Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: CAS:107-95-9 (beta-alanine)
 2,037 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Intestinal absorption of amino acids in the chicken occurs by way of processes which are concentrative, Na+-dependent and dependent upon metabolic energy in the form of ATP. Intestinal transport is carrier-mediated, subject to exchange transport (trans-membrane effects) and is inhibitable by sugars, reagents which inactivate sulfhydryl groups, potassium ion, and by deoxpyridoxine, an anti-vitamin B6 agent. It is stimulated by phlorizin, a potent inhibitor of sugar transport, and in Na+-leached tissue by modifiers of tissue cyclic AMP levels, e.g. theophylline, histamine, carbachol and secretin. Separate transport sites with broad, overlapping specificities function in the intestinal absorption of the various classes of common amino acids. A simple model for these sites includes one for leucine and other neutral amino acids, one for proline, beta-alanine and related imino and amino acids, one for basic amino acids, and one for acidic amino acids. Absorption of amino acids appears to be widespread in occurrence in the digestive tract of the domestic fowl; transport has been reported to be present in the crop, gizzard, proventriculus, small intestine and in the colon. By the end of the first week of life post-hatch, the caecum loses its ability to transport. Similarly, the yolk sac loses its ability by the second day post-hatch. Intestinal transport was noted before hatch and was found to be maximal immediately post-hatch. A requirement for Ca2+ appears to be lost after the first week of life post-hatch. The cationic amino acids appear to be reabsorbed by a common mechanism in the kidney. Transport rates of leucine measured in the intestine or in the erythrocyte were found to cluster about discrete values when many individual chickens were surveyed; such patterns may be an expression of gene differences between individuals. Two lines of chickens have been developed, one high and the other low uptake, through selective breeding based on the ability of individual birds to absorb leucine in erythrocytes. High leucine absorbing chickens were found to be more effective in absorbing lysine and glycine, were more effectively stimulated by Na+, had greater erythrocyte Na+, K+-ATPase activity, and their erythrocytes contained about 20% less Na+ than low line erythrocytes. The underlying genetic difference between these lines may reside at the level of the Na+, K+-ATPase and (or) with a regulatory gene determining carrier copies. Amino acid transport in erythrocytes was noted to be highest in pre-hatch chicks and to diminish during post-hatch development.(ABSTRACT TRUNCATED AT 400 WORDS)
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PMID:Cell membrane amino acid transport processes in the domestic fowl (Gallus domesticus). 614 42

Free amino acids and urea were analyzed in 78 human milk samples obtained during the first 5 wk of lactation from 10 mothers delivering at term. Significant differences (p less than 0.05) in the concentrations between colostral and mature milk were found for glutamic acid, glutamine, alanine, glycine, cystine, and phosphoethanolamine which increased, and with serine, phosphoserine, aspartic acid + asparagine, arginine, lysine, isoleucine, phenylalanine, proline, methionine, tryptophan, and beta-alanine which decreased. Some of these changes occurred within the first 5 days of lactation, so that differences between transitional and mature milk became negligible (glutamic acid, alanine, and serine, aspartic acid + asparagine, lysine, isoleucine, methionine, tryptophan, respectively). No significant differences between any of the three stages of lactation were found regarding the concentrations of total free amino acids, urea, taurine, threonine, valine, leucine, histidine, and tyrosine. Possible relevances for free amino acids, including nonprotein ones, in human milk are discussed.
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PMID:Human milk nonprotein nitrogen components: changing patterns of free amino acids and urea in the course of early lactation. 614 84

The dynamics of the axoplasmic transport of free beta-alanine and 3-O-methyl-D-glucose were quantitatively characterized in vivo in the pike olfactory nerve following intranasal application of the tritiated substances. Both compounds were found to be taken up by the epithelium but not metabolized to a significant extent. Axoplasmic transport showed the same dynamics as rapid transport of protein and free leucine in this nerve. No synthesis or transport of carnosine was detectable. The results are in agreement with the view that rapid axoplasmic transport is capable of conveying free, low molecular weight molecules in a non-specific manner.
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PMID:3-O-methyl-D-glucose and beta-alanine: rapid axoplasmic transport of metabolically inert low molecular weight substances. 618 11

