Acta Crystallographica Section D
Acta Crystallographica
Section D
STRUCTURAL BIOLOGY
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Acta Cryst.
(2014).
D
70
,
1695-1703
https://doi.org/10.1107/S1399004714007664
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L
-
allo
-Threonine aldolase with an H128Y/S292R mutation from
Aeromonas jandaei
DK-39 reveals the structural basis of changes in substrate stereoselectivity
H.-M. Qin
,
F. L. Imai
,
T. Miyakawa
,
M. Kataoka
,
N. Kitamura
,
N. Urano
,
K. Mori
,
H. Kawabata
,
M. Okai
,
J. Ohtsuka
,
F. Hou
,
K. Nagata
,
S. Shimizu
and
M. Tanokura
The crystal structures of
A. jandaei
L
-
allo
-threonine aldolase and a mutant were refined to 2.59 and 2.50 Å resolution, respectively. The structural basis of the substrate specificity and stereoselectivity has been elucidated.
Keywords:
L
-
allo
-threonine aldolase
;
pyridoxal 5′-phosphate
;
stereoselectivity
;
α/β domain
.
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