Trefoil (Acidic Fibroblast Growth Factor, subunit A)
endo-(1->4)-beta-xylan 4-xylanohydrolase
Multiplicity of beta-1,4-xylanase in microorganisms: functions and applications.
Structure of rice-straw arabinoglucuronoxylan and specificity of Streptomyces xylanase toward the xylan.
Structural and functional relationships in two families of beta-1,4-glycanases.
Domains in microbial beta-1, 4-glycanases: sequence conservation, function, and enzyme families.
Mode of action of three endo-beta-1,4-xylanases of Streptomyces lividans.
Characterization and N-terminal amino acid sequences of beta-(1-4)endoxylanases from Streptomyces roseiscleroticus: purification incorporating a bioprocessing agent.
Identification of two acidic residues involved in the catalysis of xylanase A from Streptomyces lividans.
Substrate specificity of Streptomyces beta-xylanase toward glucoxylan.
Increase in catalytic activity and thermostability of the xylanase A of Streptomyces lividans 1326 by site-specific mutagenesis.
Alteration of the cleavage mode and of the transglycosylation reactions of the xylanase A of Streptomyces lividans 1326 by site-directed mutagenesis of the Asn173 residue.
Crystal structure, at 2.6-A resolution, of the Streptomyces lividans xylanase A, a member of the F family of beta-1,4-D-glycanases.
Beta-glucosidase, beta-galactosidase, family A cellulases, family F xylanases and two barley glycanases form a superfamily of enzymes with 8-fold beta/alpha architecture and with two conserved glutamates near the carboxy-terminal ends of beta-strands four and seven.
Characterization of two important histidine residues in the active site of xylanase A from Streptomyces lividans, a family 10 glycanase.
Xylanolytic enzymes from fungi and bacteria.
Key residues in subsite F play a critical role in the activity of Pseudomonas fluorescens subspecies cellulosa xylanase A against xylooligosaccharides but not against highly polymeric substrates such as xylan.
Calcium protects a mesophilic xylanase from proteinase inactivation and thermal unfolding.
Endo-beta-1,4-xylanase families: differences in catalytic properties.
Asparagine-127 of xylanase A from Streptomyces lividans, a key residue in glycosyl hydrolases of superfamily 4/7: kinetic evidence for its involvement in stabilization of the catalytic intermediate.
Site-directed mutagenesis study of a conserved residue in family 10 glycanases: histidine 86 of xylanase A from Streptomyces lividans.
An investigation of the nature and function of module 10 in a family F/10 xylanase FXYN of Streptomyces olivaceoviridis E-86 by module shuffling with the Cex of Cellulomonas fimi and by site-directed mutagenesis.
Significant enhancement in the binding of p-nitrophenyl-beta-D-xylobioside by the E128H mutant F/10 xylanase from Streptomyces olivaceoviridis E-86.
Module-intron correlation and intron sliding in family F/10 xylanase genes.
Characterization of active-site aromatic residues in xylanase A from Streptomyces lividans.
Crystal structure of Streptomyces olivaceoviridis E-86 beta-xylanase containing xylan-binding domain.
Substrate specificity in glycoside hydrolase family 10. Tyrosine 87 and leucine 314 play a pivotal role in discriminating between glucose and xylose binding in the proximal active site of Pseudomonas cellulosa xylanase 10A.
Crystal structures of the sugar complexes of Streptomyces olivaceoviridis E-86 xylanase: sugar binding structure of the family 13 carbohydrate binding module.
High-resolution crystal structures of the lectin-like xylan binding domain from Streptomyces lividans xylanase 10A with bound substrates reveal a novel mode of xylan binding.
A xylobiose-derived isofagomine lactam glycosidase inhibitor binds as its amide tautomer.
Structure and function of a family 10 beta-xylanase chimera of Streptomyces olivaceoviridis E-86 FXYN and Cellulomonas fimi Cex.
This family belongs to the glycosidase family-10, which has a retaining mechanism (equatorial to equatorial conformation), and also a family of 4/7 superfamily, which has got catalytic residues at the C-terminal ends of beta-4 and beta-7 on the (alpha/beta)8 barrel fold. According to the literature [22], Glu236 and Glu128 (of 1ece) act as a nucleophile and acid-base, respectively. The catalysis proceeds through a dissociative-type (or SN1-like) mechanism, with a formation of oxocarbonium ion in the transition state, during the glycosylation of the active site. During the glycosylation, Glu236 approaches the C1 atom of xylan substrate, whilst Glu128 protonates the leaving sugar group. At the second stage, or during the deglycosylation, a water molecule can be activated by a general base, Glu128. This deglycosylation also goes through the dissociative-type reaction with an oxocarbonium ion in the transition state, in which water replaced the xylan leaving group in the first step. According to the paper [19], the conserved residue at active site, Asn127, may stabilize the intermediate or transition state. Meanwhile, the paper [20] mentioned that His86 might modulate the acid-base catalyst (Glu128), by maintaining the elevated pKa of the catalytic residue. Moreover, comparing the structural data with that of the other family-10 enzyme, xylanase (E.C. 3.2.1.8) (D00479 in EzCatDB), His207-Asp238 dyad seems to stabilize the leaving nucleophile, Glu236, during the deglycosylation.