The Pseudomonas cellulosa glycoside hydrolase family 51 arabinofuranosidase exhibits wide substrate specificity (Q28348905)

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A G Voragen

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C H Doeswijk-Voragen

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H J Gilbert

Pseudomonas cellulosa expresses a single membrane-bound glycoside hydrolase family 51 arabinofuranosidase

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language of work or name

English

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publication date

15 September 2001

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published in

Biochemical Journal

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volume

358

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issue

Pt 3

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page(s)

607-14

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cites work

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Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4

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Pseudomonas cellulose-binding domains mediate their effects by increasing enzyme substrate proximity

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Arabinanase A from Pseudomonas fluorescens subsp. cellulosa exhibits both an endo- and an exo- mode of action.

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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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Mechanistic consequences of mutation of active site carboxylates in a retaining beta-1,4-glycanase from Cellulomonas fimi

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Cloning of the Aspergillus niger gene encoding alpha-L-arabinofuranosidase A.

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Purification, characterization and gene cloning of two alpha-L-arabinofuranosidases from streptomyces chartreusis GS901.

29 September 2017

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Possible roles for a non-modular, thermostable and proteinase-resistant cellulase from the mesophilic aerobic soil bacterium Cellvibrio mixtus

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Xylanase B and an arabinofuranosidase from Pseudomonas fluorescens subsp. cellulosa contain identical cellulose-binding domains and are encoded by adjacent genes

2 June 2018

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Nucleotide sequence of arfB of Clostridium stercorarium, and prediction of catalytic residues of alpha-L-arabinofuranosidases based on local similarity with several families of glycosyl hydrolases.

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

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inferred from PubMed ID database lookup

12 December 2020

based on heuristic

Identification of the Acid/Base Catalyst in Agrobacterium faecalis .beta.-Glucosidase by Kinetic Analysis of Mutants

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inferred from PubMed ID database lookup

12 December 2020

based on heuristic

A new arabinofuranohydrolase from Bifidobacterium adolescentis able to remove arabinosyl residues from double-substituted xylose units in arabinoxylan

1 reference

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https://pubmed.ncbi.nlm.nih.gov/11535122