scholarly journals Organization and expression of the Escherichia coli K-12 dad operon encoding the smaller subunit of D-amino acid dehydrogenase and the catabolic alanine racemase.

1994 ◽  
Vol 176 (5) ◽  
pp. 1500-1510 ◽  
Author(s):  
M Lobocka ◽  
J Hennig ◽  
J Wild ◽  
T Kłopotowski
Biochemistry ◽  
1981 ◽  
Vol 20 (21) ◽  
pp. 6272-6279 ◽  
Author(s):  
Paula J. Olsiewski ◽  
Gregory J. Kaczorowski ◽  
Christopher Walsh ◽  
H. Ronald Kaback

RSC Advances ◽  
2016 ◽  
Vol 6 (84) ◽  
pp. 80557-80563 ◽  
Author(s):  
Jun Cheng ◽  
Guochao Xu ◽  
Ruizhi Han ◽  
Jinjun Dong ◽  
Ye Ni

An amino acid dehydrogenase from Bacillus clausii (BcAADH) was identified and overexpressed in Escherichia coli BL21(DE3) for the preparation of l-phenylglycine from benzoylformic acid.


2002 ◽  
Vol 277 (15) ◽  
pp. 12861-12867 ◽  
Author(s):  
Takenori Satomura ◽  
Ryushi Kawakami ◽  
Haruhiko Sakuraba ◽  
Toshihisa Ohshima

2004 ◽  
Vol 186 (13) ◽  
pp. 4402-4406 ◽  
Author(s):  
Volkmar Braun ◽  
Christina Herrmann

ABSTRACT Replacement of glutamate 176, the only charged amino acid in the third transmembrane helix of ExbB, with alanine (E176A) abolished ExbB activity in all determined ExbB-dependent functions of Escherichia coli. Combination of the mutations T148A in the second transmembrane helix and T181A in the third transmembrane helix, proposed to form part of a proton pathway through ExbB, also resulted in inactive ExbB. E176 and T148 are strictly conserved in ExbB and TolQ proteins, and T181 is almost strictly conserved in ExbB, TolQ, and MotA.


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