Topic
Transamination
About: Transamination is a research topic. Over the lifetime, 2396 publications have been published within this topic receiving 66185 citations. The topic is also known as: Transamination, aminotransfer & transamination.
Papers published on a yearly basis
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Papers
TL;DR: Current scientific interest in the Ehrlich pathway is supported by increased demands for natural flavor compounds such as isoamyl alcohol and 2-phenylethanol, which can be produced from amino acids in yeast-based bioconversion processes, as well as by the need to control flavor profiles of fermented food products.
Abstract: Saccharomyces cerevisiae has been used for at least eight millennia in the production of alcoholic beverages (41). Along with ethanol and carbon dioxide, fermenting cultures of this yeast produce many low-molecular-weight flavor compounds. These alcohols, aldehydes, organic acids, esters, organic sulfides, and carbonyl compounds have a strong impact on product quality. Indeed, the subtle aroma balance of these compounds in fermented foods and beverages is often used as an organoleptic fingerprint for specific products and brands (42). Food fermentation by yeast and lactic acid bacteria is accompanied by the formation of the aliphatic and aromatic alcohols known as fusel alcohols. Fusel oil, which derives its name from the German word fusel (bad liquor), is obtained during the distillation of spirits and is enriched with these higher alcohols. While fusel alcohols at high concentrations impart off-flavors, low concentrations of these compounds and their esters make an essential contribution to the flavors and aromas of fermented foods and beverages. Fusel alcohols are derived from amino acid catabolism via a pathway that was first proposed a century ago by Ehrlich (13). Amino acids represent the major source of the assimilable nitrogen in wort and grape must, and these amino acids are taken up by yeast in a sequential manner (23, 32). Amino acids that are assimilated by the Ehrlich pathway (valine, leucine, isoleucine, methionine, and phenylalanine) are taken up slowly throughout the fermentation time (32). After the initial transamination reaction (Fig. (Fig.1),1), the resulting α-keto acid cannot be redirected into central carbon metabolism. Before α-keto acids are excreted into the growth medium, yeast cells convert them into fusel alcohols or acids via the Ehrlich pathway.
FIG. 1.
The Ehrlich pathway. Catabolism of branched-chain amino acids (leucine, valine, and isoleucine), aromatic amino acids (phenylalanine, tyrosine, and trytophan), and the sulfur-containing amino acid (methionine) leads to the formation of fusel acids and ...
Current scientific interest in the Ehrlich pathway is supported by increased demands for natural flavor compounds such as isoamyl alcohol and 2-phenylethanol, which can be produced from amino acids in yeast-based bioconversion processes (14), as well as by the need to control flavor profiles of fermented food products. The goal of this paper is to present a concise centenary overview of the biochemistry, molecular biology, and physiology of this important pathway in S. cerevisiae.
1,396 citations
TL;DR: Cysteine, by virtue of its ability to form disulfide bonds, plays a crucial role in protein structure and in protein-folding pathways, and may be converted to such important products as glutathione and taurine.
Abstract: Methionine, cysteine, homocysteine, and taurine are the 4 common sulfur-containing amino acids, but only the first 2 are incorporated into proteins. Sulfur belongs to the same group in the periodic table as oxygen but is much less electronegative. This difference accounts for some of the distinctive properties of the sulfur-containing amino acids. Methionine is the initiating amino acid in the synthesis of virtually all eukaryotic proteins; N-formylmethionine serves the same function in prokaryotes. Within proteins, many of the methionine residues are buried in the hydrophobic core, but some, which are exposed, are susceptible to oxidative damage. Cysteine, by virtue of its ability to form disulfide bonds, plays a crucial role in protein structure and in protein-folding pathways. Methionine metabolism begins with its activation to S-adenosylmethionine. This is a cofactor of extraordinary versatility, playing roles in methyl group transfer, 5'-deoxyadenosyl group transfer, polyamine synthesis, ethylene synthesis in plants, and many others. In animals, the great bulk of S-adenosylmethionine is used in methylation reactions. S-Adenosylhomocysteine, which is a product of these methyltransferases, gives rise to homocysteine. Homocysteine may be remethylated to methionine or converted to cysteine by the transsulfuration pathway. Methionine may also be metabolized by a transamination pathway. This pathway, which is significant only at high methionine concentrations, produces a number of toxic endproducts. Cysteine may be converted to such important products as glutathione and taurine. Taurine is present in many tissues at higher concentrations than any of the other amino acids. It is an essential nutrient for cats.
1,094 citations
TL;DR: This report is the first complete description of the biosynthesis pathway of a complex cyanobacterial metabolite and represents an integrated polyketide-peptide biosynthetic pathway with a number of unusual structural and enzyme features.
1,016 citations
TL;DR: Several applications have been successfully developed, especially for intensifying or diversifying cheese flavour by controlling amino acid transamination and their importance in the formation of aroma compounds has been demonstrated by using isogenic strains lacking each enzyme.
740 citations
TL;DR: Data support the hypothesis that amino acids act as specific positive signals for maintenance of protein stores, while inhibiting other actions of insulin at multiple levels and indicate crosstalk between hormonal and nutritional signals.
Abstract: Amino acids have been shown to stimulate protein synthesis, inhibit proteolysis, and decrease whole-body and forearm glucose disposal. Using cultured hepatoma and myotube cells, we demonstrate that amino acids act as novel signaling elements in insulin target tissues. Exposure of cells to high physiologic concentrations of amino acids activates intermediates important in the initiation of protein synthesis, including p70 S6 kinase and PHAS-I, in synergy with insulin. This stimulatory effect is largely due to branched chain amino acids, particularly leucine, and can be reproduced by its transamination product, ketoisocaproic acid. Concurrently, amino acids inhibit early steps in insulin action critical for glucose transport and inhibition of gluconeogenesis, including decreased insulin-stimulated tyrosine phosphorylation of IRS-1 and IRS-2, decreased binding of grb 2 and the p85 subunit of phosphatidylinositol 3-kinase to IRS-1 and IRS-2, and a marked inhibition of insulin-stimulated phosphatidylinositol 3-kinase. Taken together, these data support the hypothesis that amino acids act as specific positive signals for maintenance of protein stores, while inhibiting other actions of insulin at multiple levels. This bidirectional modulation of insulin action indicates crosstalk between hormonal and nutritional signals and demonstrates a novel mechanism by which nutritional factors contribute to insulin resistance.
513 citations
Related Topics (5)
Performance Metrics
| Year | Papers |
|---|---|
| 2025 | 18 |
| 2024 | 33 |
| 2023 | 45 |
| 2022 | 55 |
| 2021 | 23 |
| 2020 | 46 |