To better understand the molecular basis of glucomylase selectivity, lowenergy conformers of glucosyl disaccharides obtained from relaxed-residue conformational mapping were flexibly docked into the glucoamylase active site using AutoDock 2.2. This procedure ensures that significant conformational s
Carboxyl groups and tryptophan residues in the active site of Rhizopus niveus glucoamylase
โ Scribed by Ritsuko Inokuchi
- Publisher
- John Wiley and Sons
- Year
- 1999
- Tongue
- English
- Weight
- 336 KB
- Volume
- 39
- Category
- Article
- ISSN
- 0233-111X
No coin nor oath required. For personal study only.
๐ SIMILAR VOLUMES
Glucoamylase is an important industrial glucohydrolase with a large specificity range. To investigate its interaction with the monosaccharides D-glucose, D-mannose, and D-galactose and with the substrate analogues 1-deoxynojirimycin, D-glucono-1,5lactone, and methyl a-acarviosinide, MM3(92)optimized
Understanding the role of active-site residues in enzymatic catalysis is of fundamental importance for a microscopic description of the catalytic mechanism, but also for the design of effective enzyme mimics or improvement of existing enzymes (or abzymes) for catalyzing chemical reactions. Site-dire
A new styrene derivative having an L-gulonic moiety, N-(p-vinylbenzyl)-6-L-gulonamide (VB-6-Glco, 3) was synthesized from L-gulono-1,4-lactone and p-vinylbenzylamine. The styrene derivative (3) was subjected to the radical homopolymerization and copolymerization with acrylamide and acrylic acid. The