Crystal structure of LL-diaminopimelate aminotransferase from Arabidopsis thaliana: a recently discovered enzyme in the biosynthesis of L-lysine by plants and Chlamydia.

Watanabe, Nobuhiko

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] - Journal of molecular biology Aug 2007 - 685-702 p. digital

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.

0022-2836

10.1016/j.jmb.2007.05.061 doi


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