Identification of the Residues Involved in Light-Activation and Catalytic Activity of NADP-Malate Dehydrogenase

1995 ◽  
pp. 3927-3932
Author(s):  
M. Miginiac-Maslow ◽  
E. Issakidis ◽  
M. Lemaire ◽  
P. Decottignies ◽  
M. Saarinen ◽  
...  
Keyword(s):  
Catalytic Activity ◽  
Malate Dehydrogenase ◽  
Light Activation

Light-activation of NADP-malate dehydrogenase: A highly controlled process for an optimized function

2000 ◽  
Vol 110 (3) ◽  
pp. 322-329 ◽  
Author(s):  
M. Miginiac-Maslow ◽  
K. Johansson ◽  
E. Ruelland ◽  
E. Issakidis-Bourguet ◽  
I. Schepens ◽  
...  
Keyword(s):  
Malate Dehydrogenase ◽  
Light Activation

Regulation of NADP-Malate Dehydrogenase Light-Activation by the Reducing Power. I Functional Studies

1990 ◽  
pp. 3037-3040
Author(s):  
M. Miginiac-Maslow ◽  
P. Decottignies ◽  
J.-P. Jacquot ◽  
P. Gadal
Keyword(s):  
Malate Dehydrogenase ◽  
Reducing Power ◽  
Light Activation ◽  
Functional Studies

Light-activation of NADP-malate dehydrogenase: A highly controlled process for an optimized function

2008 ◽  
Vol 110 (3) ◽  
pp. 322-329 ◽  
Author(s):  
M. Miginiac-Maslow ◽  
K. Johansson ◽  
E. Ruelland ◽  
E. Issakidis-Bourguet ◽  
I. Schepens ◽  
...  
Keyword(s):  
Malate Dehydrogenase ◽  
Light Activation

Interactions of 2-furylethylenes with thiol enzymes

1983 ◽  
Vol 48 (1) ◽  
pp. 327-335 ◽  
Author(s):  
Ernest Šturdík ◽  
Ľudovít Drobnica ◽  
Štefan Baláž
Keyword(s):  
Catalytic Activity ◽  
Chemical Modification ◽  
Glutathione Reductase ◽  
Malate Dehydrogenase ◽  
Cysteine Residues ◽  
Sh Groups ◽  
Inhibition Constants ◽  
Glucose 6 Phosphate Dehydrogenase

Furylethylenes are inhibitors of glyceraldehyde 3-phosphate dehydrogenase (GAPDH; EC 1.2.1.12), glucose 6-phosphate dehydrogenase (EC 1.1.1.49), glutathione reductase (GR; EC 1.6.4.2), and, in part, also malate dehydrogenase (EC 1.1.1.37). These four enzymes served as model thiolproteins employing the SH groups of the embodied cysteine for catalytic activity. The inhibition degree of the afore-mentioned enzymes is proportional to the reactivity of furylethylenes towards thiols. The inhibition of GAPDH and GR with 1-(5-nitro-2-furyl)-2-nitro-2-methoxycarbonylethylene (I) was characterized by inhibition constants Ki and also, its type was estimated. A direct chemical modification of SH groups of cysteine residues was found in GAPDH, a fact that could be closely connected with the inactivation of the enzyme.

NADP regulates the light activation of NADP-dependent malate dehydrogenase

Planta ◽  
1983 ◽  
Vol 157 (6) ◽  
pp. 548-553 ◽  
Author(s):  
R. Scheibe ◽  
J. -P. Jacquot
Keyword(s):  
Malate Dehydrogenase ◽  
Light Activation

Regulation of NADP-Malate Dehydrogenase Light-Activation by the Reducing Power: II. Structural Studies

1990 ◽  
pp. 3041-3044
Author(s):  
P. Decottignies ◽  
J.-M. Schmitter ◽  
M. Miginiac-Maslow ◽  
P. Le Maréchal ◽  
J.-P. Jacquot ◽  
...  
Keyword(s):  
Malate Dehydrogenase ◽  
Reducing Power ◽  
Structural Studies ◽  
Light Activation

scholarly journals Light Activation of NADP-Malate Dehydrogenase in Guard Cell Protoplasts from Vicia faba L.

1985 ◽  
Vol 79 (3) ◽  
pp. 829-832 ◽  
Author(s):  
Kiyoshi Gotow ◽  
Kiyoshi Tanaka ◽  
Noriaki Kondo ◽  
Koh Kobayashi ◽  
Kunihiko Syōno
Keyword(s):  
Vicia Faba ◽  
Malate Dehydrogenase ◽  
Guard Cell ◽  
Light Activation ◽  
Vicia Faba L ◽  
Guard Cell Protoplasts

Light activation of nadp malate dehydrogenase in a reconstituted chloroplastic system

1980 ◽  
Vol 19 (9) ◽  
pp. 1919-1924 ◽  
Author(s):  
Jean Vidal ◽  
Jean Pierre Jacquot ◽  
Pierre Gadal
Keyword(s):  
Malate Dehydrogenase ◽  
Light Activation
Sign in / Sign up

Export Citation Format

Share Document