Sim, Lyann <br/><br/>
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 
<br/><br/> Publication Type: Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't 
<br/><br/><label>ISSN: </label>1089-8638 
<br/><br/><label>Standard No.: </label>10.1016/j.jmb.2007.10.069  doi 
<br/><br/><label>Subjects--Topical Terms: </label><br/>Acarbose--chemistry<br/>Amino Acid Sequence<br/>Apoenzymes--chemistry<br/>Binding Sites<br/>Catalytic Domain<br/>Crystallography, X-Ray<br/>Cysteine--chemistry<br/>Disulfides--chemistry<br/>Enzyme Inhibitors--metabolism<br/>Humans<br/>Hydrogen Bonding<br/>Intestinal Mucosa--enzymology<br/>Intestines--enzymology<br/>Kinetics<br/>Models, Chemical<br/>Models, Molecular<br/>Molecular Sequence Data<br/>Molecular Weight<br/>Mutation<br/>Protein Binding<br/>Protein Structure, Secondary<br/>Protein Subunits--chemistry<br/>Recombinant Proteins--chemistry<br/>Sequence Homology, Amino Acid<br/>Substrate Specificity<br/>alpha-Glucosidases--chemistry