scholarly journals The Interactions between Bisulfite and Amino Acids. The Formation of Methionine Sulfoxide from Methionine in the Presence of Oxygen

1971 ◽  
Vol 19 (6) ◽  
pp. 1286-1289 ◽  
Author(s):  
MASAO INOUE ◽  
HIKOYA HAYATSU
Keyword(s):  
Amino Acids ◽  
Methionine Sulfoxide

Des acides aminés stimulateurs et inhibiteurs à la croissance de Corynebacterium sepedonicum (Spieck. et Kott., Skapt. et Burkh.) dans des milieux synthétiques

1978 ◽  
Vol 24 (9) ◽  
pp. 1087-1092
Author(s):  
G. J. Ikin ◽  
H. J. Hope ◽  
R. A. Lachance
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Ammonium Phosphate ◽  
Methionine Sulfoxide ◽  
High Rate ◽  
Molar Ratio ◽  
Corynebacterium Sepedonicum ◽  
Ring Rot ◽  
Acides Aminés ◽  
Synthetic Media

Some aspects of the growth and amino acid metabolism of Corynebacterium sepedonicum, the organism responsible for potato ring rot, have been studied in synthetic media. It has been demonstrated that organic sulfur is required for growth. Methionine supports growth and can be replaced by methionine sulfoxide and cystathionine. Methionine is a micrometabolite for this species as indicated by the fact that optimum growth can be obtained in an asparagines–methionine (asn-met) containing medium when the molar ratio of these amino acids is 56:1. Increasing the proportion of methionine does not increase the growth. Both asparagine and glutamine are metabolized very quickly and provide for equivalent rapid growth unlike aspartic and glutamic acids. In the case of the last two amino acids, growth can be increased if dibasic ammonium phosphate is added to the medium although this compound alone will not support growth in the culture medium. The intracellular soluble asparagine level is extremely low in cells from the asn-met medium indicating a high rate of metabolism compared to aspartic acid. Cystine and cysteine were found to be inhibitory to the organism: they do not affect the rate of uptake of asn or met but do alter the organism's metabolism as reflected by changes in the free amino acid pool. The concentrations of cystine and cysteine required for measurable inhibition are much higher than those found in soluble amino acids of potato tubers.

scholarly journals Kinetic Modeling of Storage Effects on Biomarkers Related to B Vitamin Status and One-Carbon Metabolism

2012 ◽  
Vol 58 (2) ◽  
pp. 402-410 ◽  
Author(s):  
Steinar Hustad ◽  
Simone Eussen ◽  
Øivind Midttun ◽  
Arve Ulvik ◽  
Puck M van de Kant ◽  
...  
Keyword(s):  
Amino Acids ◽  
Carbon Metabolism ◽  
Room Temperature ◽  
Nonlinear Models ◽  
Methionine Sulfoxide ◽  
Flavin Mononucleotide ◽  
Storage Effects ◽  
One Carbon Metabolism ◽  
Accumulation Kinetics ◽  
B Vitamin

Abstract BACKGROUND Biomarkers and metabolites related to B vitamin function and one-carbon metabolism have been studied as predictors of chronic diseases in studies based on samples stored in biobanks. For most biomarkers, stability data are lacking or fragmentary. METHODS Degradation and accumulation kinetics of 32 biomarkers were determined at 23 °C in serum and plasma (EDTA, heparin, and citrate) collected from 16 individuals and stored for up to 8 days. In frozen serum (−25 °C), stability was studied cross-sectionally in 650 archival samples stored for up to 29 years. Concentration vs time curves were fitted to monoexponential, biexponential, linear, and nonlinear models. RESULTS For many biomarkers, stability was highest in EDTA plasma. Storage effects were similar at room temperature and at −25 °C; notable exceptions were methionine, which could be recovered as methionine sulfoxide, and cystathionine, which decreased in frozen samples. Cobalamin, betaine, dimethylglycine, sarcosine, total homocysteine, total cysteine, tryptophan, asymetric and symmetric dimethyl argenine, creatinine, and methylmalonic acid were essentially stable under all conditions. Most B vitamins (folate and vitamins B2 and B6) were unstable; choline increased markedly, and some amino acids also increased, particularly in serum. The kynurenines showed variable stability. For many biomarkers, degradation (folate and flavin mononucleotide) or accumulation (pyridoxal, riboflavin, choline, amino acids) kinetics at room temperature were non–first order. CONCLUSIONS Data on stability and deterioration kinetics for individual biomarkers are required to optimize procedures for handling serum and plasma, and for addressing preanalytical bias in epidemiological and clinical studies.

