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PubMed1968

Transport of aminophosphonic acids in Lactobacillus plantarum and Streptococcus faecalis.

Aminophosphonic acids analogous to glutamic acid, aspartic acid, alanine, and valine were actively accumulated by Lactobacillus plantarum. Uptake was dependent on the availability of glucose and, in all cases, the estimated intracellular concentrations substantially exceeded extracellular levels. During uptake, there was little metabolism of tritiated 2-amino-3-phosphonopropionic acid (APP), the aspartic acid analogue, and a negligible incorporation of isotope from this substance into the nucleic acid, lipid, protein, or cell wall fractions of the cell. Competition studies with APP indicated that its transport in L. plantarum and in Streptococcus faecalis was antagonized only by structurally related compounds such as glutamic, aspartic, and cysteic acids. Kinetic studies showed that APP was taken up by a single catalytic system in S. faecalis. A mutant strain of this organism which lacks one of two kinetically distinguishable dicarboxylic amino acid transport systems failed to accumulate measurable amounts of APP. These experiments indicate that the aminophosphonic acids are accumulated by the amino acid transport systems in these bacteria with minimal metabolic changes.

Amino Acids↗

PubMed1997

Some considerations regarding the use of amino acid racemization in human dentine as an indicator of age at death.

An HPLC method is described for simultaneously obtaining the enantiomeric ratio of three amino acids (aspartic acid, serine, and glutamic acid) from dental collagen, with a view to using this information for estimating age at death. Results are reported from a sample of twenty three known age modern teeth, six known age 19th C. AD teeth, and two unknown age Romano-British teeth. It was found (as expected) that all three D/L ratios changed significantly with chronological age. Standard calibration techniques were used to estimate ages for the six 19th C. AD specimens from regression equations estimated from the modern specimens, and also to predict (for the first time) the error associated with such estimates. Errors using aspartic acid were found to be similar to those obtained by other methods of age estimation from dental evidence, serine, and glutamic acid providing much poorer age estimates. Additionally, a systematic difference in the age-enantiomeric ratio relationship was observed between modern and older dental samples. It is concluded that there is some fundamental difference in the observed enantiomeric ratios between modern teeth and older samples, possibly as a result of the chemical alteration of the dental proteins.

Age Determination by Teeth↗

PubMed2005

Effects of theanine, r-glutamylethylamide, on neurotransmitter release and its relationship with glutamic acid neurotransmission.

t Theanine, r-glutamylethylamide, is one of the major amino acid components in green tea and many researchers have compared theanine's effects with glutamic acid because the chemical structure is similar. In the previous study, we demonstrated that theanine can pass brain-blood barrier and may play as an agonist or an antagonist of some receptors. In this study, we investigated the effects of theanine on neurotransmitter release in the rat brain striatum by in vivo brain microdialysis and examined whether theanine affected glutamate transporters by comparing it with a glutamate transporter blocker, L-trans-Pyrrolidine-2,4-dicarboxylic acid (L-trans-2,4-PDC). Because we investigated whether the effects of theanine is similar to L-trans-2,4-PDC on the brain neurotransmission, we measured dopamine release and some amino acids release which are known as excitatory or inhibitory neurotransmitters from neurons by theanine or L-trans-2,4-PDC perfusion into the rat brain striatum. L-trans-2,4-PDC or theanine perfusion into the brain striatum caused dopamine release from dopaminergic neurons. In addition, L-trans-2,4-PDC perfusion increased glutamic acid, aspartic acid and, whereas theanine perfusion prevented aspartic acid release and increased glycine release. These results suggested that the mechanism of dopamine release caused by theanine is different from glutamate transporter blockers or glutamic acid. Further, L-trans-2,4-PDC cause excitatory neurotransmission, whereas theanine may inhibit excitatory neurotransmission and cause inhibitory neurotransmission via glycine receptors.

Animals↗

PubMed1996

Amino acid secretion of the hen's oviduct during the egg formation cycle.

