Stereochemical Course of Hydrolysis Catalysed by α-l-Rhamnosyl and α-d-Galacturonosyl Hydrolases fromAspergillus aculeatus
- 26 January 1998
- journal article
- Published by Elsevier in Biochemical and Biophysical Research Communications
- Vol. 242 (3) , 552-559
- https://doi.org/10.1006/bbrc.1997.8009
Abstract
No abstract availableKeywords
This publication has 38 references indexed in Scilit:
- The crystal structure of rhamnogalacturonase A from Aspergillus aculeatus: a right-handed parallel β helixStructure, 1997
- Stereochemical course of hydrolysis catalyzed by arabinofuranosyl hydrolasesFEBS Letters, 1996
- Inversion of configuration during hydrolysis of α‐1,4‐galacturonidic linkage by three Aspergillus polygalacturonasesFEBS Letters, 1996
- Rhamnogalacturonase B from Aspergillus aculeatus Is a Rhamnogalacturonan [alpha]-L-Rhamnopyranosyl-(1->4)-[alpha]-D-Galactopyranosyluronide LyasePlant Physiology, 1996
- Rhamnogalacturonan [alpha]-L-Rhamnopyranohydrolase (A Novel Enzyme Specific for the Terminal Nonreducing Rhamnosyl Unit in Rhamnogalacturonan Regions of Pectin)Plant Physiology, 1994
- Mechanisms of enzymatic glycoside hydrolysisCurrent Opinion in Structural Biology, 1994
- Specificity mapping of cellulolytic enzymes: Classification into families of structurally related proteins confirmed by biochemical analysisProtein Science, 1992
- The arabinanases of Aspergillus niger — Purification and characterisation of two α-l-arabinofuranosidases and an endo-1,5-α-l-arabinanaseCarbohydrate Polymers, 1988
- The Size of the Substrate‐Binding Site of an Aspergillus niger Extracellular EndopolygalacturonaseEuropean Journal of Biochemistry, 1973
- Polysaccharide conformation. Part VII. Model building computations for α-1,4 galacturonan and the kinking function ofL-rhamnose residues in pectic substancesJournal of the Chemical Society B: Physical Organic, 1971