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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
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.
Oxaloacetate decarboxylase is a carboxy-lyase involved in the conversion of oxaloacetate into pyruvate.. It is categorized under EC 4.1.1.3.. Oxaloacetate decarboxylase activity in a given organism may be due to activity of malic enzyme, pyruvate kinase, malate dehydrogenase, pyruvate carboxylase and PEP carboxykinase or the activity of "real" oxaloacetate decarboxylases.
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 ]
In enzymology, a malate oxidase (EC 1.1.3.3) is an enzyme that catalyzes the chemical reaction (S)-malate + O 2 oxaloacetate + H 2 O 2. Thus, the two substrates of this enzyme are (S)-malate and O 2, whereas its two products are oxaloacetate and H 2 O 2.
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Phosphoenolpyruvate carboxylase (also known as PEP carboxylase, PEPCase, or PEPC; EC 4.1.1.31, PDB ID: 3ZGE) is an enzyme in the family of carboxy-lyases found in plants and some bacteria that catalyzes the addition of bicarbonate (HCO 3 −) to phosphoenolpyruvate (PEP) to form the four-carbon compound oxaloacetate and inorganic phosphate: [1]
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