type	Journal Article
authors	Ruan J, Hu J, Yin A, Wu W, Cong X, Feng X, Li S
title	Structure of the branched-chain aminotransferase from Streptococcus mutans
journal	Acta Crystallogr D Biol Crystallogr
Activity	2.6.1.42
Family	2.6.1.42.a
sel	selected
ui	22868765
year	(2012)
volume	68
number	8
pages	996-1002
abstract	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 Å 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.
last changed	2019/09/12 13:19