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Publication Abstract from PubMed

The branched-chain amino-acid aminotransferase from Streptococcus mutans (SmIlvE) was recombinantly expressed in Escherichia coli with high yield. An effective purification protocol was established. A bioactivity assay indicated that SmIlvE had aminotransferase activity. The specific activity of SmIlvE towards amino-acid substrates was found to be as follows (in descending order): Ile > Leu > Val > Trp > Gly. The protein was crystallized using the hanging-drop vapour-diffusion method with PEG 3350 as the primary precipitant. The structure of SmIlvE was solved at 1.97 A resolution by the molecular-replacement method. Comparison with structures of homologous proteins enabled the identification of conserved structural elements that might play a role in substrate binding. Further work is needed to confirm the interaction between SmIlvE and its substrates by determining the structures of their complexes.

Structure of the branched-chain aminotransferase from Streptococcus mutans.,Ruan J, Hu J, Yin A, Wu W, Cong X, Feng X, Li S Acta Crystallogr D Biol Crystallogr. 2012 Aug;68(Pt 8):996-1002. Epub 2012 Jul, 17. PMID:22868765^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.