Literature summary for 1.1.1.40 extracted from

Pinto, S.E.; Rao, S.R.; Bhagwat, A.S.
Inactivation of maize NADP-malic enzyme by Cu2+-ascorbate (2002), Indian J. Biochem. Biophys., 39, 55-59.

Search for more literature for 1.1.1.40

Inhibitors

Inhibitors	Comment	Organism	Structure
Cu2+-ascorbate	rapid inactivation by generation of reactive oxygen species at pH 5.0, Fe2+ can substitute for Cu2+, Cu2+ or ascorbate alone are not effective, azide, 1,4-diazabicyclo-(2.2.2.)octane, histidine and imidazole protect against inhibition, the substrates L-malate and NADP+ and EDTA protect almost completely, loss of activity is accompanied with cleavage of the protein into 4 fragments of 14-55 kDa	Zea mays
Fe2+-ascorbate	rapid inactivation	Zea mays
H2O2	83% inhibition at 0.25 mM, 91.1% inhibition at 0.5 mM	Zea mays

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	-	Zea mays

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
62000	-	4 * 62000, SDS-PAGE	Zea mays

Organism

Organism	UniProt	Comment	Textmining
Zea mays	-	-	-

Source Tissue

Source Tissue	Comment	Organism	Textmining
leaf	-	Zea mays	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
(S)-malate + NADP+	-	Zea mays	pyruvate + CO2 + NADPH	-	?

Subunits

Subunits	Comment	Organism
tetramer	4 * 62000, SDS-PAGE	Zea mays

Synonyms

Synonyms	Comment	Organism
NADP-malic enzyme	-	Zea mays

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
25	-	assay at	Zea mays

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
7.5	-	assay at	Zea mays

Cofactor

Cofactor	Comment	Organism	Structure
NADP+	-	Zea mays

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Release 2023.1 (January 2023)