scholarly journals Structural Insight Into Chitin Degradation and Thermostability of a Novel Endochitinase From the Glycoside Hydrolase Family 18

2019 ◽  
Vol 10 ◽  
Author(s):  
Yan-Jun Wang ◽  
Wen-Xin Jiang ◽  
Yi-Shuo Zhang ◽  
Hai-Yan Cao ◽  
Yi Zhang ◽  
...  
Keyword(s):  
Glycoside Hydrolase ◽  
Glycoside Hydrolase Family ◽  
Chitin Degradation ◽  
Structural Insight ◽  
Hydrolase Family ◽  
Insight Into

scholarly journals Systems analysis of the glycoside hydrolase family 18 enzymes fromCellvibrio japonicuscharacterizes essential chitin degradation functions

2018 ◽  
Vol 293 (10) ◽  
pp. 3849-3859 ◽  
Author(s):  
Estela C. Monge ◽  
Tina R. Tuveng ◽  
Gustav Vaaje-Kolstad ◽  
Vincent G. H. Eijsink ◽  
Jeffrey G. Gardner
Keyword(s):  
Systems Analysis ◽  
Glycoside Hydrolase ◽  
Glycoside Hydrolase Family ◽  
Chitin Degradation ◽  
Hydrolase Family

Insight into the Thermophilic Mechanism of a Glycoside Hydrolase Family 5 β-Mannanase

2018 ◽  
Vol 67 (1) ◽  
pp. 473-483 ◽  
Author(s):  
Weina Liu ◽  
Tao Tu ◽  
Yuan Gu ◽  
Yuan Wang ◽  
Fei Zheng ◽  
...  
Keyword(s):  
Glycoside Hydrolase ◽  
Glycoside Hydrolase Family ◽  
Hydrolase Family ◽  
Insight Into

scholarly journals The structure of a family GH25 lysozyme fromAspergillus fumigatus

2010 ◽  
Vol 66 (9) ◽  
pp. 973-977 ◽  
Author(s):  
Justyna E. Korczynska ◽  
Steffen Danielsen ◽  
Ulrika Schagerlöf ◽  
Johan P. Turkenburg ◽  
Gideon J. Davies ◽  
...  
Keyword(s):  
Active Site ◽  
Glycoside Hydrolase ◽  
Catalytic Mechanism ◽  
Medical Application ◽  
Glycoside Hydrolase Family ◽  
X Ray ◽  
Fungal Structure ◽  
The Family ◽  
Hydrolase Family ◽  
Insight Into

Lysins are important biomolecules which cleave the bacterial cell-wall polymer peptidoglycan. They are finding increasing commercial and medical application. In order to gain an insight into the mechanism by which these enzymes operate, the X-ray structure of a CAZy family GH25 `lysozyme' fromAspergillus fumigatuswas determined. This is the first fungal structure from the family and reveals a modified α/β-barrel-like fold in which an eight-stranded β-barrel is flanked by three α-helices. The active site lies toward the bottom of a negatively charged pocket and its layout has much in common with other solved members of the GH25 and related GH families. A conserved active-site DXE motif may be implicated in catalysis, lending further weight to the argument that this glycoside hydrolase family operatesviaa `substrate-assisted' catalytic mechanism.

scholarly journals The deduced role of a chitinase containing two nonsynergistic catalytic domains

2018 ◽  
Vol 74 (1) ◽  
pp. 30-40 ◽  
Author(s):  
Tian Liu ◽  
Weixing Zhu ◽  
Jing Wang ◽  
Yong Zhou ◽  
Yanwei Duan ◽  
...  
Keyword(s):  
Glycoside Hydrolase ◽  
Gene Expression Pattern ◽  
Physiological Data ◽  
Glycoside Hydrolase Family ◽  
Chitin Synthesis ◽  
Group Iii ◽  
Chitin Degradation ◽  
Catalytic Domains ◽  
Hydrolase Family

