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PubMed1985

Metabolism of sulfur-containing amino acids in the dermatophyte Microsporum gypseum. II. Acidic amino acid derivatives.

The dermatophyte Microsporum gypseum was cultivated on a glucose-arginine medium supplemented with five strongly acidic derivatives of cysteine (L-cysteine sulfinic acid, L-cysteic acid, L-serine-O-sulfate and taurine at a concentration of 5 mmol/l, and L-S-sulfocysteine at a concentration of 2.5 mmol/l). The addition of these substances did not stimulate the growth as compared with the control containing 0.5 mmol/l cystine. Cysteine sulfinic acid and cysteic acid showed rather inhibitory effects. A strong inhibition of the growth was caused by the presence of serine sulfate. During the growth, all substances investigated were gradually consumed and utilized not only as a source of sulfur but of nitrogen and carbon as well. Cysteine sulfinic acid and S-sulfocysteine were utilized most rapidly. Cysteic acid was also rapidly utilized but after a certain adaptation. Taurine was utilized slowly and serine sulfate very slowly. Excess sulfur contained in the substances used was excreted into the medium in the form of sulfate. Sulfate excretion was most rapid with cysteine sulfinic acid and slowest with taurine. With cysteine sulfinic acid, S-sulfocysteine and cysteic acid, small amounts of sulfite were found in the medium. The results obtained are in accordance with the presumption that cysteine sulfinic acid (but not cysteic acid and taurine) is an intermediate of cysteine catabolism in dermatophytes.

Amino Acids, Sulfur↗
PubMed1977

Role of protein dissociation in the transport of acidic amino acids by the Ehrlich ascites tumor cell.

The pH profile for the uptake of L-glutamic acid by the Ehrlich ascites tumor cell arises largely as a sum of the decline with falling pH of a slow, Na+-dependent uptake by System A, and an increasing uptake by Na+-independent System L. The latter maximizes at about pH 4.5, following approximately the titration curve of the distal carboxyl group. This shift in route of uptake was verified by (a) a declining Na+-dependent component, (b) an almost corresponding decline in the 2-(methylamino)-isobutyric acid-inhibitable component, (c) a rising component inhibited by 2-aminonorbornane-2-carboxylic acid. Other amino acids recognized as principally reactive with Systems A or L yielded corresponding inhibitory effects with some conspicious exceptions: 2-Aminoisobutyric acid and even glycine become better substrates of System L as the pH is lowered; hence their inhibitory action on glutamic acid uptake is not lost. The above results were characterized by generally consistent relations among the half-saturation concentrations of the interacting amino acids with respect to: their own uptake, their inhibition of the uptake, one by another, and their trans stimulation of exodus, one by another. A small Na+-dependent component of uptake retained by L-glutamic acid but not by D-glutamic acid at pH 4.5 is inhibitable by methionine but by neither 2-(methylamino)-isobutyric acid nor the norbornane amino acid. We provisionally identified this component with System ASC, which transports L-glutamine throughout the pH range studied. No transport activity specific to the anionic amino acids was detected, and the unequivocally anionic cysteic acid showed neither significant mediated uptake nor inhibition of the uptake of glutamic aic or of the norbornane amino acid. The dicarboxylic amino acids take the sequence, aspartic acid less than glutamic acid less than alpha-aminoadipic acid less than S-carboxymethylcysteine, in their rate of mediated, Na+-independent uptake at low pH. Diiodotyrosine and two dissimilas isomers of nitrotyrosine also show acceleration of uptake as the phenolate group on the sidechain is protonated, a result indicating that the acidic group need not be a carboxyl group and need not take a specific position in space to be accepted at the receptor site L. The presence of the carboxyl group does not upset the normal stereospecificity of System L until it falls on the beta-carbon in aspartic acid; even then it is the presence of the carbonyl group and not of the intact carboxyl group nor of its hydroxyl group that cancels out the stereospecificity, as was shown by the absence of normal stereospecificity for aspartic acid and asparagine and its presence in glutamic acid, homoserine and glutamine. In agreement, the uptak of aspartic acid is peculiarly sensitive to the presence of an alpha-methyl group or of other structures that modify the orientation of the sidechain.

Amino Acids↗
PubMed2003

Utilization of acidic amino acids and their amides by pseudomonads: role of periplasmic glutaminase-asparaginase.

