Disease relevance of alpha-L-Aminopentanoic acid

• Incorporation of norvaline at leucine positions in recombinant human hemoglobin expressed in Escherichia coli [1].
• The assay procedure has been applied to the enzymic conversion of racemic norvaline amide into L-norvaline, catalysed by an L-specific aminopeptidase from Pseudomonas putida [2].
• Crystallization of Arthrobacter sp. strain 1C N-(1-D-carboxyethyl)-L- norvaline dehydrogenase and its complex with NAD+ [3].
• Norvaline accumulation by regulatory mutants of Serratia marcescens [4].
• Properties of some norvaline-resistant mutants of Bacillus subtilis [5].

High impact information on alpha-L-Aminopentanoic acid

• This proliferative effect was down-regulated by the arginase inhibitor L-norvaline [6].
• Finally, IL-13 significantly inhibited NO production from LPS-activated macrophages, and this effect was reversed by an arginase inhibitor, L-norvaline [7].
• The level of misincorporation correlated with the ratio of the free norvaline/leucine pool available in the cell culture [1].
• This suggests that the incorporation of norvaline for leucine occurs through misaminoacylation of tRNALeu, similar to the misincorporation of norleucine for methionine found in many recombinant proteins expressed in E. coli [1].
• The second substrate, NFF-2 (Mca-Arg-Pro-Lys-Pro-Tyr-Ala-Nva-Trp-Met-Lys(Dnp)-NH2, where Nva is norvaline), was hydrolyzed 60 times more rapidly by MMP-3 (kcat/Km = 59,400 s-1 M-1) than MMP-1 [8].

Chemical compound and disease context of alpha-L-Aminopentanoic acid

• The effects of these amino acids singly or in combinations and the amino acids norleucine and norvaline on the growth of porcine E. coli were studied [9].

Biological context of alpha-L-Aminopentanoic acid

• The enzyme catalyzes the oxidative deamination of L-leucine, L-valine, L-isoleucine, L-norvaline, L-alpha-aminobutyrate, and L-norleucine, and the reductive amination of their keto analogues [10].
• The enzyme catalyses the oxidative deamination of L-valine, L-leucine, L-2-aminobutyric acid, L-norvaline and L-isoleucine, as well as the reductive amination of their 2-oxo analogues [11].
• Lineweaver-Burk plots with varied norvaline concentration are not strictly linear, and it is concluded that a steady-state random-order model more accurately reflects the observed kinetics with norvaline as substrate [12].
• The analogues having a Phe residue in place of Val1 (X) and His or amino acid with an aliphatic side chain such as norleucine or norvaline in the Y position showed the highest inhibition of human plasma renin activity with IC50 values of about 10(-8)M [13].
• The molecular conformation and packing features show a striking resemblance to those for D-Ala-L-Met (1), and leads to the speculation that norvaline might act as an analog of methionine [14].

Anatomical context of alpha-L-Aminopentanoic acid

• To alter arginase activity in macrophages, cells (murine macrophage cell line J774A.1) were transfected with the rat liver arginase gene or treated with an arginase inhibitor, L-norvaline [6].
• Inoculation of the very virulent strain of MDV RB-1B induced strong and long-lasting arginase macrophage-dependent activity, which was inhibited by L-norvaline in vitro, but induced low NO production in monocytes and splenocytes from highly susceptible B(13)/B(13) chickens [15].
• TRH analogues containing C-terminal tioamide group and norvaline ([Nva2, Prot3] TRH) or norleucine ([Nle2, Prot3] TRH) in position 2 were synthesized and tested for hormonal and central nervous system (CNS) activities [16].

Associations of alpha-L-Aminopentanoic acid with other chemical compounds

• The ornithine transcarbamoylase catalyzed reaction and its inhibition by L-norvaline have been investigated between pH 5.5 and 10 [17].
• Hydrophobicity of the p4 residues also modulates thymocyte fate: the positively selecting norvaline and leucine variants have one and two Cgamma-methyl groups, respectively, while the weakly selecting gamma-methylleucine p4 contains three Cgamma-methyl groups [18].
• Development of cytotoxicity by irradiated cells is completely prevented with the arginase inhibitor L-norvaline, in arginine-deficient medium or when citrulline replaces arginine [19].
• Both the induction and the long-term expression of the epileptiform associative potential were dependent on the activation of glutamatergic receptors of the NMDA type, as demonstrated by perfusion with the NMDA receptor antagonist 2-aminopentanoic acid (AP5) (100 microM) [20].
• Crystal structure of human ornithine transcarbamylase complexed with carbamoyl phosphate and L-norvaline at 1.9 A resolution [21].

Gene context of alpha-L-Aminopentanoic acid

• The crystal structure of human ornithine transcarbamylase (OTCase) complexed with carbamoyl phosphate (CP) and L-norvaline (NOR) has been determined to 1.9-A resolution [21].
• On the other hand, pretreatment with cycloheximide in an artificial model of OTC deficiency (Swiss-ICR normal mice on an arginine-deficient diet treated thereafter with norvaline, an inhibitor of OTC), caused a significant decrease in urinary orotate [22].
• A steady-state random-order mechanism for the oxidative deamination of norvaline by glutamate dehydrogenase [12].
• For control purposes, norvaline, and amino acid structurally related to AP5, was administered to a second group of animals (n = 7) in a quantity (2.25 mg/injection/rat; approx. 8.2 mg/kg BW/injection) equimolar to that of the NMDA receptor antagonist [23].
• Addition of L-norvaline, an inhibitor of arginase, rescued cells from arginase-induced deprivation [24].

Analytical, diagnostic and therapeutic context of alpha-L-Aminopentanoic acid

• The presence of the norvaline was confirmed by several analytical methods such as amino acid analysis, peptide mapping, electrospray mass spectrometry, and Edman protein sequencing [1].
• Behavioral and electrophysiological (EOG) experiments indicated that the difference in relative stimulatory effectiveness levels between NVAL and PRO is > 30,000 times [25].

References