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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