scholarly journals A plasmid borne, functionally novel glycoside hydrolase family 30 subfamily 8 endoxylanase from solventogenic Clostridium

2018 ◽  
Vol 475 (9) ◽  
pp. 1533-1551 ◽  
Author(s):  
Franz J. St John ◽  
Diane Dietrich ◽  
Casey Crooks ◽  
Peter Balogun ◽  
Vesna de Serrano ◽  
...  
Keyword(s):  
Glycoside Hydrolase ◽  
Catalytic Domain ◽  
Relative Rate ◽  
Salt Bridge ◽  
Crystallographic Structure ◽  
Glycoside Hydrolase Family ◽  
Significant Activity ◽  
Sequence Comparisons ◽  
Hydrolase Family ◽  
Glycoside Hydrolase Family 30

Glycoside hydrolase family 30 subfamily 8 (GH30-8) β-1,4-endoxylanases are known for their appendage-dependent function requiring recognition of an α-1,2-linked glucuronic acid (GlcA) common to glucuronoxylans for hydrolysis. Structural studies have indicated that the GlcA moiety of glucuronoxylans is coordinated through six hydrogen bonds and a salt bridge. These GlcA-dependent endoxylanases do not have significant activity on xylans that do not bear GlcA substitutions such as unsubstituted linear xylooligosaccharides or cereal bran arabinoxylans. In the present study, we present the structural and biochemical characteristics of xylanase 30A from Clostridium acetobutylicum (CaXyn30A) which was originally selected for study due to predicted structural differences within the GlcA coordination loops. Amino acid sequence comparisons indicated that this Gram-positive-derived GH30-8 more closely resembles Gram-negative derived forms of these endoxylanases: a hypothesis borne out in the developed crystallographic structure model of the CaXyn30A catalytic domain (CaXyn30A-CD). CaXyn30A-CD hydrolyzes xylans to linear and substituted oligoxylosides showing the greatest rate with the highly arabinofuranose (Araf)-substituted cereal arabinoxylans. CaXyn30A-CD hydrolyzes xylooligosaccharides larger than xylotriose and shows an increased relative rate of hydrolysis for xylooligosaccharides containing α-1,2-linked arabinofuranose substitutions. Biochemical analysis confirms that CaXyn30A benefits from five xylose-binding subsites which extend from the −3 subsite to the +2 subsite of the binding cleft. These studies indicate that CaXyn30A is a GlcA-independent endoxylanase that may have evolved for the preferential recognition of α-1,2-Araf substitutions on xylan chains.

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

β-Glucuronidase from Lactobacillus brevis useful for baicalin hydrolysis belongs to glycoside hydrolase family 30

2013 ◽  
Vol 98 (9) ◽  
pp. 4021-4032 ◽  
Author(s):  
Haruko Sakurama ◽  
Shigenobu Kishino ◽  
Yoshie Uchibori ◽  
Yasunori Yonejima ◽  
Hisashi Ashida ◽  
...  
Keyword(s):  
Glycoside Hydrolase ◽  
Lactobacillus Brevis ◽  
Glycoside Hydrolase Family ◽  
Hydrolase Family ◽  
Glycoside Hydrolase Family 30

First Crystallographic Structure of a Xylanase from Glycoside Hydrolase Family 5:  Implications for Catalysis†,‡

Biochemistry ◽  
2003 ◽  
Vol 42 (28) ◽  
pp. 8411-8422 ◽  
Author(s):  
Steven B. Larson ◽  
John Day ◽  
Ana Paulina Barba de la Rosa ◽  
Noel T. Keen ◽  
Alexander McPherson
Keyword(s):  
Glycoside Hydrolase ◽  
Crystallographic Structure ◽  
Glycoside Hydrolase Family ◽  
Hydrolase Family

scholarly journals Glycoside Hydrolase family 30 harbors fungal subfamilies with distinct polysaccharide specificities

2021 ◽  
Author(s):  
Xinxin Li ◽  
Dimitrios Kouzounis ◽  
Mirjam A. Kabel ◽  
Ronald P. de Vries ◽  
Adiphol Dilokpimol
Keyword(s):  
Glycoside Hydrolase ◽  
Glycoside Hydrolase Family ◽  
Hydrolase Family ◽  
Glycoside Hydrolase Family 30

Crystal structures of the GH6 Orpinomyces sp. Y102 CelC7 enzyme with exo and endo activity and its complex with cellobiose

