Structures of dCTP deaminase from Escherichia coli with bound substrate and product: reaction mechanism and determinants of mono- and bifunctionality for a family of enzymes. [electronic resource]
Producer: 20050308Description: 3051-9 p. digitalISSN:- 0021-9258
- Alleles
- Amino Acid Sequence
- Arginine -- chemistry
- Binding Sites
- Catalysis
- DNA Mutational Analysis
- Diffusion
- Dose-Response Relationship, Drug
- Escherichia coli -- enzymology
- Genetic Vectors
- Glutamic Acid -- chemistry
- Hydrolysis
- Magnesium -- chemistry
- Methanococcus -- enzymology
- Models, Chemical
- Models, Molecular
- Molecular Sequence Data
- Mutation
- Nucleotide Deaminases -- chemistry
- Phosphates -- chemistry
- Protein Binding
- Protein Conformation
- Protein Structure, Secondary
- Salmonella typhimurium -- enzymology
- Selenomethionine -- chemistry
- Sequence Homology, Amino Acid
- Substrate Specificity
- Thymidylate Synthase -- chemistry
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Publication Type: Journal Article; Research Support, Non-U.S. Gov't
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