Disease relevance of Leu-Val

• Recombinant human myoglobin mutants with the distal His residue (E7, His64) replaced by Leu, Val, or Gln residues were prepared by site-directed mutagenesis and expression in Escherichia coli [1].
• Sequence analysis of two DNA fragments generated from bacteriophage T5 DNA by restriction with Hpa I and Hae III has resulted in the detection and localization of nine tRNA genes (His, two Ser genes, Leu, Val, Lys, fMet, Pro, and Ile) [2].
• RESULTS: CYP1A1 codon 462 Ile/Val or Val/Val variants and the CYP1B1 codon 432 Leu/Val variant were found more in breast cancer patients </=35 years of age at onset than the common homozygote [odds ratio (OR), 1.6 and 1.7, respectively] [3].
• Seven depsipeptides were synthesized by appending seven amino acids (Lys, Leu, Val, Phe, Ser, Gln, and Pro) at the N-terminus of the active fragment [TE-(33-43)], respectively corresponding to the C-terminal beta sheet domain of tenecin 1, an antibacterial protein and their activities were measured against Staphylococcus aureus [4].
• Leu-Val polymorphism of CYP1B1 was not associated with lung cancer risk in our study [5].

High impact information on Leu-Val

• Substitution of Tyr or His for Phe-707, but not Leu, Val, Glu, or Trp, partially restored the ability of high [Ca(2+)](o) to activate PLC [6].
• A di-hydrophobic Leu-Val motif regulates the basolateral localization of CD44 in polarized Madin-Darby canine kidney epithelial cells [7].
• If hydrophobic amino acids (Ile, Leu, Val, Phe, Met) are inserted into the five a positions of a LexA-Fos zipper fusion protein, substantial transcriptional repression is recovered showing that Fos zipper homodimerization is not only limited by the repulsion of negatively charged residues but also by the nonhydrophobic nature of the a positions [8].
• Repression was also caused by specific amino acid substitutions of Leu, Val, or Gly for Lys359, which affected DNA binding [9].
• Using the random effects methods, protective effects were seen with the Leu/Val genotype alone (OR 0.79, 95% CI 0.68-0.93) and with Leu/Val and Leu/Leu genotypes combined (OR 0.79, 95% CI 0.66-0.93) [10].

Chemical compound and disease context of Leu-Val

• Recombinant human myoglobin mutants with the distal histidine residue replaced by Leu, Val, or Gln residues have been prepared by site-directed mutagenesis and expression in Escherichia coli [11].

Biological context of Leu-Val

• These diamines were incorporated into renin inhibitors (IC50 = 4-1500 nM) replacing the Leu-Val scissile bond in small peptide analogues of angiotensinogen [12].
• The difference in the CTGGTG di-codon frequency between the backbone and island genes was correlated with the frequency of Chi sequences which were translated in the Leu-Val (-G|CTG|GTG|G-) reading frame in the K-12 strain [13].
• The prolidase exhibited a narrow substrate specificity and hydrolyzed only dipeptides with proline at the C terminus and a nonpolar amino acid (Met, Leu, Val, Phe, or Ala) at the N terminus [14].
• The contribution of the Leu/Val polymorphism to the total genetic variation of the BASELINE, PEAK, and RATE traits was 5, 30, and 27%, respectively [15].

Anatomical context of Leu-Val

• The present study describes the analysis of the associations between the growth hormone gene polymorphism (Leu/Val) and oocyte maturation and in vitro fertilisation in cattle [16].
• In mature newborn infants, 7 (Ala, Lys, Leu, Val, Ile, Phe and His) of the 20 plasma amino acids were significantly higher and 4 (Glu, Gly, Ser and Orn) were significantly lower in the umbilical vein than in the umbilical artery [17].

Associations of Leu-Val with other chemical compounds

• Cleavage was observed with Abz-MKRLTL-EDDnp, Abz-FRLVR-EDDnp, and Abz-PLGLLGR-EDDnp at Leu-Thr, Leu-Val and Leu-Leu/Leu-Gly bonds respectively as determined by isolation of the corresponding fragments by HPLC [18].
• Sansalvamide A, a cyclic depsipeptide isolated from a marine fungus of the genus Fusarium, is composed of four hydrophobic amino acids (Phe, two Leu, Val) and one hydroxy acid ((S)-2-hydroxy-4-methylpentanoic acid; O-Leu) with five stereogenic centers all having S-stereochemistry [19].
• The synthesis and in vitro renin inhibitory potencies of angiotensinogen (ANG) analogues having amide (CONH) bond replacements at P1-P1', the Leu-Val cleavage site, corresponding to Leu psi[CH2SO]Val, and the trans olefinic analogue of statine (Sta), 4(S)-amino-6-methyl-2(E)-heptenoic acid (dehydrostatine, Dhs), are reported [20].
• The current study determines the chemical shift effects of pH, urea, peptide length and neighboring amino acids on the alpha-proton of Ala using model peptides of the general sequence G(n)X(aa)AY(aa)G(n), where X(aa) and Y(aa) are Leu, Val, Phe, Tyr, His, Trp or Pro, and n = 1-3 [21].
• Eight groups of rats received an enteral modular diet supplemented with different amino acids (Group 1: Ile, Leu, Val; Group 2: Phe, Met, Gly; Group 3: Glu, Arg, Gly; Group 4: Gly, Group 5: Orn-Asp, Cys, Pro; Group 6: Lys, Ser, Thr; Group 7: Tyr, His, Ala) [22].

Gene context of Leu-Val

• New inhibitors of human renin that contain novel Leu-Val replacements. Examination of the P1 site [23].
• New inhibitors of renin that contain novel phosphostatine Leu-Val replacements [24].
• Optimization and in vivo evaluations of a series of small, potent, and specific renin inhibitors containing a novel Leu-Val replacement [25].
• Derivatives were successfully obtained with both neutral (Leu, Val, Ala, Ile, Trp, Tyr, Gly) and one acidic (Glu) amino acids [26].
• The ratio of plasma Trp to the sum of Leu, Val, Ile, Phe, Met and Tyr is increased in the Li-treated rats but not significantly [27].

References