2019 ◽  
Vol 75 (12) ◽  
pp. 1138-1147
Author(s):  
Hsiao-Chuan Huang ◽  
Liu-Hong Qi ◽  
Yo-Chia Chen ◽  
Li-Chu Tsai
Keyword(s):  
Enzymatic Hydrolysis ◽  
Crystal Structures ◽  
Active Site ◽  
Binding Sites ◽  
Glycoside Hydrolase ◽  
Catalytic Domain ◽  
Glycoside Hydrolase Family ◽  
Substrate Binding Sites ◽  
Key Residues ◽  
Hydrolase Family

The catalytic domain (residues 128–449) of the Orpinomyces sp. Y102 CelC7 enzyme (Orp CelC7) exhibits cellobiohydrolase and cellotriohydrolase activities. Crystal structures of Orp CelC7 and its cellobiose-bound complex have been solved at resolutions of 1.80 and 2.78 Å, respectively. Cellobiose occupies subsites +1 and +2 within the active site of Orp CelC7 and forms hydrogen bonds to two key residues: Asp248 and Asp409. Furthermore, its substrate-binding sites have both tunnel-like and open-cleft conformations, suggesting that the glycoside hydrolase family 6 (GH6) Orp CelC7 enzyme may perform enzymatic hydrolysis in the same way as endoglucanases and cellobiohydrolases. LC-MS/MS analysis revealed cellobiose (major) and cellotriose (minor) to be the respective products of endo and exo activity of the GH6 Orp CelC7.

scholarly journals Evidence for Temporal Regulation of the Two Pseudomonas cellulosa Xylanases Belonging to Glycoside Hydrolase Family 11

2002 ◽  
Vol 184 (15) ◽  
pp. 4124-4133 ◽  
Author(s):  
Kaveh Emami ◽  
Tibor Nagy ◽  
Carlos M. G. A. Fontes ◽  
Luis M. A. Ferreira ◽  
Harry J. Gilbert
Keyword(s):  
Glycoside Hydrolase ◽  
Catalytic Domain ◽  
Xylanase Activity ◽  
Glycoside Hydrolase Family ◽  
Side Chains ◽  
Temporal Regulation ◽  
Degrading Bacterium ◽  
Genes Encoding ◽  
Combined Action ◽  
Hydrolase Family

ABSTRACT Pseudomonas cellulosa is a highly efficient xylan-degrading bacterium. Genes encoding five xylanases, and several accessory enzymes, which remove the various side chains that decorate the xylan backbone, have been isolated from the pseudomonad and characterized. The xylanase genes consist of xyn10A, xyn10B, xyn10C, xyn10D, and xyn11A, which encode Xyn10A, Xyn10B, Xyn10C, Xyn10D, and Xyn11A, respectively. In this study a sixth xylanase gene, xyn11B, was isolated which encodes a 357-residue modular enzyme, designated Xyn11B, comprising a glycoside hydrolase family 11 catalytic domain appended to a C-terminal X-14 module, a homologue of which binds to xylan. Localization studies showed that the two xylanases with glycoside hydrolase family (GH) 11 catalytic modules, Xyn11A and Xyn11B, are secreted into the culture medium, whereas Xyn10C is membrane bound. xyn10C, xyn10D, xyn11A, and xyn11B were all abundantly expressed when the bacterium was cultured on xylan or β-glucan but not on medium containing mannan, whereas glucose repressed transcription of these genes. Although all of the xylanase genes were induced by the same polysaccharides, temporal regulation of xyn11A and xyn11B was apparent on xylan-containing media. Transcription of xyn11A occurred earlier than transcription of xyn11B, which is consistent with the predicted mode of action of the encoded enzymes. Xyn11A, but not Xyn11B, exhibits xylan esterase activity, and the removal of acetate side chains is required for xylanases to hydrolyze the xylan backbone. A transposon mutant of P. cellulosa in which xyn11A and xyn11B were inactive displayed greatly reduced extracellular but normal cell-associated xylanase activity, and its growth rate on medium containing xylan was indistinguishable from wild-type P. cellulosa. Based on the data presented here, we propose a model for xylan degradation by P. cellulosa in which the GH11 enzymes convert decorated xylans into substituted xylooligosaccharides, which are then hydrolyzed to their constituent sugars by the combined action of cell-associated GH10 xylanases and side chain-cleaving enzymes.

scholarly journals Purification, characterization and gene cloning of two α-l-arabinofuranosidases from Streptomyces chartreusis GS901

