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Chemical Compound Review

AC1O530W     (2S)-2-[[(2R)-2-amino-3- hydroxy...

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High impact information on Ser-Leu

  • The mutation in this strain maps near the middle of the psbC gene and consists of a 6 bp duplication that creates a Ser-Leu repeat at the end of one transmembrane domain [1].
  • Substitutions of Arg-4 with Ser, Leu, or Glu also produced the RRol phenotype, while Lys substitutions for Arg-1 or Arg-4 did not generate any abnormal phenotypes [2].
  • To confirm the importance of MRP1 Thr(1242) for E(2)17betaG transport and drug resistance, we mutated this residue to Ala, Cys, Ser, Leu, and Lys [3].
  • Class I mutants in which Phe26, Tyr27, and Val43 were substituted with Ser, Leu, and Leu, respectively, bound to enriched preparations of rat placental IGF-II/CIM6-P receptors with apparent equilibrium dissociation constants (Kd(app)) that were only slightly greater, i.e. 0.10, 0.05, and 0.06 nM, than that of rIGF-II (0.04 nM) or hIGF-II (0.03 nM) [4].
  • Eleven amino acid substitutions at Val-121 of human carbonic anhydrase II including Gly, Ala, Ser, Leu, Ile, Lys, and Arg, were constructed by site-directed mutagenesis [5].

Biological context of Ser-Leu


Associations of Ser-Leu with other chemical compounds

  • The polypeptide, designated Morulin Pm, has a molecular weight of 3825 +/- 0.6 and has a simple amino acid composition consisting mainly of TOPA and 6-BrW as well as Ser, Leu, Phe, and Ala [9].

Gene context of Ser-Leu

  • Since residue 68 is known to influence the ligation of small molecules to the heme iron, we constructed H64D/V68X Mb bearing Ala, Ser, Leu, Ile, and Phe at position 68 to improve the oxidation activity [10].
  • A corresponding network is not present in bovine Mc cyt b5 because positions 18, 32, and 47, are occupied by Ser, Leu, and Arg, respectively [11].
  • The second-site mutations were found to be located at several sites within the lactose permease (Pro-28 --> Ser, Leu, or Thr; