Simultaneous determination of d-amino acids by the coupling method of d-amino acid oxidase with high-performance liquid chromatography

Kato, Shiro; Kito, Yukihiko; Hemmi, Hisashi; Yoshimura, Teizo

doi:10.1016/j.jchromb.2010.12.005

Cited by 22 publications

(10 citation statements)

References 24 publications

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“…L-Val originates exclusively from pyruvate, and 2-aminobutyrate is produced from 2-ketobutyrate; hence, we quantified the levels of intracellular keto acids, including pyruvate and 2-ketobutyrate, with the fluorescent labeling agent 1,2-diamino-4,5-methylenedioxybenzene as previously described (10). This experiment revealed that the log-phase ⌬yggS cells accumulated 2-ketobutyrate at a more than 6-fold higher level (5.0 pmol/mg) than the WT (0.8 pmol/mg) ( Table 2).…”

Section: Resultsmentioning

confidence: 99%

Conserved Pyridoxal Protein That Regulates Ile and Val Metabolism

et al. 2013

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Escherichia coli YggS is a member of the highly conserved uncharacterized protein family that binds pyridoxal 5=-phosphate (PLP). To assist with the functional assignment of the YggS family, in vivo and in vitro analyses were performed using a yggSdeficient E. coli strain (⌬yggS) and a purified form of YggS, respectively. In the stationary phase, the ⌬yggS strain exhibited a completely different intracellular pool of amino acids and produced a significant amount of L-Val in the culture medium. The log-phase ⌬yggS strain accumulated 2-ketobutyrate, its aminated compound 2-aminobutyrate, and, to a lesser extent, L-Val. It also exhibited a 1.3-to 2.6-fold increase in the levels of Ile and Val metabolic enzymes. The fact that similar phenotypes were induced in wild-type E. coli by the exogenous addition of 2-ketobutyrate and 2-aminobutyrate indicates that the 2 compounds contribute to the ⌬yggS phenotypes. We showed that the initial cause of the keto acid imbalance was the reduced availability of coenzyme A (CoA); supplementation with pantothenate, which is a CoA precursor, fully reversed phenotypes conferred by the yggS mutation. The plasmid-borne expression of YggS and orthologs from Bacillus subtilis, Saccharomyces cerevisiae, and humans fully rescued the ⌬yggS phenotypes. Expression of a mutant YggS lacking PLP-binding ability, however, did not reverse the ⌬yggS phenotypes. These results demonstrate for the first time that YggS controls Ile and Val metabolism by modulating 2-ketobutyrate and CoA availability. Its function depends on PLP, and it is highly conserved in a wide range species, from bacteria to humans.

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Section: Resultsmentioning

confidence: 99%

Conserved Pyridoxal Protein That Regulates Ile and Val Metabolism

et al. 2013

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“…To date, many studies employ high-performance liquid chromatography (HPLC) for determination of various kinds of d-amino acids. Kato et al reported an HPLC method combining d-amino acid oxidase (DAO) and 1,2-diamino-4,5-methylenedioxybenzene (DMB) [4]. In this method, d-amino acids were oxidized to their corresponding 2-oxo acids by DAO, and these 2-oxo acids were nonenzymatically reacted with DMB.…”