Reduction of methionine sulfoxide with : Compatibility with peptides containing cysteine and aromatic amino acids

Tetrahedron ◽  
1998 ◽  
Vol 54 (50) ◽  
pp. 15273-15286 ◽  
Author(s):  
Marta Vilaseca ◽  
Ernesto Nicolás ◽  
Fina Capdevila ◽  
Ernest Giralt
Keyword(s):  
Amino Acids ◽  
Aromatic Amino Acids ◽  
Methionine Sulfoxide

scholarly journals STUDIES ON THE NATURE OF RESISTANCE OF GRAM-NEGATIVE BACILLI TO PENICILLIN

1946 ◽  
Vol 83 (1) ◽  
pp. 65-88 ◽  
Author(s):  
Gregory Shwartzman
Keyword(s):  
Amino Acids ◽  
Casein Hydrolysate ◽  
Basal Medium ◽  
Quantitative Relationship ◽  
Methionine Sulfoxide ◽  
Amino Acid Mixture ◽  
Acid Mixture ◽  
Mixed Composition ◽  
Gram Negative ◽  
E Coli

The susceptibility of E. coli and Salmonella to penicillin is highest in a basal medium devoid of amino acids. Blood serum in certain concentrations, meat infusion broth, yeast extract, and casein hydrolysate interfere with the penicillin activity. The effect is apparently due to the antagonism of certain amino acids in the materials. Dicarboxyl-monoamino acids (i.e. aspartic, glutamic, and hydroxyglutamic acids and asparagine) cystine, arginine, histidine, and hydroxyproline are capable of suppressing the effect of penicilhn upon Gram-negative organisms. The antagonism of amino acids is not primarily related to their effect upon the rate of bacterial growth. It is suggested from the experiments detailed, that the antipenicillin activity is due to the effect of the amino acids upon bacterial metabolism. Prepassages in media of various concentrations of antagonistic amino acids alter the resistance of E. coli to penicillin. The changes are in inverse relation to the concentration of the antagonists. The antipenicillin activity of amino acids may be reversed significantly by dl-methionine. The substance, however, reverses only incompletely the antagonism of materials of mixed composition; i.e., casein hydrolysate, meat infusion broth, and serum. Upon addition of methionine, methionine sulfoxide, and threonine, there occurs a marked enhancement of penicillin susceptibility of broth cultures of Brucella, Eberthella, Salmonella, and Shigella. The enhancement is apparently due to the ability of this amino acid mixture to reverse effectively the action of the antagonists present in the cultures. Methionine is essential for the enhancement of penicillin susceptibility. Threonine and methionine sulfoxide facilitate the effect of methionine following a reciprocal quantitative relationship.

scholarly journals Evidence for the Formation of Ozone (or Ozone-Like Oxidants) by the Reaction of Singlet Oxygen with Amino Acids

2018 ◽  
Vol 2018 ◽  
pp. 1-6 ◽  
Author(s):  
George W. Wanjala ◽  
Arnold N. Onyango ◽  
David Abuga ◽  
Calvin Onyango ◽  
Moses Makayoto
Keyword(s):  
Amino Acids ◽  
Hydrogen Peroxide ◽  
Amino Acid ◽  
Singlet Oxygen ◽  
Oxidation Product ◽  
Alternative Hypothesis ◽  
Methionine Sulfoxide ◽  
Amino Acid Derivatives ◽  
Water Molecules ◽  
Ozone Formation