The free amino acid content of 34 hens' oviducts was determined in different phases of the egg formation cycle. In addition, quantitative changes of transmitter-type amino acids (glutamic acid, aspartic acid, taurine, glycine) were monitored in comparison with those of other amino acids participating in protein synthesis (e.g., lysine, tyrosine, valine). Different portions of the hen's oviduct, primarily the magnum and the uterus, were characterised by substantial amino acid secreting activity. The amino acids detectable in the highest quantity were taurine, glutamic acid, glycine and aspartic acid. These amino acids were present in high concentrations throughout the egg formation cycle, but their quantity abruptly decreased at the time of oviposition and ovulation. The quantitative changes of transmitter-type amino acids are mostly independent of those of other amino acids participating in protein synthesis. Since in our earlier in vitro studies the concentration changes of the transmitter amino acids studied were found to affect the motility and agglutination of spermatozoa, they--besides other factors--can be assumed to exert an influence on the sperm storage and release processes of the uterovaginal sperm storage tubules located in the oviduct of birds.

Amino Acids↗

PubMed1981

Erythrocytic enzymes and amino acids related to glutamic acid metabolism in childhood hypoproteinemic states.

The erythrocyte enzymes of glutamic acid metabolism (glutaminase I, glutaminase II, glutamic acid decarboxylase, glutamine synthetase, and transaminases) and related amino acids (glutamine, glutamic acid, aspartic acid, alanine, and gamma-aminobutyric acid) were estimated in 69 children with protein-energy malnutrition, 13 with nephrosis, and 10 with Indian childhood cirrhosis. Twenty-one apparently healthy children served as controls. There was a significant increase in the activities of erythrocytic glutaminase I, glutaminase II, glutamic acid decarboxylase, and glutamine synthetase in all the three hypoproteinemic states, while the activities of the transaminases showed a decrease in all the conditions. The concentrations of all the amino acids were significantly increased in both the varieties of protein-energy malnutrition (edematous and nonedematous). In nephrosis and Indian childhood cirrhosis, aspartic acid, alanine, and gamma-aminobutyric acid showed a significant rise. The concentration of glutamic acid was also significantly increased in nephrosis. The observations of the present study suggest an increase in intracellular production of glutamic acid in hypoproteinemia.

Alanine Transaminase↗

PubMed1996

Importance of the region around glycine-338 for the activity of enzyme I of the Escherichia coli phosphoenolpyruvate:sugar phosphotransferase system.

The gene encoding enzyme I of the phosphoenolpyruvate:sugar phosphotransferase system from an Escherichia coli enzyme I mutant was cloned and sequenced. The mutation was shown to be a guanine to adenine transition resulting in an altered protein in which glycine-338 was replaced by aspartic acid. The enzyme I structural gene was mutated to change glycine-338 to a variety of other amino acid residues. Fermentation tests indicated that glycine-338 could be mutated to alanine with no gross loss in phosphotransferase activity, while mutation to valine, glutamic acid, aspartic acid, arginine, histidine, or asparagine led to significant loss of activity. An expression vector for enzyme I was mutated to change glycine-338 to a variety of other amino acid residues and highly purified mutant proteins were prepared. Analysis of phosphorylation of the proteins by PEP indicated that mutation of glycine-338 to alanine had little effect on phosphorylation, mutation to valine substantially decreased phosphorylation, change to histidine or arginine drastically diminished phosphorylation, and mutation to aspartic or glutamic acids abolished phosphorylation activity. Mutation at glycine-338 influences the autophosphorylation rather than the phosphoryl transfer activity of enzyme I.

Amino Acid Sequence↗

PubMed2000

Oncogenic transformation by the FOX protein Qin requires DNA binding.

Some functions of the Qin oncoprotein are not dependent on DNA binding. In order to test the requirement for DNA binding in Qin-induced oncogenic transformation, site directed mutations were introduced in the winged helix (WH) DNA binding domain of the Qin protein. In cellular Qin (c-Qin), the glycine at position 233 was either deleted or substituted with the amino acids aspartic acid, alanine, glutamic acid, asparagine, proline or lysine. The same position carries aspartic acid in the viral Qin protein (v-Qin). The adjacent residues, threonine 232 and lysine 234, were separately mutated to proline. Several additional amino acid substitutions believed to be involved in DNA contacts were introduced at the following c-Qin positions: asparagine 189, histidine 193, serine 196 or arginine 236. Most of the substitutions reduced DNA binding of Qin, one mutation, H193A, completely abolished DNA binding, and another mutation, T232P, increased DNA binding affinity. Mutant H193A failed to transform chicken embryo fibroblasts (CEF), all other mutants, even those showing minimal DNA binding, retained oncogenicity for CEF. The efficiencies of focus formation induced by these mutant proteins in cell culture were not significantly different from that of wild type. However, the rate of focus development and the size of foci induced by the Qin mutants were greater with strong DNA binders than with weak DNA binders. Transdominant negative constructs consisting of the winged helix domain of cQin or v-Qin interfered with focus formation induced by full length Qin proteins. These results suggest that DNA binding is a prerequisite for transformation by Qin, and strong DNA binding is related to accelerated transformation in CEF.

