PubMed Health⌕ Search

SEARCH · PubMed Health

Results for “GLUTAMIC ACID”

Explore indexed PubMed citations for clinical trials, systematic reviews and public health research. Read source abstracts and follow each citation to its original PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 109 records · Page 6Linked to original sources
PubMed1984

[Effect of glutamic acid content of the diet on the catabolic rate of isotope-labeled glutamic acid in rats. 3. Determination of 14CO2 and 15N excretion following intragastric infusion of 14C- and 15N-glutamic acid].

Male rats (body weight 100 g) received during a 8 days experimental feeding period diets with different contents in glutamic acid. The daily feed intake was restricted to the energy maintenance level of 460 kJ/kg0.75. The diet contained a mixture of L-amino acids corresponding to the pattern of egg protein except glutamic acid. Glutamic acid was added successively at 10 levels (0 to 14,8% of dry matter) and the resulting diets were fed to groups of 4 animals each. At the end of the experimental feeding period 14C- and 15N-labelled glutamic acid were applied by intragastric infusion. CO2- and 14CO2-excretion was measured during the following 4 hours and the urinary N- and 15N-excretion during the following 24 hours. The CO2-excretion decreased from 53 to 44 mmol CO2/100 g body weight with increasing levels of dietary glutamic acid. This change seems to result from the increasing proportion of amino acids as an energetic fuel. While the amount of oxidized glutamic acid increased with increasing supplements of glutamic acid the relative 14CO2-excretion decreased from 57 to 48% of the applied radioactivity. The urinary 15N-excretion during 24 hours was 31% of the given amount of 15N if no glutamic acid was included in the diet. This proportion increased successively up to 52% in the case of the highest supply of glutamic acid. Because the total N-excretion increased at the same extent as the 15N-excretion a complete mixing of the NH2-groups resulting from glutamic acid due to desamination with the ammonia pool was assumed. No correlation between glutamic acid content of the diet and specific radioactivity of CO2 or atom-% 15N excess of urinary N was observed.

Animal Feed↗
PubMed2003

Alteration in catalytic properties of human CYP2D6 caused by substitution of glycine-42 with arginine, lysine and glutamic acid.

The effects of the substitution of glycine at position 42 with various other amino acid residues on the functions of CYP2D6 were studied using debrisoquine (DB) and bunitrolol (BTL) 4-hydroxylations as indices of drug-metabolizing enzymes. The substitution with hydrophobic amino acid residues such as valine and phenylalanine did not affect the enzymatic properties such as reduced CO-difference spectra, microsomal CYP contents and oxidation activities towards DB and BTL. The substitution of glycine-42 with a polar but noncharged amino acid residue (serine) exhibited a similar reduced CO-different spectrum, but the substitution with a charged basic (lysine and arginine) or acidic (glutamic acid) amino acid residue commonly produced a peak at 420 nm in addition to a Soret peak at 450 nm. Cytochrome P450 contents and microsomal contents of G42S, G42K, G42R and G42E estimated spectrophotometrically and estimated by Western blot analysis, respectively, were lower than those of the wild-type. Kinetic analysis revealed that the substitution of glycine-42 with charged amino acid residues such as lysine, arginine and glutamic acid markedly increased the apparent K(m) values for DB and BTL oxidations without remarkable changes in the V(max) values. The subsitution with noncharged amino acid residues such as serine, valine and phenylalanine did not cause such a marked change in the K(m) values. Efficiencies (V(max)/K(m)) as DB and BTL 4-hydroxylases of CYP2D6 mutant proteins having charged amino acid residues were found to be decreased mainly by increasing their K(m) values. These results indicate that the properties of amino acid residues at position 42 affect the behavior of CYP2D6 proteins such as anchoring into ER membranes, conversion of P450 to P420 and incorporation of heme into apoproteins.

Journal Article↗
PubMed2004

Substitution of aspartic acid with glutamic acid increases the unfolding transition temperature of a protein.

Proteins from thermophiles are more stable than those from mesophiles. Several factors have been suggested as causes for this greater stability, but no general rule has been found. The amino acid composition of thermophile proteins indicates that the content of polar amino acids such as Asn, Gln, Ser, and Thr is lower, and that of charged amino acids such as Arg, Glu, and Lys is higher than in mesophile proteins. Among charged amino acids, however, the content of Asp is even lower in thermophile proteins than in mesophile proteins. To investigate the reasons for the lower occurrence of Asp compared to Glu in thermophile proteins, Glu was substituted with Asp in a hyperthermophile protein, MjTRX, and Asp was substituted with Glu in a mesophile protein, ETRX. Each substitution of Glu with Asp decreased the Tm of MjTRX by about 2 degrees C, while each substitution of Asp with Glu increased the Tm of ETRX by about 1.5 degrees C. The change of Tm destabilizes the MjTRX by 0.55 kcal/mol and stabilizes the ETRX by 0.45 kcal/mol in free energy.

