Crystal structures of 2-methylisocitrate lyase in complex with product and with isocitrate inhibitor provide insight into lyase substrate specificity, catalysis and evolution. [electronic resource]
Producer: 20050418Description: 2949-62 p. digitalISSN:- 0006-2960
- Amino Acid Sequence
- Carbon-Carbon Lyases -- chemistry
- Catalysis
- Cloning, Molecular
- Conserved Sequence
- Crystallography, X-Ray
- Escherichia coli -- enzymology
- Escherichia coli Proteins -- chemistry
- Evolution, Molecular
- Kinetics
- Magnesium -- metabolism
- Models, Molecular
- Molecular Sequence Data
- Protein Binding
- Protein Conformation
- Protein Structure, Secondary
- Recombinant Proteins -- chemistry
- Salmonella typhimurium -- enzymology
- Sequence Alignment
- Sequence Homology, Amino Acid
- Substrate Specificity
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Publication Type: Journal Article; Research Support, U.S. Gov't, Non-P.H.S.; Research Support, U.S. Gov't, P.H.S.
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