
TY  - JOUR
A1  - Gallais, Stéphane 
A1  - Crescenzo, Marie-Anne Pou de 
A1  - Laval-Martin, Danielle L. 
T1  - Characterization of soluble calcium calmodulin-dependent and -independent NAD<emph type="7">+</emph> kinases from <emph type="2">Avena sativa</emph> seeds
JF  - Functional Plant Biology
JO  - Functional Plant Biol.
Y1  - 2001
VL  - 28
IS  - 5
SP  - 363
EP  - 371
KW  - Avena sativa, calmodulin, dormancy, NAD+ kinase.
UR  - https://doi.org/10.1071/PP00080 
N2  - Two NAD+ kinase isoforms were separated from Avena sativa L. embryo extracts from dormant and after-ripened seeds by size-exclusion chromatography: a 410-kDa Ca2+&#8211;calmodulin (CaCam)-independent NAD+ kinase was observed in both dormant and after-ripened seeds and a 63-kDa CaCam-dependent isoform was found to be abundant only in embryos of after-ripened Avena seeds. The characterization of these two isoforms showed differences in Michaelis&#8211;Menten constant (Km) values and enzymatic mechanisms, as well as distinct sensitivities to inhibitors, oxidants, reductants and CaCam inhibitors. It is therefore proposed that the 410-kDa isoform could be a &#8216;housekeeping&#8217; enzyme with Km values corresponding to the intracellular concentrations of ATPMg and NAD+. We speculate that the 63-kDa CaCam-dependent NAD+ kinase, possessing a low Km, would be mainly involved in the adaptation and response of A. sativa to environmental signals or stresses through changes of redox potential and/or calcium signalling pathways. 
ER  -