Amino Acid Sequence↗
PubMed1993

Site-directed mutagenesis of histidine 93, aspartic acid 180, glutamic acid 205, histidine 290, and aspartic acid 291 at the active site and tryptophan 279 at the raw starch binding site in barley alpha-amylase 1.

The pseudotetrasaccharide acarbose has high affinity for the active site (Ki,app = 1 microM) and low affinity for a secondary site (Kd = 2.3 mM) in barley alpha-amylase 1, distinguished by inhibition kinetics and spectral perturbation. Mutants of putative catalytic residues, D180N, E205Q, and D291N, are inactive and display low affinity for acarbose-Sepharose. H93N and H290N mutants, at invariant residues, have kcat/Km for p-nitrophenylmaltoheptaoside of 0.3 and 1.2% of wild-type. A corresponding 370- and 85-fold increased Ki,app for acarbose and a lack of shifts in pH activity profiles indicate that these histidines participate in transition state stabilization but not directly in catalysis. This finding agrees with H bonding to OH groups of the valienamine ring of acarbose in the three-dimensional structure. Loss of inhibition above pH 6 supports that acarbose is most potent in protonated form. The low affinity site contains Trp278 and Trp279, known to bind cyclomaltoheptaose. While the W279A mutant has 10-fold decreased affinity for starch granules, production of Trp278 mutants failed. The invariant Trp278 is perhaps critical for stability or folding in cereal alpha-amylases.

Amino Acid Sequence↗
PubMed1994

Mutagenesis of the conserved aspartic acid 443, glutamic acid 478, asparagine 494, and aspartic acid 498 residues in the ribonuclease H domain of p66/p51 human immunodeficiency virus type I reverse transcriptase. Expression and biochemical analysis.

The effects of point mutations of the conserved Asp443, Glu478, Asn494, and Asp498 residues in the RNase H domain of human immunodeficiency virus type I (HIV-1) reverse transcriptase (RT) have been analyzed. The mutants fell into two classes: (i) functional RT, but not detectable ribonuclease H activity, and (ii) uncharacterizable phenotype due to protein instability in the context of the RT/protease Escherichia coli co-expression system (Mizrahi, V., Lazarus, G. M., Miles, L. M., Meyers, C. A., and Debouck, C. (1989) Arch. Biochem. Biophys. 273, 347-358). The only mutation in the former class was D443A, whereas those in the latter included D443E, E478D, E478Q, D498E, D443A/D498N, D443E/D498N, D443Q/D498N, N494A, N494D, and N494Q. The results were interpreted in terms of the x-ray crystal structure of the HIV-1 RNase H domain (Davies, J. F., II, Hostomaska, Z., Hostomsky, Z., Jordan, S. R., and Matthews, D. A. (1991) Science 252, 88-95) and a general acid-general base hydrolysis mechanism (Katayanagi, K., Okumura, M., and Morikawa, K. (1993) Proteins Struct. Funct. Genet. 17, 337-346). The data suggested that structural perturbations within the RNase H domain interfered with maturation of the pol precursor by HIV-1 protease. Analysis of selected D443/D498 double mutants suggested that the destabilization caused by the D498N mutation could be suppressed by the formation of a new hydrogen bond between Asn498 and Asn443.

Amino Acid Sequence↗
PubMed1982

Presence of gamma-aminobutyric acid and glutamic acid decarboxylase in Auerbach's plexus of cat colon.

Regional distributions of endogenous gamma-aminobutyric acid (GABA) and ganglion cells in Auerbach's plexus were studied in the gastrointestinal tract of cats. GABA was determined by enzymatic and fluorometric assay. There was a positive correlation between the GABA content and the number of cells in this plexus. We analyzed the precise localization of GABA and glutamic acid-decarboxylase (GAD) in individual layers, mucosa, circular and longitudinal muscles and Auerbach's plexus, from freeze-dried sections of cat colon by the enzymatic cycling method. Both GABA contents and GAD activity in Auerbach's plexus were highest in all 4 layers. Thus, the possibility that GABA is synthesized and localized within Auerbach's plexus has to be considered.

Animals↗