|
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 |
|