High impact information on (E,4S)-4-amino-4-carboxy-2-hydroxy-pent-1-ene-1-diazonium

• The hapten-binding antibodies were screened for binding of the planar Schiff base formed from PLP and D- or L-norleucine by competition enzyme-linked immunosorbent assay [1].
• In the absence of another exogenous nutrient, L-leucine but not L-norleucine stimulates insulin release from rat pancreatic islets, although the corresponding keto acids, 2-ketoisocaproate and 2-ketocaproate, are equally potent secretagogues [2].
• Indeed, in the presence of a suitable activator of glutamate dehydrogenase, L-leucine and L-norleucine stimulate secretion to the same extent [2].
• The insulin secretory potency of L-leucine was less than half of that of the keto acids and L-norleucine did not induce any insulin release by isolated islets and by the perfused pancreas from ob/ob mice [3].
• 2.0A resolution crystal structures of the ternary complexes of human phenylalanine hydroxylase catalytic domain with tetrahydrobiopterin and 3-(2-thienyl)-L-alanine or L-norleucine: substrate specificity and molecular motions related to substrate binding [4].

Biological context of (E,4S)-4-amino-4-carboxy-2-hydroxy-pent-1-ene-1-diazonium

• The crystal structures of the catalytic domain of human phenylalanine hydroxylase (hPheOH) in complex with the physiological cofactor 6(R)-L-erythro-5,6,7,8-tetrahydrobiopterin (BH(4)) and the substrate analogues 3-(2-thienyl)-L-alanine (THA) or L-norleucine (NLE) have been determined at 2.0A resolution [4].
• For L-norvaline, L-norleucine, S-methyl-L-cysteine, and L-methionine, the rate of alpha-hydrogen exchange followed first-order kinetics, but the rate of total beta-hydrogen exchange decreased due to a primary isotope effect at the alpha-position [5].
• The MNT broth consists of 0.5% Trypticase (BBL Microbiology Systems, Cockeysville, Md.), 0.5% yeast extract (Difco Laboratories, Detroit, Mich.), 0.2% L-norleucine, and 0.1% L-tyrosine [6].

Anatomical context of (E,4S)-4-amino-4-carboxy-2-hydroxy-pent-1-ene-1-diazonium

• On the role of branched-chain amino acids in protein turnover of skeletal muscle. Studies in vivo with L-norleucine [7].
• The neutral amino acids L-valine, L-norleucine, and L-alanine and the aliphatic 2-keto acids 2-ketoisovalerate and pyruvate do not stimulate insulin secretion and do not increase 2-ketoglutarate generation in pancreatic B-cell mitochondria [8].

Associations of (E,4S)-4-amino-4-carboxy-2-hydroxy-pent-1-ene-1-diazonium with other chemical compounds

• 2. Islet homogenates catalysed transamination reactions between 3-phenylpyruvate and L-glutamate, L-leucine, L-norleucine or L-valine [9].
• Using solution peptide synthesis, we have made three series of N alpha-formylated homooligopeptides, from the dipeptide to the heptapeptide, derived from L-methionine, L-norleucine, and S-methyl-L-cysteine and related to the chemotactic peptide N alpha-formylmethionylleucylphenylalanine [10].
• In contrast to l-leucine, l-norleucine or l-valine did not enhance insulin release or fluorescence of NAD(P)H [11].
• A new enzyme which catalyzes the transamination of L-norleucine (2-aminohexanoic acid) and L-leucine with 2-oxoglutarate was purified to homogeneity from cells of Candida guilliermondii var. membranaefaciens [12].
• Evidence is presented which shows that with serine hydroxymethyltransferase, L-norleucine is not bound at the same catalytic site as glycine [13].

Gene context of (E,4S)-4-amino-4-carboxy-2-hydroxy-pent-1-ene-1-diazonium

• A modified (Lys28 to L-norleucine) version of the synthetic peptide was also cross-linked, but another modified version (Lys16 to L-norleucine) was very poorly cross-linked, indicating that Lys16 is involved exclusively in the cross-linking of the partial-length peptide catalyzed by transglutaminase [14].
• When L-norleucine was employed as an amino acid supplement, new NE congeners, named NEs NL1 and NL2, were preferentially produced; but the amount of NEs produced was not markedly affected [15].
• Leucine in position B17 of the native molecule was substituted by its D-enantiomer and by L-norleucine, respectively [16].

Analytical, diagnostic and therapeutic context of (E,4S)-4-amino-4-carboxy-2-hydroxy-pent-1-ene-1-diazonium

• In this method for measuring amino acids in urine, serum, and tissue, the amino acids to be assayed and the internal standard, L-norleucine, are converted to phenylthiohydantoins , isolated by organic solvent extraction, separated by reversed-phase "high-pressure" liquid chromatography, and detected by ultraviolet absorbance [17].
• Plasma samples were prepared for analysis by addition of internal standard (L-norleucine) followed by ultrafiltration using disposable centrifugal filtration units [18].

References