scholarly journals Structure, activity, and stability of metagenome-derived glycoside hydrolase family 9 endoglucanase with an N-terminal Ig-like domain

2015 ◽  
Vol 24 (3) ◽  
pp. 408-419 ◽  
Author(s):  
Hiroyuki Okano ◽  
Eiko Kanaya ◽  
Masashi Ozaki ◽  
Clement Angkawidjaja ◽  
Shigenori Kanaya
Keyword(s):  
Glycoside Hydrolase ◽  
Glycoside Hydrolase Family ◽  
Structure Activity ◽  
Glycoside Hydrolase Family 9 ◽  
Hydrolase Family

Characterization of a Theme C Glycoside Hydrolase Family 9 Endo-Beta-Glucanase from a Biogas Reactor Metagenome

2018 ◽  
Vol 37 (5) ◽  
pp. 454-460
Author(s):  
Carola Schröder ◽  
Christin Burkhardt ◽  
Philip Busch ◽  
Georg Schirrmacher ◽  
Jörg Claren ◽  
...  
Keyword(s):  
Glycoside Hydrolase ◽  
Glycoside Hydrolase Family ◽  
Beta Glucanase ◽  
Glycoside Hydrolase Family 9 ◽  
Biogas Reactor ◽  
Hydrolase Family

The crystal structure of an inverting glycoside hydrolase family 9 exo-β-D-glucosaminidase and the design of glycosynthase

2016 ◽  
Vol 473 (4) ◽  
pp. 463-472 ◽  
Author(s):  
Yuji Honda ◽  
Sachiko Arai ◽  
Kentaro Suzuki ◽  
Motomitsu Kitaoka ◽  
Shinya Fushinobu
Keyword(s):  
Crystal Structure ◽  
Glycoside Hydrolase ◽  
Saturation Mutagenesis ◽  
Glycoside Hydrolase Family ◽  
Glycoside Hydrolase Family 9 ◽  
Hydrolase Family

The crystal structure of an inverting exo-β-D-glucosaminidase from glycoside hydrolase family 9 was determined. This is the first description of the structure of an exo-type enzyme from this family. A glycosynthase was produced from this enzyme through saturation mutagenesis.

Characterization of a novel theme C glycoside hydrolase family 9 cellulase and its CBM-chimeric enzymes

2017 ◽  
Vol 101 (14) ◽  
pp. 5723-5737 ◽  
Author(s):  
Cheng-Jie Duan ◽  
Ming-Yue Huang ◽  
Hao Pang ◽  
Jing Zhao ◽  
Chao-Xing Wu ◽  
...  
Keyword(s):  
Glycoside Hydrolase ◽  
Glycoside Hydrolase Family ◽  
Chimeric Enzymes ◽  
Glycoside Hydrolase Family 9 ◽  
Hydrolase Family

Identification and Characterization of a Glycoside Hydrolase Family 9 Member from the Digestive Gland of the Snail Achatina fulica

2021 ◽  
Author(s):  
Youssef Bacila Sade ◽  
Camila Silva Gonçalves ◽  
Sandra Mara Naressi Scapin ◽  
Guilherme Luiz Pinheiro ◽  
Roberto Becht Flatschart ◽  
...  
Keyword(s):  
Digestive Gland ◽  
Glycoside Hydrolase ◽  
Glycoside Hydrolase Family ◽  
Achatina Fulica ◽  
Glycoside Hydrolase Family 9 ◽  
Identification And Characterization ◽  
Hydrolase Family

scholarly journals An intron-containing glycoside hydrolase family 9 cellulase gene encodes the dominant 90 kDa component of the cellulosome of the anaerobic fungus Piromyces sp. strain E2

