Crystallographic and enzymatic investigations on the role of Ser558, His610, and Asn614 in the catalytic mechanism of Azotobacter vinelandii dihydrolipoamide acetyltransferase (E2p). [electronic resource]
Producer: 19950510Description: 4287-98 p. digitalISSN:- 0006-2960
- Acetyltransferases -- chemistry
- Amino Acid Sequence
- Asparagine -- chemistry
- Azotobacter vinelandii -- enzymology
- Binding Sites
- Catalysis
- Crystallization
- Crystallography, X-Ray
- Dihydrolipoyllysine-Residue Acetyltransferase
- Histidine -- chemistry
- Hydrogen Bonding
- Hydrogen-Ion Concentration
- Kinetics
- Models, Molecular
- Molecular Sequence Data
- Mutagenesis, Site-Directed
- Pyruvate Dehydrogenase Complex
- Serine -- chemistry
- Structure-Activity Relationship
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Publication Type: Journal Article; Research Support, Non-U.S. Gov't
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