Amino Acid Sequence↗

PubMedDate not supplied

[Amino acid composition of human semen from different clinical diagnoses].

The amino acid analysis of human semen shows for the different clinical diagnoses the predominant amino acids aspartic acid, serine, glycine, leucine and lysine. Analytical data indicate that there were differences in the amino acid composition between oligo- or azoospermia and terato- or asthenozoospermia by aspartic acid, glutamic acid, threonine, glycine, alanine and isoleucine.

Amino Acids↗

PubMed1985

General method for the rapid solid-phase synthesis of large numbers of peptides: specificity of antigen-antibody interaction at the level of individual amino acids.

A novel yet simple method is described that facilitates the synthesis of large numbers of peptides to the extent that the synthesis process need no longer be the limiting factor in many studies involving peptides. By using the methods described, 10-20 mg of 248 different 13-residue peptides representing single amino acid variants of a segment of the hemagglutinin protein (HA1) have been prepared and characterized in less than 4 weeks. Through examination of the binding of these analogs to monoclonal antibodies raised against residues 75-110 of HA1, it was found that a single amino acid, aspartic acid at position 101, is of unique importance to the interaction. Two other residues, aspartic acid-104 and alanine-106, were found to play a lesser but significant role in the binding interaction. Other single positional residue variations appear to be of little or no importance.

Amino Acid Sequence↗

PubMed1987

Human aldolase A deficiency associated with a hemolytic anemia: thermolabile aldolase due to a single base mutation.

Fructose-1,6-bisphosphate aldolase A (fructose-bisphosphate aldolase; EC 4.1.2.13) deficiency is an autosomal recessive disorder associated with hereditary hemolytic anemia. To clarify the molecular mechanism of the deficiency at the nucleotide level, we have cloned aldolase A cDNA from a patient's poly(A)+ RNA that was expressed in cultured lymphoblastoid cells. Nucleotide analysis of the patient's aldolase A cDNA showed a substitution of a single nucleotide (adenine to guanine) at position 386 in a coding region. As a result, the 128th amino acid, aspartic acid, was replaced with glycine (GAT to GGT). Furthermore, change of the second letter of the aspartic acid codon extinguished a F ok I restriction site (GGATG to GGGTG). Southern blot analysis of the genomic DNA showed the patient carried a homozygous mutation inherited from his parents. When compared with normal human aldolase A, the patient's enzyme from erythrocytes and from cultured lymphoblastoid cells was found to be highly thermolabile, suggesting that this mutation causes a functional defect of the enzyme. To further examine this possibility, the thermal stability of aldolase A of the patient and of a normal control, expressed in Escherichia coli using expression plasmids, was determined. The results of E. coli expression of the mutated aldolase A enzyme confirmed the thermolabile nature of the abnormal enzyme. The Asp-128 is conserved in aldolase A, B, and C of eukaryotes, including an insect, Drosophila, suggesting that the Asp-128 of the aldolase A protein is likely to be an amino acid residue with a crucial role in maintaining the correct spatial structure or in performing the catalytic function of the enzyme.

Anemia, Hemolytic, Congenital↗

PubMed1995

Effect of stress on amino acids and related compounds in various tissues of the rat.

