Literature summary extracted from
Gomez, I.; Merchan, F.; Fernandez, E.; Quesada, A.
NADP-malate dehydrogenase from Chlamydomonas: prediction of new structural determinants for redox regulation by homology modelling (2002), Plant Mol. Biol., 48, 211-221.
Activating Compound
EC Number |
Activating Compound |
Comment |
Organism |
Structure |
---|
1.1.1.82 |
DTT |
activates enzyme in free extracts |
Chlamydomonas reinhardtii |
|
1.1.1.82 |
additional information |
the enzyme is active in the light |
Chlamydomonas reinhardtii |
|
Cloned(Commentary)
EC Number |
Cloned (Comment) |
Organism |
---|
1.1.1.82 |
- |
Chlamydomonas reinhardtii |
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
1.1.1.82 |
Chlamydomonas reinhardtii |
Q9FNS5 |
- |
- |
Reaction
EC Number |
Reaction |
Comment |
Organism |
Reaction ID |
---|
1.1.1.82 |
(S)-malate + NADP+ = oxaloacetate + NADPH + H+ |
The enzyme is highly conserved with plant counterparts, but bearing differences at regulatory determinants with a critical role for redox control of protein activity |
Chlamydomonas reinhardtii |
|
Subunits
EC Number |
Subunits |
Comment |
Organism |
---|
1.1.1.82 |
More |
homology-based 3D modelling of enzyme evidences close positioning of two new disulfide bridges in an accessible region of the protein surface |
Chlamydomonas reinhardtii |