2000 ◽  
Vol 346 (1) ◽  
pp. 9-15 ◽  
Author(s):  
Noriki MATSUO ◽  
Satoshi KANEKO ◽  
Atsushi KUNO ◽  
Hideyuki KOBAYASHI ◽  
Isao KUSAKABE
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Glycoside Hydrolase ◽  
Catalytic Domain ◽  
Gum Arabic ◽  
Glycoside Hydrolases ◽  
Glycoside Hydrolase Family ◽  
Amino Acid Sequencing ◽  
Molecular Masses ◽  
Hydrolase Family

α-L-Arabinofuranosidases I and II were purified from the culture filtrate of Streptomyces chartreusis GS901 and were found to have molecular masses of 80 and 37 kDa and pI values of 6.6 and 7.5 respectively. Both enzymes demonstrated slight reactivity towards arabinoxylan and arabinogalactan as substrates but did not hydrolyse gum arabic or arabinoxylo-oligosaccharides. α-L-Arabinofuranosidase I hydrolysed all of the α-linkage types that normally occur between two α-L-arabinofuranosyl residues, with the following decreasing order of reactivity being observed for the respective disaccharide linkages: α-(1 → 2) α-(1 → 3) α-(1 → 5). This enzyme cleaved the (1 → 3) linkages of the arabinosyl side-chains of methyl 3,5-di-O-α-L-arabinofuranosyl-α-L-arabinofuranoside in preference to the (1 → 5) linkages. α-L-Arabinofuranosidase I hydrolysed approx. 30% of the arabinan but hydrolysed hardly any linear arabinan. In contrast, α-L-Arabinofuranosidase II hydrolysed only (1 → 5)-arabinofuranobioside among the regioisomeric methyl arabinobiosides and did not hydrolyse the arabinotrioside. Linear 1 → 5-linked arabinan was a good substrate for this enzyme, but it hydrolysed hardly any of the arabinan. Synergism between the two enzymes was observed in the conversion of arabinan and debranched arabinan into arabinose. Complete amino acid sequencing of α-L-arabinofuranosidase I indicated that the enzyme consists of a central catalytic domain that belongs to family 51 of the glycoside hydrolases and additionally that unknown functional domains exist in the N-terminal and C-terminal regions. The amino acid sequence of α-L-arabinofuranosidase II indicated that this enzyme belongs to family 43 of the glycoside hydrolase family and, as this is the first report of an exo-1,5-α-L-arabinofuranosidase, it represents a novel type of enzyme.

scholarly journals Structural analysis of a glycoside hydrolase family 43 arabinoxylan arabinofuranohydrolase in complex with xylotetraose reveals a different binding mechanism compared with other members of the same family

2009 ◽  
Vol 418 (1) ◽  
pp. 39-47 ◽  
Author(s):  
Elien Vandermarliere ◽  
Tine M. Bourgois ◽  
Martyn D. Winn ◽  
Steven van Campenhout ◽  
Guido Volckaert ◽  
...  
Keyword(s):  
Glycoside Hydrolase ◽  
Catalytic Domain ◽  
Crystallographic Analysis ◽  
Glycoside Hydrolase Family ◽  
Carbohydrate Binding ◽  
Carbohydrate Binding Module ◽  
Stacking Interactions ◽  
Glycoside Hydrolase Family 43 ◽  
Arabinoxylan Arabinofuranohydrolase ◽  
Hydrolase Family

AXHs (arabinoxylan arabinofuranohydrolases) are α-L-arabinofuranosidases that specifically hydrolyse the glycosidic bond between arabinofuranosyl substituents and xylopyranosyl backbone residues of arabinoxylan. Bacillus subtilis was recently shown to produce an AXH that cleaves arabinose units from O-2- or O-3-mono-substituted xylose residues: BsAXH-m2,3 (B. subtilis AXH-m2,3). Crystallographic analysis reveals a two-domain structure for this enzyme: a catalytic domain displaying a five-bladed β-propeller fold characteristic of GH (glycoside hydrolase) family 43 and a CBM (carbohydrate-binding module) with a β-sandwich fold belonging to CBM family 6. Binding of substrate to BsAXH-m2,3 is largely based on hydrophobic stacking interactions, which probably allow the positional flexibility needed to hydrolyse both arabinose substituents at the O-2 or O-3 position of the xylose unit. Superposition of the BsAXH-m2,3 structure with known structures of the GH family 43 exo-acting enzymes, β-xylosidase and α-L-arabinanase, each in complex with their substrate, reveals a different orientation of the sugar backbone.

Sign in / Sign up

Export Citation Format

Share Document