Deamination and transamination

Deamination examples

The amino acid threonine has its amino group removed by threonine dehydratase (1p209). This particular amino acid is commonly deaminated along with glutamate, histidine, serine and glycine (1p209). In the case of thronine, the reaction proceeds with loss of water, which is why the enzyme catalyzing the reaction is called a dehydratase instead of a deaminase (1p209). Vitamin B6 is important for this reaction to occur (1p209). The amino group is used by periportal hepatocytes to synthesize urea (1p209).

Transamination examples

The transfer of an amino groupf from one amino acid to an amino acid carbon skeleton or alpha-keto acid occurs to feed protein synthesis (1p209). The enzymes include tyrosine aminotransferase, branched-chain aminotransferases, alanine aminotransferase, and aspartate aminotransferase (1p209). The enzymes can often require vitamin B6 in a coenzyme form (1p209). The reactions are reversible and are often used to create non-essential amino acids from essential ones except lysine, histidiene and threonine (1p209).

Reference List

1. Gropper SS, Smith JL, Groff JL. Advanced Nutrition and Human Metabolism. Belmont, CA: Thomson Wadsworth, 2009.

Published by David Despain, MS, CFS

David is a science and health writer living on Long Island, New York. He's written for a variety of publications including Scientific American, Outside Online, the American Society for Nutrition's (ASN) Nutrition Notes Daily, and Institute of Food Technologists' (IFT) Food Technology magazine and Live! blog. He's also covered new findings reported at scientific meetings including Experimental Biology, AAAS, AOCS, CASW, Sigma Xi, IFT, and others on his personal blog "Evolving Health." David is also an active member of organizations including the National Association of Science Writers (NASW), the American Association for the Advancement of Science (AAAS), the American Society for Nutrition, the Institute of Food Technologists, and the National Audubon Society. David has a master's degree in human nutrition from the University of Bridgeport, and a bachelor's degree in English from University of Illinois at Springfield. He also earned his Certified Food Scientist credential from the Institute of Food Technologists.

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