Acyl carrier protein (ACP) functions as a cofactor in fatty acid biosynthesis due to the covalent linkage of an acyl moiety to its 4'-phosphopantetheine prosthetic group. This prosthetic group undergoes turnover in vivo and since the apoprotein is functionally inactive, the interconversion between ACP and apo-ACP has been considered as a possible regulatory point in lipid biosynthesis. To investigate this possibility, the ratio of ACP to apo-ACP was measured in Escherichia coli. An apo-ACP standard was synthesized using [ACP] phosphodiesterase (EC 3.1.4.14) and could be clearly separated from ACP by conformationally sensitive gel electrophoresis, thus providing a reliable assay for the presence of these two species. Antibodies specific for ACP were purified from rabbit serum on an ACP-Sepharose column and subsequently used to synthesize an immunoaffinity column. Chromatography of leucine-labeled cell extracts on this support resulted in the specific binding of ACP, but apo-ACP was not detected in either logarithmically growing or stationary phase cells, although both ACP species bound to the purified anti-ACP IgG. Apo-ACP was not detected as an intermediate in ACP biosynthesis, suggesting that apo-ACP is rapidly converted to ACP following translation. CoA is the biosynthetic precursor to the ACP prosthetic group, but apo-ACP did not accumulate when the intracellular CoA concentration was severely depressed in strain SJ16 (panD), a beta-alanine auxotroph. Strain MP4 (acpS) is conditionally defective in [ACP]synthase (EC 2.7.8.7) and apo-ACP was the predominant form of ACP synthesized in this strain under nonpermissive conditions. Even under conditions that permitted growth, apo-ACP comprised 70% of the total ACP pool in strain MP4. Strain MP4 possessed a phospholipid to protein ratio within the normal range, suggesting that the ratio of ACP to apo-ACP can be significantly altered without affecting total lipid content. Thus, it appears that the prosthetic group turnover cycle maintains all of the ACP in an active form in vivo and a regulatory role for the ACP/apo-ACP ratio seems doubtful.
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PMID:Ratio of active to inactive forms of acyl carrier protein in Escherichia coli. 631 88

Structural genes have been identified for all of the enzymes involved in the biosynthesis of pantothenic acid in Salmonella typhimurium and Escherichia coli K-12, with the exception of ketopantoic acid reductase, which catalyzes the conversion of alpha-ketopantoate to pantoate. The acetohydroxy acid isomeroreductase from S. typhimurium efficiently bound alpha-ketopantoate (K(m) = 0.25 mM) and catalyzed its reduction at 1/20 the rate at which alpha-acetolactate was reduced. Since two enzymes could apparently participate in the synthesis of pantoate, a S. typhimurium ilvC8 strain was mutagenized to derive strains completely blocked in the conversion of alpha-ketopantoate to pantoate. Several isolates were obtained that grew in isoleucine-valine medium supplemented with either pantoate or pantothenate, but not in the same medium supplemented with alpha-ketopantoate or beta-alanine. The mutations that conferred pantoate auxotrophy (designated panE) to these isolates appeared to be clustered, but were not linked to panB or panC. All panE strains tested had greatly reduced levels of ketopantoic acid reductase (3 to 12% of the activity present in DU201). The capacity of the isomeroreductase to synthesize pantoate in vivo was assessed by determining the growth requirements of ilvC(+) derivatives of panE ilvC8 strains. These strains required either alpha-ketopantoate, pantoate, or pantothenate when the isomeroreductase was present at low levels; when the synthesis of isomeroreductase was induced, panE ilvC(+) strains grew in unsupplemented medium. These phenotypes indicate that a high level of isomeroreductase is sufficient for the synthesis of pantoate. panE ilvC(+) strains also grew in medium supplemented with lysine and methionine. This phenotype resembles that of some S. typhimurium ilvG mutants (e.g., DU501) which are partially blocked in the biosynthesis of coenzyme A and are limited for succinyl coenzyme A. panE ilvC(+) strains which lack the acetohydroxy acid synthases required only methionine for growth (in the presence of leucine, isoleucine, and valine). This and other evidence suggested that the synthesis of pantoic acid by isomeroreductase was blocked by the alpha-acetohydroxy acids and that pantoic acid synthesis was enhanced in the absence of these intermediates, even when the isomeroreductase was at low levels. panE ilvC(+) strains reverted to pantothenate independence. Several of these revertants were shown to have elevated isomeroreductase levels under noninduced and induced conditions; the suppressing mutation in each revertant was shown to be closely linked to ilvC by P22 transduction. This procedure presents a means for obtaining mutants with altered regulation of isomeroreductase.
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PMID:Role of acetohydroxy acid isomeroreductase in biosynthesis of pantothenic acid in Salmonella typhimurium. 640 Dec 79

