Preferential hydrolysis of aberrant intermediates by the type II thioesterase in Escherichia coli nonribosomal enterobactin synthesis: substrate specificities and mutagenic studies on the active-site residues. [electronic resource]
Producer: 20100624Description: 1712-22 p. digitalISSN:- 1520-4995
- Amino Acids -- metabolism
- Catalytic Domain
- Crystallography, X-Ray
- Enterobactin -- biosynthesis
- Escherichia coli -- drug effects
- Escherichia coli Proteins -- chemistry
- Fatty Acid Synthases -- metabolism
- Hydrogen-Ion Concentration -- drug effects
- Hydrolysis -- drug effects
- Hydroxybenzoates -- pharmacology
- Kinetics
- Models, Molecular
- Mutagenesis, Site-Directed
- Mutant Proteins -- chemistry
- Protein Structure, Quaternary
- Protein Structure, Tertiary
- Ribosomes -- drug effects
- Substrate Specificity -- drug effects
- Temperature
- Thiolester Hydrolases -- chemistry
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Publication Type: Journal Article; Research Support, Non-U.S. Gov't
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