Literature summary for 1.1.1.40 extracted from
Pinto, S.E.; Misra, H.S.; Rao, S.R.; Andreo, C.S.; Bhagwat, A.S.
Site directed mutagenesis studies to demonstrate the involvement of carboxyl triates located at the active site of NADP-malic enzyme in metal binding and reaction catalysis (2005), Physiol. Mol. Biol. Plants, 11, 219-224.
No PubMed abstract available
Cloned(Commentary)
Cloned (Comment) |
Organism |
expression in Escherichia coli |
Zea mays |
Metals/Ions
Metals/Ions |
Comment |
Organism |
Structure |
Mg2+ |
required. Important role of Asp-351, Asp-350 and Glu-327 in the binding of Mg2+ and NADP+ |
Zea mays |
|
Organism
Organism |
UniProt |
Comment |
Textmining |
Zea mays |
- |
- |
- |
Synonyms
Synonyms |
Comment |
Organism |
NADP-malic enzyme |
- |
Zea mays |
Cofactor
Cofactor |
Comment |
Organism |
Structure |
NADP+ |
important role of Asp-351, Asp-350 and Glu-327 in the binding of Mg2+ and NADP+ |
Zea mays |
|