The transport of the dibasic amino acid L-lysine across the serosal pole of the intestinal epithelium has been studied using the vascularly perfused anuran small intestine. The exit of pre-loaded lysine into the vascular bed was inhibited by L-ornithine (2 mM) and L-arginine (10 mM) when pulsed through the lumen during the wash-out, while 2-aminoisobutyric acid (AIB), L-histidine, L-citrulline and L-cystine had no effect. Luminal L-leucine and L-alanine at a concentration of 10 mM markedly stimulated the unloading of lysine into the vascular bed and sarcosine, L-proline and beta-alanine also did so to a lesser extent. The instantaneous rate constant for lysine exit into the vascular bed was increased by the presence of L-arginine, L-ornithine, L-citrulline, L-histidine, AIB, L-leucine and L-alanine at a concentration of 10 mM in the vascular bed. L-proline had no effect. The simultaneously measured efflux of lysine into the lumen was unaffected by the presence of the other amino acids in the vascular bed. The uptake of lysine into the epithelium from the vascular bed was accelerated by L-ornithine and slightly by L-arginine when they were present in the lumen, while L-leucine, L-alanine, beta-alanine, L-proline, L-citrulline, sarcosine, L-histidine and AIB had no effect. The instantaneous rate constant for lysine wash-out into the vascular bed was transiently increased by the presence of L-leucine in the vascular bed at concentrations of 10, 0.10 and 0.01 mM. The steady-state transfer of lysine from the lumen to the vascular bed was stimulated in a biphasic manner by 5 mM-leucine in the lumen and by 0.5 mM-leucine in the vascular bed. The mechanisms for these interactions between lysine transport across the basolateral membrane of the enterocyte and other amino acids are discussed and a possible role for neutral amino acid stimulation of lysine exit is proposed.
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PMID:Characteristics of lysine transport across the serosal pole of the anuran small intestine. 641 62

Fatty acid synthase from the uropygial gland of goose was inactivated by iodoacetamide with a second-order rate constant of 1.3 M-1 S-1 at pH 6.0 and 25 degrees C. Of the seven component activities of the synthase, only the condensation activity was significantly inhibited by iodoacetamide modification. Since preincubation of the enzyme with acetyl-CoA, but not with malonyl-CoA, protected the enzyme from inactivation by iodoacetamide, it is suggested that iodoacetamide probably modified the primer-binding thiol group at the condensation active site. Determination of the stoichiometry of modification was done using [1-14C]iodoacetamide that was purified by high-performance liquid chromatography. Graphical analysis of the data showed that binding of 1.2 carboxamidomethyl groups per subunit of fatty acid synthase would result in complete inhibition of the enzyme activity, suggesting that there is one condensation domain per subunit of fatty acid synthase. Analysis of the tryptic peptide map of the enzyme that was modified with [1-14C]iodoacetamide in the presence and absence of acetyl-CoA revealed that acetyl-CoA prevented the labeling of a major radioactive peptide and a minor radioactive peptide. These two peptides were purified by high-performance liquid chromatography. Amino acid analysis of these two peptides revealed that the major radioactive peptide contained S-carboxymethylcysteine while the minor radioactive peptide did not. However, the latter peptide contained beta-alanine, suggesting that this peptide was from the acyl carrier protein segment of fatty acid synthase and that the iodoacetamide treatment resulted in modification of the pantetheine thiol, although to a lower extent than the primer-binding thiol. The sequence of the primer-binding active site peptide from the condensation domain was H2N-Gly-Pro-Ser-Leu-Ser-Ile-Asp- Thr-Ala-Cys(carboxamidomethyl)-X-Ser-Ser-Leu-Met-Ala-Leu-Glu-Asn-A la-Tyr-Lys- COOH, the first reported sequence of the condensation active site from a vertebrate fatty acid synthase. The acyl carrier protein segment showed extensive sequence homology with the acyl carrier protein of Escherichia coli, particularly in the vicinity of the phosphopantetheine attachment, and the sequence was H2N-Asp-Val-Ser-Ser-Leu- Asn-Ala-Asp-Ser-Thr-Leu-Ala-Asp-Leu-Gly-Leu-Asp-Ser(4'-phosphopanteth ein e) -Leu-Met-Gly-Val-Glu-Val-Arg-COOH.
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PMID:Specific modification of the condensation domain of fatty acid synthase and the determination of the primary structure of the modified active site peptides. 671 25

