Kinetic mechanism of NADP-malic enzyme from maize leaves View Full Text


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Article Info

DATE

1995-01

AUTHORS

Claudia P. Spampinato, Carlos S. Andreo

ABSTRACT

The kinetic mechanism of NADP-dependent malic enzyme purified from maize leaves was studied in the physiological direction. Product inhibition and substrate analogues studies with 3′ aminopyridine dinucleotide phosphate and tartrate indicate that the enzyme reaction follows a sequential ordered Bi-Ter kinetic mechanism. NADP is the leading substrate followed by l-malate and the products are released in the order of CO2, pyruvate and NADPH. The enzyme also catalyzes a slow, magnesium-dependent decarboxylation of oxaloacetate and reduction of pyruvate and oxaloacetate in the presence of NADPH to produce l-lactate and l-malate, respectively. More... »

PAGES

1-9

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/bf00029456

DOI

http://dx.doi.org/10.1007/bf00029456

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1037889370

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/24306633


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