Human intestinal maltase-glucoamylase: crystal structure of the N-terminal catalytic subunit and basis of inhibition and substrate specificity.

Sim, Lyann

Human intestinal maltase-glucoamylase: crystal structure of the N-terminal catalytic subunit and basis of inhibition and substrate specificity. [electronic resource] - Journal of molecular biology Jan 2008 - 782-92 p. digital

Publication Type: Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't

1089-8638

10.1016/j.jmb.2007.10.069 doi


Acarbose--chemistry
Amino Acid Sequence
Apoenzymes--chemistry
Binding Sites
Catalytic Domain
Crystallography, X-Ray
Cysteine--chemistry
Disulfides--chemistry
Enzyme Inhibitors--metabolism
Humans
Hydrogen Bonding
Intestinal Mucosa--enzymology
Intestines--enzymology
Kinetics
Models, Chemical
Models, Molecular
Molecular Sequence Data
Molecular Weight
Mutation
Protein Binding
Protein Structure, Secondary
Protein Subunits--chemistry
Recombinant Proteins--chemistry
Sequence Homology, Amino Acid
Substrate Specificity
alpha-Glucosidases--chemistry