Substrate specificity and subsite mobility in T. aurantiacus xylanase 10A (Q27636747)

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S Kalogiannis

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K Eckert

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S C Teixeira

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M K Bhat

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C Andrei

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R W Pickersgill

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S Larsen

Purification of xylanase, beta-glucosidase, endocellulase, and exocellulase from a thermophilic fungus, Thermoascus aurantiacus

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language of work or name

English

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publication date

7 December 2001

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published in

FEBS Letters

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volume

509

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issue

2

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page(s)

303-8

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cites work

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Crystal structure at 1.8 A resolution and proposed amino acid sequence of a thermostable xylanase from Thermoascus aurantiacus

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Structure of the catalytic core of the family F xylanase from Pseudomonas fluorescens and identification of the xylopentaose-binding sites

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Crystal structure of the catalytic domain of the beta-1,4-glycanase cex from Cellulomonas fimi

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A common protein fold and similar active site in two distinct families of β-glycanases

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Structure of the xylanase from Penicillium simplicissimum

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Crystal structure of Streptomyces olivaceoviridis E-86 beta-xylanase containing xylan-binding domain

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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-strand

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Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases

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Characterization of active-site aromatic residues in xylanase A from Streptomyces lividans

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Exploring the Cellulose/Xylan Specificity of the β-1,4-Glycanase Cex from Cellulomonas fimi through Crystallography and Mutation,

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Substrate specificity in glycoside hydrolase family 10. Structural and kinetic analysis of the Streptomyces lividans xylanase 10A

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Nomenclature for sugar-binding subsites in glycosyl hydrolases

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Xylan binding subsite mapping in the xylanase from Penicillium simplicissimum using xylooligosaccharides as cryo-protectant

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X-ray crystallographic study of xylopentaose binding to Pseudomonas fluorescens xylanase A

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High resolution X-ray crystallography shows that ascorbate is a cofactor for myrosinase and substitutes for the function of the catalytic base

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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.

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The topology of the substrate binding clefts of glycosyl hydrolase family 10 xylanases are not conserved

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