Section: Analytical Techniques Of D-amino Acidsmentioning

confidence: 99%

d-Amino Acids and Lactic Acid Bacteria

Kobayashi

2019

Microorganisms

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Proteins are composed of l-amino acids except for glycine, which bears no asymmetric carbon atom. Accordingly, researchers have studied the function and metabolism of l-amino acids in living organisms but have paid less attention to the presence and roles of their d-enantiomers. However, with the recent developments in analytical techniques, the presence of various d-amino acids in the cells of various organisms and the importance of their roles have been revealed. For example, d-serine (d-Ser) and d-aspartate (d-Asp) act as neurotransmitters and hormone-like substances, respectively, in humans, whereas some kinds of d-amino acids act as a biofilm disassembly factor in bacteria. Interestingly, lactic acid bacteria produce various kinds of d-amino acids during fermentation, and many d-amino acids taste sweet, compared with the corresponding l-enantiomers. The influence of d-amino acids on human health and beauty has been reported in recent years. These facts suggest that the d-amino acids produced by lactic acid bacteria are important in terms of the taste and function of lactic-acid-fermented foods. Against this background, unique d-amino-acid-metabolizing enzymes have been searched for and observed in lactic acid bacteria. This review summarizes and introduces the importance of various d-amino acids in this regard.Proteins are basically made up of 20 kinds of α-amino acids in the form of monomers, and these amino acids have at least one asymmetric carbon, except for glycine. This yields 19 kinds of amino acid (glycine has been excepted) with l-and d-form varieties. As proteins are made up of l-amino acids, many researchers, in fields such as medical, food, and nutritional science, have paid close attention to l-amino acids, giving rise to considerable knowledge of l-amino acids, including proteins. Until the 1970s, many researchers thought that d-amino acids were rare in nature and did not play an important role in living organisms. After that, however, d-alanine (d-Ala), d-glutamate (d-Glu), and d-aspartate (d-Asp) were found in bacterial cell walls as constituents, and d-amino acids were observed to exist in nature. This finding led to the conclusion that d-amino acids were only rarely present in bacterial cell walls, but in the 1990s, the development of analytical techniques, such as chiral column chromatography, meant that various kinds of d-amino acids were identified in free forms in diverse organisms. These d-amino acids were initially considered to be derived from foods or enterobacteria, but it is now known that some parts of d-amino acids such as d-serine (d-Ser) and d-Asp can be synthesized in mammalian cells. d-Amino acids have similar physical and chemical characteristics with l-amino acids, but the physiological functions of d-amino acids are completely different with those of l-amino acids. For example, d-Ser works as neurotransmitter in the brain, but l-Ser has no such role. Furthermore, d-amino acids are uncommon in living organisms, compared with l-amino acids, and despite the fact that some d-...

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“…Cardiac concentrations of BCKAs were analysed using HPLC . Briefly, ~ 30 mg pulverized frozen heart was homogenized in 180 μL of 0.8 m perchloric acid and then centrifuged at 18 000 g at 4 °C for 15 min to remove precipitated proteins.…”

Section: Methodsmentioning

confidence: 99%

mTORC1 is involved in the regulation of branched‐chain amino acid catabolism in mouse heart

et al. 2016

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The branched‐chain α‐ketoacid dehydrogenase ( BCKDH ) complex regulates branched‐chain amino acid ( BCAA ) catabolism by controlling the second step of this catabolic pathway. In the present study, we examined the in vivo effects of treatment with an mTORC 1 inhibitor, rapamycin, on cardiac BCKDH complex activity in mice. Oral administration of leucine in control mice significantly activated the cardiac BCKDH complex with an increase in cardiac concentrations of leucine and α‐ketoisocaproate. However, rapamycin treatment significantly suppressed the leucine‐induced activation of the complex despite similar increases in cardiac leucine and α‐ketoisocaproate levels. Rapamycin treatment fully inhibited mTORC 1 activity, measured by the phosphorylation state of ribosomal protein S6 kinase 1. These results suggest that mTORC 1 is involved in the regulation of cardiac BCAA catabolism.

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Simultaneous determination of d-amino acids by the coupling method of d-amino acid oxidase with high-performance liquid chromatography

Cited by 22 publications

References 24 publications

Conserved Pyridoxal Protein That Regulates Ile and Val Metabolism

Conserved Pyridoxal Protein That Regulates Ile and Val Metabolism

d-Amino Acids and Lactic Acid Bacteria

mTORC1 is involved in the regulation of branched‐chain amino acid catabolism in mouse heart

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