The acidic amino acids (Asp, Glu) and their amides (Asn, Gln) support rapid growth of a variety of Pseudomonas strains when provided as the sole source of carbon and nitrogen. All key enzymes of glutamate metabolism were detected in P. fluorescence, with glutaminase and asparaginase showing the highest specific activities. A periplasmic glutaminase/asparaginase activity (PGA) was found in all pseudomonads examined, including a number of root-colonizing biocontrol strains. The enzyme was purified and shown to be identical with the ansB gene product described previously. In addition to PGA, P. fluorescens contains a cytoplasmic asparaginase with marked specificity for Asn. PGA is strongly and specifically induced by its substrates (Asn, Gln) but also by the reaction products (Asp, Glu). In addition, PGA is subject to efficient carbon catabolite repression by glucose and by citrate cycle metabolites. A mutant of P. putida KT2440 with a disrupted ansB gene was unable to utilize Gln, whereas growth of the mutant on other amino acids was normal.

Amino Acids, Acidic↗
PubMedDate not supplied

Studies on the transport of anions and zwitterions of acidic amino acids in Streptomyces hydrogenans.

In Streptomyces hydrogenans, acidic amino acids are taken up either as anions by a specific transport system or as zwitterions via a nonspecific one. Variations in the zwitterion concentration caused by changes in pH influence the uptake and exchange diffusion by the nonspecific system. Differences in pH-optima for L-glutamate and L-aspartate transport are due to the different pK2-values of these amino acids. The anion transport by the specific system is accompanied by a short hyperpolarization of the membrane potential followed by a secondary influx of potassium ions into the cells.

Amino Acids↗
PubMed2006

CDC7 kinase phosphorylates serine residues adjacent to acidic amino acids in the minichromosome maintenance 2 protein.

Cdc7 is an essential kinase required for the initiation of eukaryotic DNA replication. Previous studies in many species showed that the minichromosome maintenance complex is a major physiological target of this kinase. In this study, we have mapped the sites in human Mcm2 protein that are phosphorylated by Cdc7. The in vitro phosphorylation of several Mcm2 truncated proteins and peptides revealed that Mcm2 contains two major ((5)S and (53)S) and at least three minor phosphorylation sites ((4)S, (7)S, and (59)T) located at the N-terminal region. Alanine substitution experiments with Mcm2 peptides showed that the phosphorylation of (5)S and (53)S by Cdc7 required the presence of an acidic amino acid adjacent to a serine residue. Furthermore, although Cdc7 was unable to phosphorylate a Mcm2 peptide (spanning amino acids 19-30 and containing (26)S and (27)S), it phosphorylated (26)S efficiently when this peptide contained a chemically synthesized phospho-(27)S modification. Hence, additional Cdc7 phosphorylation sites could be generated in Mcm2 by its prior phosphorylation by a cyclin-dependent kinase. This finding may explain why the sequential action of cyclin-dependent and Cdc7 kinases is essential for the initiation of DNA replication.

Amino Acid Sequence↗
PubMed1996

The role of acidic amino acid residues in the structural stability of snake cardiotoxins.

We have recently shown that membrane-related activities of cardiotoxin V from Naja naja atra (CTX A5) are diminished at acidic pH although the overall beta-sheet structure of the molecule is maintained. In order to understand more about the mechanism of inactivation of CTX at acidic pH, we studied the effect of pH and denaturing reagents on the structural stability of CTX. We found, first, pH-induced structural transitions occurred in CTX A5 at two pH values as judged by the CD ellipticity around 195 nm: an increase in the beta-sheet content occurred around pH 4 and followed by a decrease, therein, around pH 2. The pKa of three acidic amino acid residues in CTX A5, i.e., Glu-17, Asp-42, and Asp-59, were determined to be 4.0, 3.2, and below 2.3, respectively, by NMR spectroscopy. The low pKa value of Asp-59 implies salt bridge formation between Lys-2 and Asp-59. Thus, electrostatic interaction may stabilize the three loop structure in addition to the hydrogen bonds between N- and C-termini of CTX molecule. Second, 2,2,2-trifluoroethanol (TFE) and guanidinium chloride (GdmHCI) were found to induce alpha-helical and random coil formation, respectively, in CTX A5 and eight other beta-sheet CTXs. Comparison of the relative potencies of TFE and GdmHCI to induce structural changes suggests that the amino acid residue located at position 17 plays a role in the structural stability. Specifically, CTXs containing negatively charged Glu-17 are least stable. It is suggested that Glu-17 may perturb the interaction between Lys-2 and Asp-59, and thus the overall stability of beta-sheet, in the presence of denaturing reagent. In conclusion, the perturbed structural stability of CTXs may partially explain the lower activity CTX exhibits at acidic pH. A structural model to account for the unfolding and refolding of CTX molecules without the breaking of disulfide bonds is also proposed.