The composition of various amino acids and related compounds in the aorta, ventricle, atria, liver, kidney, pancreas, bronchi and adrenals of rats is presented. These patterns are qualitatively similar, but quantitatively different. Stress changed these patterns. In the aorta, alpha-aminobutyric acid and ammonia are decreased. In the ventricle, phosphoserine and red. Glutathione are increased; and ammonia, arginine, asparagine, carnosine, ethanolamine, glutamic acid, glutamine, lysine, phosphoethanolamine and taurine are decreased. In the atria, alpha-aminobutyric acid, aspartic acid, ethanolamine and red. glutathione are increased; and ammonia is decreased. In the liver, alpha-aminobutyric acid, cystine, isoleucine, red. glutathione, methionine and phenylalanine are increased. In the kidney, ethanolamine is increased; and beta - aminobutyric acid, citrulline, cystathionine, glutamic acid, glycine and tryptophan are decreased. In the pancreas, alpha-aminoadipic acid, ox. glutathione, leucine, glutamine, 1-methylhistidine, phenylalanine, phosphoserine, tryptophan and valine are increased; and ammonia, cystine and aspartic acid are decreased. In the adrenal glands, anserine, glutamic acid, glutamine and ox. glutathione are increased; and arginine is decreased. In the bronchi, ethanolamine and beta-alanine are increased and alpha-aminobutyric acid and ox. glutathione are decreased. Thus, stress affects certain amino compounds but changes are substance and tissue specific and independent of changes seen in the plasma.

Amino Acids↗

PubMed1986

[Ability of amino acid components of proteins to stimulate the thymus-dependent immune response].

The ability of protein amino acids to facilitate differentiation of mouse bone marrow cells into T lymphocytes in vitro and to stimulate primary immune response to sheep red blood cells in vivo was studied. Nine out of twenty amino acids (aspartic acid, asparagine, glutaminic acid, cysteine, serine, threonine, tryptophan, alanine and valine) were shown to possess immunologic activity, with the highest activity revealed in aspartic acid.

Adjuvants, Immunologic↗

PubMed1977

[Passage of amino acids through the minimal wall in sheep].

Three sheep with a small isolated rumen (after Gridin et al., 1964) were studied for the passage of amino acids from the blood to the isolated rumen before feeding and 1, 2, 3, 4 and 5 hours after feeding. It was found that, on an average for all the time intervals mentioned above, the passage of glycine was the largest of all the amino acids studied (0.512 muMol per 100 ml), followed, in descending order, by lysine, alanine, glutamic acid, aspartic acid, serine, leucine, threonine, isoleucine, arginine, tyrosine, and phenylalanine (0.038 muMol per 100 ml). Before feeding and one hour after feeding, lysine shared the greatest proportion of all amino acids that had passed into the isolated rumen (0.565-0.43 muMol per 100 ml), followed, in descending order, by glycine, alanine, valine, aspartic acid, glutamic acid, leucine, serine, threonine, isoleucine, tyrosine, phenylalanine; arginine was, in this case, represented by the smallest proportion (0.042-0.030 muMol per 100 ml). It is inferred from the results that the amount of amino acids passing from the blood through the rumen wall changes with the time that has elapsed from feeding, and that before feeding this passage is more intensive than after feeding. These changes are held to be related with an increased passage of endogenous nitrogen to the rumen in the period of a relative deficiency of substances which are derived from the feed and are essential for maintaining homeostasis in the rumen.

Amino Acids↗

PubMed2006

A comparative study of metabolic engineering anti-metabolite tolerance in Escherichia coli.

A problem in strain engineering is that mutations that benefit the expression of a phenotype in one environment may impose a cost to biological fitness in a new environment. The overall objective of this study was to improve understanding of this phenomenon within the context of a classic anti-metabolite selection strategy. We have engineered Escherichia coli using three mutagenesis techniques (chemical mutagenesis, insertional mutagenesis, and plasmid-based overexpression) and assessed the relative costs and benefits to biological fitness of mutants selected for tolerance to five amino acid analogs whose target amino acids (glutamatic acid, aspartic acid, tryptophan, glycine, and serine) differ in metabolic connectivity and biosynthetic energy requirements. Our major findings include (i) the fold increase in anti-metabolite tolerance, independent of mutagenesis strategy, was much greater for aspartic acid beta-hydroxamate (AAH) compared to all other tested hydroxamates, (ii) increased tolerance to glutamic acid gamma-hydroxamate (GAH) was not achieved using any of the mutagenesis strategies, and (iii) characteristics of the anti-metabolite, rather than those of the corresponding metabolite, were more important in determining the ability to increase tolerance.

Drug Tolerance↗

PubMed1993

Design of helix ends. Amino acid preferences, hydrogen bonding and electrostatic interactions.