2002 ◽  
Vol 365 (1) ◽  
pp. 193-204 ◽  
Author(s):  
Peter J.M. STEENBAKKERS ◽  
Wimal UBHAYASEKERA ◽  
Harry J.A.M. GOOSSEN ◽  
Erik M.H.M. van LIEROP ◽  
Chris van der DRIFT ◽  
...  
Keyword(s):  
Glycoside Hydrolase ◽  
Catalytic Domain ◽  
Homology Modelling ◽  
Large Family ◽  
Glycoside Hydrolase Family ◽  
Reading Frame ◽  
Glycoside Hydrolase Family 9 ◽  
Molecular Masses ◽  
Β Sheet ◽  
Hydrolase Family

The cellulosome produced by Piromyces sp. strain E2 during growth on filter paper was purified by using an optimized cellulose-affinity method consisting of steps of EDTA washing of the cellulose-bound protein followed by elution with water. Three dominant proteins were identified in the cellulosome preparation, with molecular masses of 55, 80 and 90kDa. Treatment of cellulose-bound cellulosome with a number of denaturing agents was also tested. Incubation with 0.5% (w/v) SDS or 8M urea released most cellulosomal proteins, while leaving the greater fraction of the 80, 90 and 170kDa components. To investigate the major 90kDa cellulosome protein further, the corresponding gene, cel9A, was isolated, using immunoscreening and N-terminal sequencing. Inspection of the cel9A genomic organization revealed the presence of four introns, allowing the construction of a consensus for introns in anaerobic fungi. The 2800bp cDNA clone contained an open reading frame of 2334bp encoding a 757-residue extracellular protein. Cel9A includes a 445-residue glycoside hydrolase family 9 catalytic domain, and so is the first fungal representative of this large family. Both modelling of the catalytic domain as well as the activity measured with low level expression in Escherichia coli indicated that Cel9A is an endoglucanase. The catalytic domain is succeeded by a putative β-sheet module of 160 amino acids with unknown function, followed by a threonine-rich linker and three fungal docking domains. Homology modelling of the Cel9A dockerins suggested that the cysteine residues present are all involved in disulphide bridges. The results presented here are used to discuss evolution of glycoside hydrolase family 9 enzymes.

scholarly journals CalkGH9T: A Glycoside Hydrolase Family 9 Enzyme from Clostridium alkalicellulosi

Catalysts ◽  
2021 ◽  
Vol 11 (8) ◽  
pp. 1011
Author(s):  
Paripok Phitsuwan ◽  
Sengthong Lee ◽  
Techly San ◽  
Khanok Ratanakhanokchai
Keyword(s):  
Glycoside Hydrolase ◽  
Cellulose Degradation ◽  
Glycoside Hydrolase Family ◽  
Carbohydrate Binding ◽  
Type I ◽  
Amorphous Cellulose ◽  
Carbohydrate Binding Modules ◽  
Glycoside Hydrolase Family 9 ◽  
Hydrolysis Of ◽  
Hydrolase Family

Glycoside hydrolase family 9 (GH9) endoglucanases are important enzymes for cellulose degradation. However, their activity on cellulose is diverse. Here, we cloned and expressed one GH9 enzyme (CalkGH9T) from Clostridium alkalicellulosi in Escherichia coli. CalkGH9T has a modular structure, containing one GH9 catalytic module, two family 3 carbohydrate binding modules, and one type I dockerin domain. CalkGH9T exhibited maximal activity at pH 7.0–8.0 and 55 °C and was resistant to urea and NaCl. It efficiently hydrolyzed carboxymethyl cellulose (CMC) but poorly degraded regenerated amorphous cellulose (RAC). Despite strongly binding to Avicel, CalkGH9T lacked the ability to hydrolyze this substrate. The hydrolysis of CMC by CalkGH9T produced a series of cello-oligomers, with cellotetraose being preferentially released. Similar proportions of soluble and insoluble reducing ends generated by hydrolysis of RAC indicated non-processive activity. Our study extends our knowledge of the molecular mechanism of cellulose hydrolysis by GH9 family endoglucanases with industrial relevance.

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