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Testicular Cancers - UCSF | Department of Medicine
Testicular Cancers - UCSF | Department of Medicine

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The Aerobic Fate of Pyruvate
The Aerobic Fate of Pyruvate

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Slide 1
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Problem Set 3 (Due February 4th) 1. In 1896, Christiaan Eijkman
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... Please read the attached paper and discuss how this E. coli enzyme is regulated and how this mechanism relates to the ‘dietary’ carbon source. E. coli Isocitrate Dehydrogenase (IDH) can be inhibited by the activity of another enzyme, IDH kinase/phosphorylase (gene aceK). This enzyme, which is part o ...
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Lactate dehydrogenase



A lactate dehydrogenase (LDH or LD) is an enzyme found in nearly all living cells (animals, plants, and prokaryotes). LDH catalyzes the conversion of pyruvate to lactate and back, as it converts NADH to NAD+ and back. A dehydrogenase is an enzyme that transfers a hydride from one molecule to another.LDH exist in four distinct enzyme classes. This article is about the common NAD(P)-dependent L-lactate dehydrogenase. Other LDHs act on D-lactate and/or are dependent on cytochrome c: D-lactate dehydrogenase (cytochrome)) and L-lactate (L-lactate dehydrogenase (cytochrome)). LDH has been of medical significance because it is found extensively in body tissues, such as blood cells and heart muscle. Because it is released during tissue damage, it is a marker of common injuries and disease such as heart failure.
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