Biotechnology Progress

View full text Add to dashboard Cite

Chitin, its deacetylated form, chitosan and chitinolytic enzymes viz. endo-chitinase, N-acetylglucosaminidase, chitosanase, chitin deacetylase (CDA) are gaining importance for their biotechnological applications. Presently, chitin degrading enzymes constitute high-cost low-volume products in human health care and associated research. Indeed chitinases and CDA-chitosanase complex possesss tremendous potential in agriculture to control plant pathogenic fungi and insects. The success in exploring chitinases especially for agriculture, i.e. as a high-volume low-cost product, depends on the availability of highly active preparations with a reasonable cost. Therefore, a reconsideration in terms of understanding the roles of chitinolytic enzymes in applications, e.g. host-pathogen interaction for biocontrol, different mechanisms of chitin degradation, and identification of new enzymes with varying specificities, may make them more useful in a variety of commercial processes in the near future. The possible issues and challenges encountered in the translation of proof of concept into a commercial product will be appraised in this review.

show abstract

The Structural Basis of Substrate Recognition in an exo-β-d-Glucosaminidase Involved in Chitosan Hydrolysis

Cited by 36 publications

References 41 publications

Insights into the structure and function of fungal β‐mannosidases from glycoside hydrolase family 2 based on multiple crystal structures of the Trichoderma harzianum enzyme

Insights into the structure and function of fungal β‐mannosidases from glycoside hydrolase family 2 based on multiple crystal structures of the Trichoderma harzianum enzyme

Cloning and overexpression of a new chitosanase gene from Penicillium sp. D-1

Chitinolytic enzymes: An appraisal as a product of commercial potential

Contact Info

Product

Resources

About