Glycosyl hydrolase family 10.

Glycosyl hydrolase family 10.

Endo-1,4-beta-xylanase, GH35 family [Carbohydrate transport and metabolism].

Catalytic NodB homology domain of Clostridium thermocellum acetylxylan esterase and its bacterial homologs. This family is represented by Clostridium thermocellum acetylxylan esterase (CtAXE, EC 3.1.1.72), a member of the carbohydrate esterase 4 (CE4) superfamily. CtAXE deacetylates O-acetylated xylan, a key component of plant cell walls. It shows no detectable activity on generic esterase substrates including para-nitrophenyl acetate. It is specific for sugar-based substrates and will precipitate acetylxylan, as a consequence of deacetylation. CtAXE is a monomeric protein containing a catalytic NodB homology domain with the same overall topology and a deformed (beta/alpha)8 barrel fold as other CE4 esterases. However, due to differences in the topography of the substrate-binding groove, the chemistry of the active center, and metal ion coordination, CtAXE has different metal ion preference and lacks activity on N-acetyl substrates. It is significantly activated by Co2+. Moreover, CtAXE displays distinctly different ligand coordination to the metal ion, utilizing an aspartate, a histidine, and four water molecules, as opposed to the conserved His-His-Asp zinc-binding triad of other CE4 esterases.

Catalytic NodB homology domain of rhizobial NodB-like proteins. This family belongs to the large and functionally diverse carbohydrate esterase 4 (CE4) superfamily, whose members show strong sequence similarity with some variability due to their distinct carbohydrate substrates. It includes many rhizobial NodB chitooligosaccharide N-deacetylase (EC 3.5.1.-)-like proteins, mainly from bacteria and eukaryotes, such as chitin deacetylases (EC 3.5.1.41), bacterial peptidoglycan N-acetylglucosamine deacetylases (EC 3.5.1.-), and acetylxylan esterases (EC 3.1.1.72), which catalyze the N- or O-deacetylation of substrates such as acetylated chitin, peptidoglycan, and acetylated xylan. All members of this family contain a catalytic NodB homology domain with the same overall topology and a deformed (beta/alpha)8 barrel fold with 6- or 7 strands. Their catalytic activity is dependent on the presence of a divalent cation, preferably cobalt or zinc, and they employ a conserved His-His-Asp zinc-binding triad closely associated with the conserved catalytic base (aspartic acid) and acid (histidine) to carry out acid/base catalysis. Several family members show diversity both in metal ion specificities and in the residues that coordinate the metal.

ChainA, ENDO-1,4-BETA-XYLANASE Y [Acetivibrio thermocellus],2W5F_B Chain B, ENDO-1,4-BETA-XYLANASE Y [Acetivibrio thermocellus]

ChainA, ENDO-1,4-BETA-XYLANASE Y [Acetivibrio thermocellus],2WYS_B Chain B, ENDO-1,4-BETA-XYLANASE Y [Acetivibrio thermocellus],2WZE_A Chain A, ENDO-1,4-BETA-XYLANASE Y [Acetivibrio thermocellus],2WZE_B Chain B, ENDO-1,4-BETA-XYLANASE Y [Acetivibrio thermocellus]

Structureof Caldicellulosiruptor danielii GH10 module of glycoside hydrolase WP_045175321 [Caldicellulosiruptor danielii],6D5C_B Structure of Caldicellulosiruptor danielii GH10 module of glycoside hydrolase WP_045175321 [Caldicellulosiruptor danielii],6D5C_C Structure of Caldicellulosiruptor danielii GH10 module of glycoside hydrolase WP_045175321 [Caldicellulosiruptor danielii]

Highlyactive enzymes by automated modular backbone assembly and sequence design [synthetic construct]

Crystalstructure of N-terminal domain of bifunctional CbXyn10C [Caldicellulosiruptor bescii DSM 6725]

Bifunctional endo-1,4-beta-xylanase XylA OS=Ruminococcus flavefaciens OX=1265 GN=xynA PE=3 SV=1

Endo-1,4-beta-xylanase Y OS=Acetivibrio thermocellus OX=1515 GN=xynY PE=1 SV=1

Endo-1,4-beta-xylanase A OS=Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) OX=243274 GN=xynA PE=1 SV=1

Endo-1,4-beta-xylanase A OS=Thermotoga neapolitana OX=2337 GN=xynA PE=1 SV=1

Endo-1,4-beta-xylanase B OS=Butyrivibrio fibrisolvens OX=831 GN=xynB PE=3 SV=1