Amino Acid Sequence↗
PubMed2005

Photorelease of carboxylic acids, amino acids, and phosphates from N-alkylpicolinium esters using photosensitization by high wavelength laser dyes.

Visible light (>450 nm) is used to efficiently cleave carboxylic acids, amino acids, and phosphates from their N-methyl picolinium esters. Photolysis using pyrromethene dyes PM 546 and PM 597 and also coumarin 6 as photosensitizers effects release of carboxylic acids, N-protected amino acids, and phosphates in quantitative yields. The effective rate of photorelease by the dyes, Phiepsilon, was found to be as high as 4500 M-1 cm-1. The photorelease proceeds through photoinduced electron transfer from the dye sensitizers to the N-methyl picolinium group. Fluorescence quenching and laser flash photolysis experiments support the photoinduced electron-transfer mechanism.

Amino Acids↗
PubMed1984

The DNA sequence of the nuclear gene coding for the 17-kd subunit VI of the yeast ubiquinol-cytochrome c reductase: a protein with an extremely high content of acidic amino acids.

We have determined the DNA sequence of the nuclear gene coding for the 17-kd subunit VI of the ubiquinol-cytochrome c reductase. The reading frame found encodes a putative polypeptide of 17 394 daltons. This protein is highly unusual: 38% of its residues are acidic and 14% are basic amino acids. The most notable feature in the protein sequence is a stretch of 25 consecutive acidic amino acids. The polypeptide has homology with the 9-kd so-called 'hinge' protein of beef-heart complex III, which also has a cluster of acidic residues. Acidic amino acids are likely to be essential for the function of these proteins, since their degree of conservation is higher than that of other residues.

Amino Acid Sequence↗
PubMed1982

Acidic amino acid antagonists of lateral perforant path synaptic transmission: agonist-antagonist interactions in the dentate gyrus.

Acidic amino acid antagonists were tested for their ability to block depolarizations produced by excitatory amino acids in the outer molecular layer of the dentate gyrus in hippocampal slices. 2-Amino-4-phosphonobutyrate (APB) and serine-O-phosphate (SOP), potent synaptic blockers of the lateral perforant path input to this system, are moderately selective antagonists of kainate and N-methyl-DL-aspartate depolarizations, but not depolarizations produced by L-glutamate, quisqualate, or serine-O-sulfate. N-Methyl-DL-aspartate responses were potently blocked by 2-amino-5-phosphonovalerate, but this antagonist is less potent than APB or SOP against the synaptic response.

2-Amino-5-phosphonovalerate↗
PubMed1979

The effect of acidic amino acid antagonists on synaptic transmission in the hippocampal formation in vitro.

The effects on synaptic efficacy of the putative acidic amino acid antagonists, 2-amino-4-phosphonobutyric acid (APB), 2-amino-3-phosphonopropionic acid (APP), 1-hydroxy-3-amino-pyrrolidone-2 (HA-966) and glutamic acid diethyl ester (GDEE), were tested by bath application to the hippocampal slice preparation. On the basis of previous work, we hypothesized that APB, HA-966 and GDEE might antagonize synaptic responses to either glutamate or aspartate, but APP should antagonize only synaptic responses to aspartate. APB and HA-966 reduced the amplitude of the extracellular EPSP recorded during stimulation of the perforant path fibers, but APP and GDEE were without effect. APB, APP and HA-966, but not GDEE, consistently inhibited transmission at Schaffer collateral and commissural synapses. The mossy fiber evoked extracellular EPSP was unaffected by these agents. At the concentrations used in this study (usually 2.5 mM) none of these drugs affected the amplitude of presynaptic fiber potentials or antidromic responses, indicating that they probably acted at synapses. The spontaneous activity of hippocampal pyramidal cells, but not of dentate granule cells, increased in the presence of 2.5 mM APB. The amplitude of the population spike generated by Schaffer commissural stimulation initially increased following introduction of APB into the medium and then declined in parallel with the extracellular EPSP. In addition, APB reduced the duration of recurrent inhibition during the period when pyramidal cell firing was enhanced. These results can be explained by an antagonism at the synapse between pyramidal cell and inhibitory interneuron.

Afferent Pathways↗
PubMed1988

[Action of l-DOPA and acidic amino acids on isolated neurons of spinal cord in the lamprey].

Ionic currents induced by application of L-3, 4-dihydroxyphenylalanine (L-DOPA) and acidic amino acids: L-glutamate, kainate, N-methyl-D-aspartate (NMDA) were investigated in experiments on isolated spinal cord neurons of the lamprey by means of whole-cell recording and concentration clamp methods. L-DOPA was found to activate glycine, but not excitatory amino acid receptors.