The glycoside hydrolase family 18 chitinases degrade or alter chitin. Multiple catalytic domains in a glycoside hydrolase family 18 chitinase function synergistically during chitin degradation. Here, an insect group III chitinase from the agricultural pestOstrinia furnacalis(OfChtIII) is revealed to be an arthropod-conserved chitinase that contains two nonsynergistic GH18 domains according to its catalytic properties. Both GH18 domains are active towards single-chained chitin substrates, but are inactive towards insoluble chitin substrates. The crystal structures of each unbound GH18 domain, as well as of GH18 domains complexed with hexa-N-acetyl-chitohexaose or penta-N-acetyl-chitopentaose, suggest that the two GH18 domains possess endo-specific activities. Physiological data indicated that the developmental stage-dependent gene-expression pattern ofOfChtIII was the same as that of the chitin synthaseOfChsA but significantly different from that of the chitinaseOfChtI, which is indispensable for cuticular chitin degradation. Additionally, immunological staining indicated thatOfChtIII was co-localized withOfChsA. Thus,OfChtIII is most likely to be involved in the chitin-synthesis pathway.

Xylanases of glycoside hydrolase family 30 – An overview

2021 ◽  
Vol 47 ◽  
pp. 107704
Author(s):  
Vladimír Puchart ◽  
Katarína Šuchová ◽  
Peter Biely
Keyword(s):  
Glycoside Hydrolase ◽  
Glycoside Hydrolase Family ◽  
Hydrolase Family ◽  
Glycoside Hydrolase Family 30

scholarly journals Modeled 3D-Structures of Proteobacterial Transglycosylases from Glycoside Hydrolase Family 17 Give Insight in Ligand Interactions Explaining Differences in Transglycosylation Products

2021 ◽  
Vol 11 (9) ◽  
pp. 4048
Author(s):  
Javier A. Linares-Pastén ◽  
Lilja Björk Jonsdottir ◽  
Gudmundur O. Hreggvidsson ◽  
Olafur H. Fridjonsson ◽  
Hildegard Watzlawick ◽  
...  
Keyword(s):  
Glycoside Hydrolase ◽  
Ligand Docking ◽  
Glycoside Hydrolase Family ◽  
Ligand Interactions ◽  
Tim Barrel ◽  
Branching Point ◽  
The Difference ◽  
Dynamics Simulations ◽  
And Function ◽  
Hydrolase Family

The structures of glycoside hydrolase family 17 (GH17) catalytic modules from modular proteins in the ndvB loci in Pseudomonas aeruginosa (Glt1), P. putida (Glt3) and Bradyrhizobium diazoefficiens (previously B. japonicum) (Glt20) were modeled to shed light on reported differences between these homologous transglycosylases concerning substrate size, preferred cleavage site (from reducing end (Glt20: DP2 product) or non-reducing end (Glt1, Glt3: DP4 products)), branching (Glt20) and linkage formed (1,3-linkage in Glt1, Glt3 and 1,6-linkage in Glt20). Hybrid models were built and stability of the resulting TIM-barrel structures was supported by molecular dynamics simulations. Catalytic amino acids were identified by superimposition of GH17 structures, and function was verified by mutagenesis using Glt20 as template (i.e., E120 and E209). Ligand docking revealed six putative subsites (−4, −3, −2, −1, +1 and +2), and the conserved interacting residues suggest substrate binding in the same orientation in all three transglycosylases, despite release of the donor oligosaccharide product from either the reducing (Glt20) or non-reducing end (Glt1, Gl3). Subsites +1 and +2 are most conserved and the difference in release is likely due to changes in loop structures, leading to loss of hydrogen bonds in Glt20. Substrate docking in Glt20 indicate that presence of covalently bound donor in glycone subsites −4 to −1 creates space to accommodate acceptor oligosaccharide in alternative subsites in the catalytic cleft, promoting a branching point and formation of a 1,6-linkage. The minimum donor size of DP5, can be explained assuming preferred binding of DP4 substrates in subsite −4 to −1, preventing catalysis.

scholarly journals Understanding the Polymerization Mechanism of Glycoside-Hydrolase Family 70 Glucansucrases

2006 ◽  
Vol 281 (42) ◽  
pp. 31254-31267
Author(s):  
Claire Moulis ◽  
Gilles Joucla ◽  
David Harrison ◽  
Emeline Fabre ◽  
Gabrielle Potocki-Veronese ◽  
...  
Keyword(s):  
Glycoside Hydrolase ◽  
Glycoside Hydrolase Family ◽  
Polymerization Mechanism ◽  
Hydrolase Family
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