Human intestinal maltase-glucoamylase: crystal structure of the N-terminal catalytic subunit and basis of inhibition and substrate specificity. [electronic resource]
Producer: 20080111Description: 782-92 p. digitalISSN:- 1089-8638
- 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
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Publication Type: Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't
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