Determination of the genetic, molecular, and biochemical basis of the Arabidopsis thaliana thiamin auxotroph th1

2007 ◽  
Vol 459 (1) ◽  
pp. 107-114 ◽  
Author(s):  
Imad Ajjawi ◽  
Yoseph Tsegaye ◽  
David Shintani
2011 ◽  
Vol 23 (4) ◽  
pp. 324-331 ◽  
Author(s):  
Chin-Lin Hsieh ◽  
Kai-Wun Yeh ◽  
Luit J. De Kok ◽  
Ryh-Nan Pan ◽  
Yueh-Hsiung Kuo ◽  
...  

2008 ◽  
Vol 56 (16) ◽  
pp. 6825-6834 ◽  
Author(s):  
Xue Feng Chang ◽  
Richard Chandra ◽  
Thomas Berleth ◽  
Rodger P. Beatson

2014 ◽  
Vol 4 (1) ◽  
Author(s):  
María I. Vaquero-Sedas ◽  
Miguel A. Vega-Palas

Sugar Tech ◽  
2019 ◽  
Vol 22 (2) ◽  
pp. 259-265
Author(s):  
S. N. Sushil ◽  
Amaresh Chandra ◽  
Sharmila Roy ◽  
A. K. Jaiswal ◽  
M. R. Singh ◽  
...  

2008 ◽  
Vol 55 (1) ◽  
pp. 151-160 ◽  
Author(s):  
Blanka Szurmak ◽  
Aleksandra Wysłouch-Cieszyńska ◽  
Małgorzata Wszelaka-Rylik ◽  
Wojciech Bal ◽  
Marta Dobrzańska

Asymmetrical diadenosine 5',5''-P(1)P(4) tetraphosphate (Ap(4)A) hydrolases are key enzymes controlling the in vivo concentration of Ap(4)A--an important signaling molecule involved in regulation of DNA replication and repair, signaling in stress response and apoptosis. Sequence homologies indicate that the genome of the model plant Arabidopsis thaliana contains at least three open reading frames encoding presumptive Ap(4)A hydrolases: At1g30110, At3g10620, and At5g06340. In this work we present efficient overexpression and detailed biochemical characteristics of the AtNUDX25 protein encoded by the At1g30110 gene. Aided by the determination of the binding constants of Mn(Ap(4)A) and Mg(Ap(4)A) complexes using isothermal titration calorimetry (ITC) we show that AtNUDX25 preferentially hydrolyzes Ap(4)A in the form of a Mn(2+) complex.


2004 ◽  
Vol 31 (4) ◽  
pp. 346-353 ◽  
Author(s):  
K. G. Skryabin ◽  
D. V. Alekseev ◽  
T. A. Ezhova ◽  
V. N. Kozlov ◽  
V. B. Kudryavtsev ◽  
...  

1994 ◽  
Vol 13 (11) ◽  
Author(s):  
Thomas Altmann ◽  
Brigitte Damm ◽  
WolfB. Frommer ◽  
Thomas Martin ◽  
PeterC. Morris ◽  
...  

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