The thermostable alpha-l-rhamnosidase RamA of Clostridium stercorarium: biochemical characterization and primary structure of a bacterial alpha-l-rhamnoside hydrolase, a new type of inverting glycoside hydrolase-Reference-Cited by-同舟云学术

The thermostable alpha-l-rhamnosidase RamA of Clostridium stercorarium: biochemical characterization and primary structure of a bacterial alpha-l-rhamnoside hydrolase, a new type of inverting glycoside hydrolase

Published:2000-01 Issue:1 Volume:35 Page:173-179
ISSN:0950-382X
Container-title:Molecular Microbiology
language:en
Short-container-title:Mol Microbiol

Author:

Zverlov Vladimir V.,Hertel Christian,Bronnenmeier Karin,Hroch Angelika,Kellermann J.,Schwarz Wolfgang H.

Publisher

Wiley

Subject

Molecular Biology,Microbiology

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1046/j.1365-2958.2000.01691.x/fullpdf

Reference33 articles.

1. Enzymatic Hydrolysis of the Cytotoxic Triterpenoid Glycoside Virgaureasaponin 1

2. Juvenile-Specific Localization and Accumulation of a Rhamnosyltransferase and Its Bitter Flavonoid in Foliage, Flowers, and Young Citrus Fruits

3. Separation of the cellulytic and xylanolytic enzymes of Clostridium stercorarium

4. 4P.M. Coutinho, and B. Henrissat (1999 ) Carbohydrate-active Enzymes server at URL http://afmb.cnrs-mrs.fr/~pedro/CAZY/db.html

5. 1H-N.m.r. study of l-rhamnose, methyl α-l-rhamnopyranoside, and 4-O-β-d-galactopyranosyl-l-rhamnose in deuterium oxide

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