BCAA aminotransferase

Bacteria, gut micToflora, 142, 143, 147-150 Bactemdes, 14 , 149 Banana, starch content, 139 BarorEceptor , 712 Basal level of transcription, 5 5 Basal metabolic rate (BMR), 302, 735-736 BCAA aminotransferase, 209, 430,433,434, 343... 

The activity of BCAA aminotransferase is low in liver and relatively high in skeletal muscle. The opposite is true of the activity of BCKA dehydrogenase. This difference in enzyme activity is most likely the cause of the small extraction of BCAA by the liver. The majority of BCAA is taken up by skeletal muscles and converted to their respective branched-chain keto acids, which are partly consumed in the muscle cells. The remainder of BCKA is released into the blood. Part of the circulating BCKA is extracted by the liver. Inside the hepatocytes, BCKA is either degraded in the oxidative metabolic pathway or reaminated to preserve the total body content of BCAA (Harper et al., 1984). 

BCAA catabolism, 209 chemical structure, 18 plasma concentrahon, 465 waste nitrogen and, 209-210 Alanine aminotransferase, 426 Alanine cycle, amino transferases and, 427-428... 

Although the enzyme that catalyzes this reaction, alanine aminotransferase, has cytoplasmic and mitochondrial forms, the majority of its activity has been found in the cytoplasm. Recall that the alanine cycle (Chapter 8) contributes to the maintenance of blood glucose. BCAA are the ultimate source of many of the amino groups transferred from glutamate in the alanine cycle (Figure 8.9). 

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