Partial purification and characterization of dihydrodipicolinic Acid reductase from maize |
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Authors: | Tyagi V V Henke R R Farkas W R |
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Affiliation: | Botany Department, University of Tennessee, Knoxville, Tennessee 37996-1100. |
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Abstract: | Dihydrodipicolinic acid reductase, an enzyme which catalyzes the pyridine nucleotide-linked reduction of dihydrodipicolinic acid to tetrahydrodipicolinic acid in the biosynthetic pathway leading to l-lysine, has been partially purified from maize (Zea mays cv Pioneer 3145) kernels. The crude maize extract and the partially purified enzyme were assayed for dihydrodipicolinic acid reductase by their ability to restore the capability of crude extracts of a mutant Escherichia coli (CGSC 4549; defective in dihydrodipicolinic acid reductase) to synthesize diaminopimelic acid from aspartic acid and pyruvic acid. |
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