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Malate is acted on by malate dehydrogenase to become oxaloacetate, producing a molecule of NADH. After that, oxaloacetate will be recycled to aspartate, as transaminases prefer these keto acids over the others. This recycling maintains the flow of nitrogen into the cell. Relationship of oxaloacetic acid, malic acid, and aspartic acid
Malate, in the mitochondrial matrix, can be used to make pyruvate (catalyzed by malic enzyme) or oxaloacetic acid, both of which can enter the citric acid cycle. Glutamine can also be used to produce oxaloacetate during anaplerotic reactions in various cell types through "glutaminolysis", which is also seen in many c-Myc transformed cells. [ 3 ]
The amino acid sequences of archaeal MDH are more similar to that of LDH than that of MDH of other organisms. This indicates that there is a possible evolutionary linkage between lactate dehydrogenase and malate dehydrogenase. [8] Each subunit of the malate dehydrogenase dimer has two distinct domains that vary in structure and functionality.
In enzymology, a malate dehydrogenase (oxaloacetate-decarboxylating) (EC 1.1.1.38) is an enzyme that catalyzes the chemical reaction below (S)-malate + NAD + pyruvate + CO 2 + NADH. Thus, the two substrates of this enzyme are (S)-malate and NAD +, whereas its 3 products are pyruvate, CO 2, and NADH.
The reaction it catalyzes is: pyruvate + HCO − 3 + ATP → oxaloacetate + ADP + P. It is an important anaplerotic reaction that creates oxaloacetate from pyruvate. PC contains a biotin prosthetic group [1] and is typically localized to the mitochondria in eukaryotes with exceptions to some fungal species such as Aspergillus nidulans which have a cytosolic PC.
Malate is oxidized to pyruvate and CO 2, and NADP + is reduced to NADPH. This enzyme belongs to the family of oxidoreductases, to be specific those acting on the CH-OH group of donor with NAD + or NADP + as acceptor. The systematic name of this enzyme class is (S)-malate:NADP + oxidoreductase (oxaloacetate-decarboxylating).
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Oxaloacetic acid + Glutamate ⇌ α-Ketoglutarate + Aspartate (catalyzed by aspartate aminotransferase) When skeletal muscle is at rest (ADP<ATP), the aspartate is no longer needed for the purine nucleotide cycle and can therefore be used with α-ketoglutarate to produce glutamate and oxaloacetic acid (the above reaction reversed).