Amino Acids↗
PubMed1985

Afferent facilitation induced by iontophoretic application of acidic amino acids in the ampullary electroreceptors of Plotosus.

In an attempt to identify the afferent transmitter in acousticolateralis receptors, effects of some acidic amino acids were examined in ampullary electroreceptors of the marine catfish Plotosus anguillaris, which have only afferent innervation. The ampulla (sensory epithelium) was first hyperpolarized in situ to suppress receptor-cell activity and release of transmitter, and hence resting afferent discharges completely. In the absence of transmitter, amino acids were applied to the ampulla by iontophoresis through three-barreled electrodes. Afferent impulses were recorded from the nerve trunk by a suction electrode, and single-unit responses were analyzed by their instantaneous frequency (F) records. L-Glutamate (Glu) induces single-unit responses postsynaptically at discrete spots over the ampulla. The F records showed graded and slow time courses, and F peaks increased sigmoidally against Glu doses with Hill coefficients of 2-3. Response maxima reached 120-210 Hz in doses of one log unit over the threshold. Glu response showed little desensitization. At the Glu-sensitive spots, kainate (KA) and quisqualate (QA) induced more persistent excitation and L-homocysteate (HCA) weaker excitation than did Glu, with similar latency. L-Aspartate (Asp) induced small slow responses with long latency in only one third of the tested Glu spots. D-Glutamate (D-Glu), D-aspartate (D-Asp), L-cysteate (CA), L-cysteine sulfinate (CSA), and N-methyl-DL-aspartate generally induced no response. Some aspartate analogues, L- and D-Asp, CA, and CSA induced persistent potentiation of Glu responses. Apparent affinity increase and change in response shape during potentiation indicated suppression of Glu uptake. However, apparent slope change in the log dose-response curves suggested that additional mechanisms were involved. In contrast, QA, KA, Glu, and HCA induced the excitation only. Comparable topical application of the transmitter was simulated by stimulating a few receptor cells at Glu spots to induce focal responses. Some aspects of the focal and Glu responses were compared. Pharmacological and neurochemical evidence so far available on this material is discussed with respect to the Glu hypothesis. Glu, even though a potent agonist in terms of afferent excitation, seems to act on extrasynaptic receptor sites in the nonmyelinated nerve terminals.

Afferent Pathways↗
PubMed1995

The transport of acidic amino acids and their analogues across monolayers of human intestinal absorptive (Caco-2) cells in vitro.

The X-AG system, a sodium-dependent, acidic amino-acid transport system has been implicated in the transport of L-aspartate and L-glutamate across monolayers of human Caco-2 cells, an in vitro model of intestinal absorption. This system, which shares many properties with the L-glutamate carrier present in the human jejunum, is highly saturable (> 95% at 50 microM), vectorial (apical-to-basolateral >> basolateral-to-apical) and sodium-, pH- and temperature-dependent. L-Aspartate was also transported against a 10-fold reverse concentration gradient. These data are consistent with a major (saturable) carrier-mediated pathway superimposed onto a minor non-saturable (diffusional) pathway. The carrier has an absolute sodium-dependence and the Michaelis constants for the sodium-dependent transport component (Km) for L-aspartate and L-glutamate were 56 +/- 3 microM and 65 +/- 6 microM, respectively. Cross-inhibition studies showed that strong interaction with the carrier was limited to close analogues of the natural substrates. Potent inhibitors included L-aspartate, D-aspartate (Ki, 70 microM), L-glutamate (Ki 180 microM) and threo-beta-hydroxy-DL-aspartate (Ki, 55 microM), while partial inhibitors included alpha-methyl-DL-aspartate, D-glutamate, L-asparagine, L-proline and L-alanine. Replacement of the side-chain -COO- group (aspartate) with -SO-3 (L-cysteate, Ki, 65 microM) or -(H)P(O)O- (DL-3-(hydroxyphosphoryl)alanine, Ki, 60 microM) maintained strong interaction with the carrier while -As(O)(OH)O- (DL-3-arsonoalanine, Ki, 1100 microM) and -P(O)(OH)O- (DL-3-phosphonoalanine, Ki, 3270 microM) were much more weakly bound, with the larger, but probably less ionised, arsono analogue being more tightly bound than the phosphono compound. The corresponding analogues of glutamate (homologous extension of the methylene chain) showed negligible interaction. We conclude that Caco-2 monolayers are a relevant experimental model for the study of the transport of acidic amino acids and their analogues in man.

Amino Acids, Dicarboxylic↗
PubMed1991

Acidic Amino Acids and Self-stimulation of the Prefrontal Cortex in the Rat: A Pharmacological Study.

