Skip to main navigation
Skip to search
Skip to main content
Home
Profiles
Departments and Centers
Scholarly Works
Activities
Equipment
Grants
Prizes
Search by expertise, name or affiliation
Energetic and mechanistic studies of glucoamylase using molecular recognition of maltose OH groups coupled with site-directed mutagenesis
Michael R. Sierks
, Birte Svensson
Research output
:
Contribution to journal
›
Article
›
peer-review
14
Scopus citations
Overview
Fingerprint
Fingerprint
Dive into the research topics of 'Energetic and mechanistic studies of glucoamylase using molecular recognition of maltose OH groups coupled with site-directed mutagenesis'. Together they form a unique fingerprint.
Sort by
Weight
Alphabetically
Chemical Compounds
Molecular recognition
Mutagenesis
Glucan 1,4-alpha-Glucosidase
Maltose
Binding energy
Substrates
Hydroxyl Radical
Substitution reactions
Hydrogen bonds
Enzymes
Aspergillus
Crystal structure
Stabilization
Medicine & Life Sciences
Glucan 1,4-alpha-Glucosidase
Maltose
Hydroxyl Radical
Site-Directed Mutagenesis
Catalytic Domain
Hydrogen
Enzymes
Aspergillus niger
Amides
Mutation