Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.1.1.82 extracted from

  • Scheibe, R.; Fickenscher, K.
    The dark (oxidized) form of the light-activatable NADP-malate dehydrogenase from pea chloroplasts is catalytically active in the presence of guanidine-HCl (1985), FEBS Lett., 180, 317-320.
No PubMed abstract available

Activating Compound

Activating Compound Comment Organism Structure
guanidine can activate oxidized enzyme Pisum sativum

Inhibitors

Inhibitors Comment Organism Structure
HgCl2 activity of the oxidized enzyme in presence of guanidine is unaffected by 0.1 mM HgCl2 in presence of 1 mM EDTA and by 0.005 mM HgCl2 in absence of EDTA, activity of the reduced form of enzyme is completely abolished Pisum sativum
NEM 1 mM, activity of the oxidized enzyme in presence of guanidine is unaffected, activity of the reduced form of enzyme is completely abolished Pisum sativum

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.039
-
NADPH reduced native enzyme Pisum sativum
0.048
-
oxaloacetate reduced native enzyme Pisum sativum
0.077
-
oxaloacetate reduced enzyme, + 200 mM guanidine Pisum sativum
0.095
-
NADPH reduced enzyme, + 200 mM guanidine Pisum sativum
0.22
-
NADPH oxidized enzyme, + 250 mM guanidine Pisum sativum
0.32
-
oxaloacetate oxidized enzyme, + 250 mM guanidine Pisum sativum

Organism

Organism UniProt Comment Textmining
Pisum sativum
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
leaf
-
Pisum sativum
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
oxaloacetate + NADPH
-
Pisum sativum (S)-malate + NADP+
-
?

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
guanidine-activated oxidized enzyme and reduced enzyme Pisum sativum