Mutational analysis of Mycobacterium tuberculosis lysine ɛ-aminotransferase and inhibitor co-crystal structures, reveals distinct binding modes
Author:
Funder
Council of Scientific and Industrial Research
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry,Biophysics
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3. A subfamily of PLP-dependent enzymes specialized in handling terminal amines;Schiroli;Biochim. Biophys. Acta,2015
4. Direct evidence for a glutamate switch necessary for substrate recognition: crystal structures of lysine ε-aminotransferase (Rv3290c) from Mycobacterium tuberculosis H37Rv;Tripathi;J. Mol. Biol.,2006
5. Overexpression, purification and crystallization of lysine ε-aminotransferase (Rv3290c) from Mycobacterium tuberculosis H37Rv;Tripathi;Actacrystallograph. Sect. F Struct. Biol. Cryst. Commun.,2006
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