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

Charnock, S J; Spurway, T D; Xie, H; Beylot, M H; Virden, R; Warren, R A; Hazlewood, G P; Gilbert, H J

Charnock, S J; Spurway, T D; Xie, H; Beylot, M H; Virden, R; Warren, R A; Hazlewood, G P; Gilbert, H J.

Affiliation

Charnock SJ; Department of Biological and Nutritional Sciences, University of Newcastle upon Tyne, Newcastle upon Tyne NE1 7RU, United Kingdom.

J Biol Chem ; 273(48): 32187-99, 1998 Nov 27.

Article in En | MEDLINE | ID: mdl-9822697

Subject(s)

Xylosidases/chemistry; Xylosidases/metabolism; beta-Glucosidase/chemistry; beta-Glucosidase/metabolism; Amino Acid Sequence; Catalysis; Catalytic Domain; Conserved Sequence; Endo-1,4-beta Xylanases; Glucan 1,3-beta-Glucosidase; Gram-Positive Asporogenous Rods/enzymology; Kinetics; Models, Molecular; Mutagenesis, Site-Directed; Protein Conformation; Pseudomonas fluorescens/enzymology; Recombinant Proteins/chemistry; Recombinant Proteins/metabolism; Substrate Specificity

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Collection: 01-internacional Database: MEDLINE Main subject: Xylosidases / Beta-Glucosidase Language: En Journal: J Biol Chem Year: 1998 Document type: Article

Search on Google

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PubMed Links

Collection: 01-internacional Database: MEDLINE Main subject: Xylosidases / Beta-Glucosidase Language: En Journal: J Biol Chem Year: 1998 Document type: Article