Antibodies or some amino acids, namely, cysteine, methionine, histidine, and tryptophan, were previously reported to catalyse the conversion of singlet oxygen (1O2) to ozone (O3). The originally proposed mechanism for such biological ozone formation was that antibodies or amino acids catalyse the oxidation of water molecules by singlet oxygen to yield dihydrogen trioxide (HOOOH) as a precursor of ozone and hydrogen peroxide (H2O2). However, because HOOOH readily decomposes to form water and singlet oxygen rather than ozone and hydrogen peroxide, an alternative hypothesis has been proposed; ozone is formed due to the reaction of singlet oxygen with amino acids to form polyoxidic amino acid derivatives as ozone precursors. Evidence in support of the latter hypothesis is presented in this article, in that in the presence of singlet oxygen, methionine sulfoxide (RS(O)CH3), an oxidation product of methionine (RSCH3), was found to promote reactions that can best be attributed to the trioxidic anionic derivative RS+(OOO−)CH3 or ozone.

scholarly journals Characterization of Bacillus thuringiensis l-Isoleucine Dioxygenase for Production of Useful Amino Acids

2011 ◽  
Vol 77 (19) ◽  
pp. 6926-6930 ◽  
Author(s):  
Makoto Hibi ◽  
Takashi Kawashima ◽  
Tomohiro Kodera ◽  
Sergey V. Smirnov ◽  
Pavel M. Sokolov ◽  
...  
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Bacillus Thuringiensis ◽  
Methionine Sulfoxide ◽  
Oxidation Reactions ◽  
Content Type ◽  
Enzymatic Characteristics ◽  
Different Types ◽  
Sulfur Containing

ABSTRACTWe determined the enzymatic characteristics of an industrially important biocatalyst, α-ketoglutarate-dependentl-isoleucine dioxygenase (IDO), which was found to be the enzyme responsible for the generation of (2S,3R,4S)-4-hydroxyisoleucine inBacillus thuringiensis2e2. Depending on the amino acid used as the substrate, IDO catalyzed three different types of oxidation reactions: hydroxylation, dehydrogenation, and sulfoxidation. IDO stereoselectively hydroxylated several hydrophobic aliphaticl-amino acids, as well asl-isoleucine, and produced (S)-3-hydroxy-l-allo-isoleucine, 4-hydroxy-l-leucine, (S)-4-hydroxy-l-norvaline, 4-hydroxy-l-norleucine, and 5-hydroxy-l-norleucine. The IDO reaction product ofl-isoleucine, (2S,3R,4S)-4-hydroxyisoleucine, was again reacted with IDO and dehydrogenated into (2S,3R)-2-amino-3-methyl-4-ketopentanoate, which is also a metabolite found inB. thuringiensis2e2. Interestingly, IDO catalyzed the sulfoxidation of some sulfur-containingl-amino acids and generatedl-methionine sulfoxide andl-ethionine sulfoxide. Consequently, the effective production of various modified amino acids would be possible using IDO as the biocatalyst.

Homochirality as the Signature of Extra-Terrestrial Life

1997 ◽  
Vol 161 ◽  
pp. 505-510
Author(s):  
Alexandra J. MacDermott ◽  
Laurence D. Barron ◽  
Andrè Brack ◽  
Thomas Buhse ◽  
John R. Cronin ◽  
...  
Keyword(s):  
Amino Acids ◽  
Protein Synthesis ◽  
Optical Rotation ◽  
Physical Origin ◽  
Natural Choice ◽  
Rosetta Mission ◽  
Terrestrial Life ◽  
Subsurface Layers ◽  
Solar System Bodies ◽  
Origin Of Homochirality

AbstractThe most characteristic hallmark of life is its homochirality: all biomolecules are usually of one hand, e.g. on Earth life uses only L-amino acids for protein synthesis and not their D mirror images. We therefore suggest that a search for extra-terrestrial life can be approached as a Search for Extra- Terrestrial Homochirality (SETH). The natural choice for a SETH instrument is optical rotation, and we describe a novel miniaturized space polarimeter, called the SETH Cigar, which could be used to detect optical rotation as the homochiral signature of life on other planets. Moving parts are avoided by replacing the normal rotating polarizer by multiple fixed polarizers at different angles as in the eye of the bee. We believe that homochirality may be found in the subsurface layers on Mars as a relic of extinct life, and on other solar system bodies as a sign of advanced pre-biotic chemistry. We discuss the chiral GC-MS planned for the Roland lander of the Rosetta mission to a comet and conclude with theories of the physical origin of homochirality.

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