Amino Acid Metabolism

Proteins exert essential functions in biology, from structural roles, secreted signaling molecules, ion channels, transport, or catalysts of biochemical reactions (enzymes). The unique characteristics of a protein are dictated by its linear sequence of amino acids, termed its primary structure. This...

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Main Authors: Newsholme, Philip, Stenson, L., Sulvucci, M., Sumayao, R., Krause, M.
Other Authors: Murray Moo-Young
Format: Book Chapter
Published: Elsevier 2011
Online Access:http://hdl.handle.net/20.500.11937/22807
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author Newsholme, Philip
Stenson, L.
Sulvucci, M.
Sumayao, R.
Krause, M.
author2 Murray Moo-Young
author_facet Murray Moo-Young
Newsholme, Philip
Stenson, L.
Sulvucci, M.
Sumayao, R.
Krause, M.
author_sort Newsholme, Philip
building Curtin Institutional Repository
collection Online Access
description Proteins exert essential functions in biology, from structural roles, secreted signaling molecules, ion channels, transport, or catalysts of biochemical reactions (enzymes). The unique characteristics of a protein are dictated by its linear sequence of amino acids, termed its primary structure. This sequence can determine the final conformation of a protein and also its interactions with other proteins or molecules to exert their function inside and outside the cells. It is generally accepted that only 20 proteinogenic amino acids are included in the genetic code and therefore regularly found in proteins. However, it is now accepted that a 21st amino acid, selenocyteine, exists in mammalian proteins. Hence, every mammalian protein is constructed from a set of 21 amino acids [4]. Beyond their importance for the synthesis of proteins, amino acids can also be fully or partially oxidized in order to produce energy or to be converted into other compounds such as glucose, fatty acids, ketone bodies, and purine and pyrimidine bases (used for nucleotide synthesis from which RNA and DNA are formed). In this article, we describe the structure, the characteristics, and the metabolism of the key amino acids, and also discuss the importance of their availability in health and disease conditions.
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spelling curtin-20.500.11937-228072023-01-27T05:26:32Z Amino Acid Metabolism Newsholme, Philip Stenson, L. Sulvucci, M. Sumayao, R. Krause, M. Murray Moo-Young Michael Butler Colin Webb Antonio Moreira Bernard Grodzinski Z F Cui Spiros Agathos Proteins exert essential functions in biology, from structural roles, secreted signaling molecules, ion channels, transport, or catalysts of biochemical reactions (enzymes). The unique characteristics of a protein are dictated by its linear sequence of amino acids, termed its primary structure. This sequence can determine the final conformation of a protein and also its interactions with other proteins or molecules to exert their function inside and outside the cells. It is generally accepted that only 20 proteinogenic amino acids are included in the genetic code and therefore regularly found in proteins. However, it is now accepted that a 21st amino acid, selenocyteine, exists in mammalian proteins. Hence, every mammalian protein is constructed from a set of 21 amino acids [4]. Beyond their importance for the synthesis of proteins, amino acids can also be fully or partially oxidized in order to produce energy or to be converted into other compounds such as glucose, fatty acids, ketone bodies, and purine and pyrimidine bases (used for nucleotide synthesis from which RNA and DNA are formed). In this article, we describe the structure, the characteristics, and the metabolism of the key amino acids, and also discuss the importance of their availability in health and disease conditions. 2011 Book Chapter http://hdl.handle.net/20.500.11937/22807 Elsevier restricted
spellingShingle Newsholme, Philip
Stenson, L.
Sulvucci, M.
Sumayao, R.
Krause, M.
Amino Acid Metabolism
title Amino Acid Metabolism
title_full Amino Acid Metabolism
title_fullStr Amino Acid Metabolism
title_full_unstemmed Amino Acid Metabolism
title_short Amino Acid Metabolism
title_sort amino acid metabolism
url http://hdl.handle.net/20.500.11937/22807