Kinetic and crystallographic analyses support a sequential-ordered bi bi catalytic mechanism for Escherichia coli glucose-1-phosphate thymidylyltransferase. [electronic resource]
Producer: 20011205Description: 831-43 p. digitalISSN:- 0022-2836
- Amino Acid Sequence
- Binding Sites
- Catalysis
- Crystallography, X-Ray
- Enzyme Inhibitors -- chemistry
- Escherichia coli -- enzymology
- Glucose -- analogs & derivatives
- Glucosephosphates -- metabolism
- Hydrogen Bonding
- Kinetics
- Models, Chemical
- Models, Molecular
- Molecular Sequence Data
- Nucleotidyltransferases -- antagonists & inhibitors
- Protein Structure, Quaternary
- Protein Structure, Tertiary
- Protein Subunits
- Recombinant Fusion Proteins -- chemistry
- Rhamnose -- metabolism
- Sequence Alignment
- Structure-Activity Relationship
- Thymine Nucleotides -- metabolism
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Publication Type: Journal Article; Research Support, Non-U.S. Gov't
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