The effects of intraventricular and intracortical microinjections of acidic amino acid antagonists on self-stimulation (SS) of the medial prefrontal cortex (MPC) were investigated. Self-stimulation was measured by depressing a lever in a standard chamber. Spontaneous motor activity of the animal and SS of the contralateral non-injected MPC were used as control for non-specific effects of the drugs. Intraventricular microinjections of gamma-d-glutamylglycine (DGG), an antagonist of NMDA, kainate and quisqualate receptors, or 2-amino-5-phosphonovalerate (AP-5), a specific antagonist of NMDA receptors, produced a dose-related decrease of SS in the MPC. Spontaneous motor activity of the animal was not significantly affected. Unilateral microinjections into the medial prefrontal cortex of DGG or AP-5 produced a decrease of SS in the ipsilateral side while no effects were found on the contralateral MPC. On the contrary, intraventricular microinjections of gamma-d-glutamyltaurine (Glu-tau), an antagonist with more relative affinity for kainate and quisqualate receptors, produced a dose-related decrease of both self-stimulation and spontaneous motor activity of the rats. Moreover, intracortical microinjections of Glu-tau had no effect on self-stimulation of this cortical area. These results suggest that acidic amino acids through NMDA, but not kainate or quisqualate, receptors could be part of the neurochemical substrate underlying SS of the MPC in the rat.

Journal Article↗
PubMed1986

In vivo inhibition of tyrosine uptake into rat retina by large neutral but not acidic amino acids.

The uptake of tyrosine into rat retina and brain was studied in vivo after its peripheral injection alone or in combination with other amino acids. Both retinal and brain tyrosine levels increased monotonically for at least 60 min after tyrosine administration. When tyrosine was injected along with branched-chain amino acids, but not with acidic amino acids, such increments in retinal and brain tyrosine levels were significantly attenuated. The postinjection tyrosine levels in retina and brain paralleled better the serum ratio of tyrosine to the sum of the other large neutral amino acids (which include the branched-chain amino acids) than the serum tyrosine level alone. These results suggest that tyrosine uptake into rat retina, like that into brain, is mediated by a competitive transport system shared among the large neutral amino acids.

Amino Acids↗
PubMed1983

Kinetics and localization of tubular resorption of "acidic" amino acids. A microperfusion and free flow micropuncture study in rat kidney.

The unidirectional resorption rates of L-glutamate (initial concentrations of 0.07, 0.66, 2.0 or 20.0 mmol X 1(-1)), D-glutamate (0.66 mmol X 1(-1) in the presence or absence of 20 mmol X 1(-1) L-glutamate), and of L-aspartate (0.073, 0.3, 0.66, 2.0 or 5.0 mmol X 1(-1)) were determined in the rat proximal convolution. L-Glutamate resorption was saturable. A permeability coefficient (P) of less than or equal to 20 microns2 X S-1, and a maximum resorption rate (Jmax) of 0.15 +/- 0.015 (SEM) nmol X S-1 X m-1 at a Km of 0.17 +/- 0.025 (SEM) mmol X 1(-1) was obtained for L-glutamate. For L-aspartate, Jmax was 0.13 +/- 0.005 at a Km of 0.1 +/- 0.013. A free flow glutamate concentration profile along the proximal convolution was (I) predicted from these constants and (II) actually measured by means of free flow micropuncture. The data agree very well and show that more than 90% of the filtered load is resorbed within the first third of the proximal convolution. The late proximal and early distal free flow recoveries of L-glutamate amounted to 5.3 +/- 1.7% (SEM) and 6.6 +/- 1.4% of the filtered load, respectively. In contrast to this, unidirectional resorption during the microperfusion of the same tubule section was high: fractional resorption amounted to ca. 96% at 2 mmol X 1(-1) initial L-glutamate. It fell to 35 or 33% respectively if the initial L-glutamate concentration was 20 mmol X 1(-1) or if the resorption of 0.66 mmol X 1(-1) D-glutamate in presence of 20 mmol X 1(-1) L-glutamate was measured. The fractional excretion of endogenous L-glutamate in the final urine amounted to 0.13 +/- 0.012% of the filtered load. It is concluded that L-glutamate and L-aspartate are quickly resorbed in early parts of the proximal convolution (low Km). Saturation already occurs when there is a small increase in the filtered load (low Jmax). The nephron section between the late proximal and early distal nephron sites also reabsorbs "acidic" amino acids. Normally, however, the back leak cancels this out, and net flux becomes zero. Deep nephrons seem to handle amino acids somewhat differently than superficial nephrons do.

Animals↗