Crystal structure of LL-diaminopimelate aminotransferase from Arabidopsis thaliana: a recently discovered enzyme in the biosynthesis of L-lysine by plants and Chlamydia. [electronic resource]
Producer: 20070927Description: 685-702 p. digitalISSN:- 0022-2836
- Amino Acid Sequence
- Arabidopsis -- enzymology
- Arabidopsis Proteins -- chemistry
- Binding Sites
- Catalysis
- Chlamydia -- enzymology
- Crystallography, X-Ray
- Diaminopimelic Acid -- chemistry
- Dimerization
- Glutamic Acid -- metabolism
- Lysine -- biosynthesis
- Malates -- metabolism
- Models, Molecular
- Molecular Sequence Data
- Protein Structure, Secondary
- Protein Subunits -- chemistry
- Pyridoxal Phosphate -- metabolism
- Sequence Alignment
- Sequence Homology, Amino Acid
- Solvents
- Static Electricity
- Substrate Specificity
- Transaminases -- chemistry
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Publication Type: Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.
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