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

The role of four aromatic residues (W85, Y172, W266 and W274) in the structure–function relationship in xylanase A from Streptomyces lividans (XlnA) was investigated by site-directed mutagenesis where each residue was subjected to three substitutions (W85A/H/F; W266A/H/F; W274A/H/F and Y172A/F/S). T...

Ausführliche Beschreibung

Gespeichert in:

Bibliographische Detailangaben
Veröffentlicht in:	Protein engineering 1999-03, Vol.12 (3), p.251-257
Hauptverfasser:	Roberge, Martin, Shareck, Francıois, Morosoli, Rolf, Kluepfel, Dieter, Dupont, Claude
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Base Sequence Binding Sites Catalytic Domain Circular Dichroism DNA Primers Endo-1,4-beta Xylanases Enzyme Stability family 10 hydrolase glycosyl hydrolase Molecular Sequence Data Mutagenesis, Site-Directed Sequence Homology, Amino Acid site-directed mutagenesis Spectrophotometry, Ultraviolet Streptomyces - enzymology Streptomyces lividans structure–function xylanase Xylosidases - chemistry Xylosidases - genetics Xylosidases - metabolism
Online-Zugang:	Volltext
Tags:	Tag hinzufügen Keine Tags, Fügen Sie den ersten Tag hinzu!

Schreiben Sie den ersten Kommentar!