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• W1578703670 abstract "The metabolic regulation of Neurospora crass cytoplasmic malate dehydrogenase (l-malate:NAD oxidoreductase, EC 1.1.1.37) is described. Synthesis of the cytoplasmic isozyme is subject to glucose repression whereas the mitochondrial forms are constitutive. Mycelia upon transfer from glucose to acetate as sole carbon source differentially synthesize cytoplasmic malate dehydrogenase, other enzymes of the glyoxylate cycle, and cytoplasmic aspartate aminotransferase (l-aspartate:2-oxoglutarate aminotransferase, EC 2.6.1.1). The kinetics of cytoplasmic malate dehydrogenase synthesis indicate that the apparent increase in activity is 7-fold above the basal level of mitochondrial malate dehydrogenase activity and the absolute increase is several hundred-fold; maximal derepression occurs at the onset of growth on acetate; glucose repression after maximal derepression is not a rapid process; inhibition of derepression by antibiotics indicates that the isozymes are synthesized by cytoplasmic and not mitochondrial ribosomes; mineral starvation does not release glucose repression of either cytoplasmic malate dehydrogenase or aspartate aminotransferase but leads to gross cytological abnormalities. A purification procedure for the cytoplasmic and mitochondrial isozymes is described. The enzymes are demonstrated to differ in stability, ethanol solubility, isoelectric point, kinetics with substrate inhibition, coenzyme and substrate analogs, and inhibition by either low-molecular-weight compounds, antiserum, or mitochondrial structural protein. Differential association of the two isozymes of Neurospora and porcine heart with homologous structural protein is described." @default.
• W1578703670 created "2016-06-24" @default.
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• W1578703670 date "1970-11-01" @default.
• W1578703670 modified "2023-10-16" @default.
• W1578703670 title "Cytoplasmic and mitochondrial malate dehydrogenases of Neurospora" @default.
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• W1578703670 doi "https://doi.org/10.1016/0005-2744(70)90003-3" @default.
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