The amino acid sequence and chemical interactions at the ends of 163 helices were surveyed so as better to understand amino acid preferences previously observed [Richardson, J.S. & Richardson, D.C. (1988) Science 240, 1648-1652]. Amino acid preferences differed from the previous survey in some significant details and in ways that might affect the choice of amino acids during the design of a protein helix. The following major conclusions about helix ends were deduced from additional patterns of amino acid occurrence and interactions that were observed. (1) A specific pair of hydrogen bonds is often observed between a glutamic acid (or glutamine) side chain at the N3 position and the N-cap amide hydrogen, and between the N-cap side chain (often threonine) and the N3 amide hydrogen. This reciprocal interaction may be an important means of stabilizing the N-terminal end of a helix. (2) Negatively charged amino acids (aspartic acid and glutamic acid) at the N-terminal end of helices may be more important in stabilizing protein helices than positively charged residues (chiefly lysine) at the C-terminal end. (3) The identity of the residue at the N-cap position is correlated with the backbone conformation at that position. (4) Aspartic acid (or asparagine) at the N2 or N3 position may adopt a conformation that suggests a hydrogen-bonding interaction with the end of the helix, especially when the N-cap side chain does not form a hydrogen bond with the end of the helix.

Amino Acids↗

PubMed2004

Interaction of aluminium ions with some amino acids present in human blood.

The interaction of aluminium with some amino acids present in human blood was studied combining ion-chromatography (IC), atomic absorption spectrometry (AAS) and ultrafiltration (UF) techniques. An IC system for simultaneous determination of ornithine, lysine, glutamic acid, aspartic acid and tyrosine was developed. By adding aluminium to standard solutions of the amino acids and keeping the pH at 6 and 7 it was possible to verify that aluminium caused a reduction on the amino acid chromatographic signals. Similar experiment, carried out for copper showed the same behaviour (with different percentage of signal reductions) and validated the results for aluminium, considering that the interaction Cu-amino acid is well-established. The AAS analysis of sample fractions (500 microl) after the IC separation showed that aluminium (as copper as well) is not present in the fractions in which the amino acid peaks appear in the chromatogram. These approaches carried out with serum samples after UF showed that part of the "free" fraction of serum aluminium is distributed, besides other ligands, among these amino acids. It was found that in serum the affinity for aluminium followed the sequence Lys>Orn>Tyr>Glu approximately Asp.

Aluminum↗

PubMed1998

The neurochemical markers in cerebrospinal fluid to differentiate between aseptic and tuberculous meningitis.

In this study, the use of neurochemical markers in patients with aseptic and tuberculous meningitis has been investigated. The cerebrospinal fluid levels of amino acids, nitrite (a metabolite of nitric oxide), vitamin B12 and homocysteine were quantitated in both groups of patients. Among the amino acids, aspartic acid and glutamic acid both excitatory amino acid, GABA, glycine and tryptophan were all significantly increased in both patient groups whereas decreased level of taurine and increased level of phenylalanine were only found in patients with tuberculous meningitis. The levels of nitrite and its precursor arginine were significantly higher in patients with tuberculous meningitis whereas unchanged levels were found in patients with aseptic meningitis. A significantly increased homocysteine level and a decreased level of vitamin B12 were found only in patients with tuberculous meningitis whereas unchanged levels were found in patients with aseptic meningitis. This indicates that patients with tuberculous meningitis are particularly prone to vitamin B12 deficiency resulting into increased level of HC, and involvement of free radical showing the importance of these biological markers for promoting the possibility for the design of therapeutic approach.

Adult↗

PubMed1997

Ontogeny of neurotransmitter amino acids in human fetal brains.

A wide spectrum of developmental profiles is presented for a few important neurotransmitter amino acids, namely gamma-aminobutyric acid, glycine, glutamic acid, aspartic acid and taurine as well as the key enzymes involved in their metabolism in human fetal brains of different gestational ages. Besides taurine almost all these amino acids and their key metabolic enzymes were found to be progressively enhanced upto the mid period of third trimester of pregnancy indicating a rapid growth of nerve processes, myelination and maturation of fetal brains particularly during this period. Interestingly taurine showed an inverse relationship of ontogenic pattern with respect to its biosynthesizing enzyme in fetal brains.

4-Aminobutyrate Transaminase↗