1. Beta-alanine is found in mycelial walls of mature tan, but not immature white, stage of Morchella esulenta, nor in any stage of a permanently white mutant. 2. Beta-alanine is also found in hydrolysed water-extracts of human hair, the concentration being higher in blond than in dark brown, and in pigmented than in unpigmented hair. 3. Beta-alanine, added to tyrosinase-oxidized tyrosine, dopa, or dopamine has only a slight yellowing influence on the final black pigment; but when the amino group of tyrosine is combined with leucine, added beta-alanine produces stable tan pigments. 4. With L-alanine substituted for beta-alanine in this reaction, green pigment results. 5. Gelatin filters stained with the tan pigment allow solar heating of underlaying water more quickly than do those stained with the black pigment. Unstained filters allow such heating even more quickly. 6. Beta-alanine enhances production of tan pigment when heated with the phospholipid, lecithin. Implications for pigmentary adaptation, and formation of lipofuscin-like age pigments are discussed.
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PMID:Beta-alanine and tanning polymorphisms. 681 Nov 92

The effect of continuous treatments of single L-amino acids (0.1mM) on the free running rhythm from the isolated Aplysia eye was examined. A variation in the change in free running period produced by different amino acids was observed. Two well-known precursors of neurotransmitters (tyrosine, tryptophan) had the largest effects. These amino acids lengthened the period ca. 1.7 h. Another group of amino acids (alanine, threonine, proline) lengthened the period by about 1 h. Smaller effects were produced by aspartic acid and leucine and no effects were caused by lysine, glycine, valine, and serine. Phenylalanine may shorten the period a small amount. Glucose (5mM) lengthens the period a small amount (0.4 h), decreases the effect of tyrosine somewhat, and has no effect on the lengthening of the period produced by tryptophan. Three amino acids not involved in protein synthesis (ornithine, beta-alanine, citrulline) had at most small effects on the free running period. Also, D-tryptophan lengthened the period by 0.6 h but the effect of D-tryptophan was considerably smaller than the effect of L-tryptophan. A few of the amino acids had small short-term effects on spike rate and longer-term effects on the amplitudes of the rhythms but these effects did not correlate with the effects of the amino acids on the free running period. Though continuous treatments of certain amino acids lengthened the periods, shorter treatments (tryptophan, 6 h) did not phase-shift the rhythm. Since eyes maintained in a commonly used culture medium have longer periods than eyes in a simple seawater medium, the amino acids of the culture medium must be responsible, at least in part, for the lengthening effect of the culture medium. The mechanism of action of the amino acids is unknown. The magnitude of the effects did not correlate with physical-chemical properties of the amino acids nor with whether the amino acids were "essential" or "nonessential." The effects of the amino acids may be mediated by their effects on neurotransmitter and/or protein synthesis.
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PMID:Differential effects of amino acids on the period of the circadian rhythm from the Aplysia eye. 707 20

Characteristics of taurine (2-aminoethanesulfonic acid) transport were studied in freshly isolated rat hepatocytes prepared by a collagenase perfusion technique. The uptake of taurine at 37 degrees C was linear up to 30 min of incubation, but gradually decreased thereafter and reached a plateau at 90 min after initiation of the incubation. Taurine uptake at 4 degrees C by isolated hepatocytes was not saturable, whereas that at 37 degrees C was saturable with the following parameters: Km, 37 microM; Vmax, 0.043 nmoles/mg prot./min; and EA, 5.6 Kcal/mol. The taurine uptake at 37 degrees C was found to be sodium dependent, and this was inhibited competitively by guanidinoethyl sulfonate and beta-alanine with the Ki values of 1.75 mM and 285 microM, respectively. Conjugated cholate, conjugated chenodeoxycholate, alanine, isethionate and leucine had no effect on the taurine uptake. The present results indicate that taurine uptake by isolated hepatocytes consists of unsaturable and energy independent, and carrier-mediated and energy dependent transport processes.
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PMID:Characteristics of taurine transport in freshly isolated rat hepatocytes. 733 29


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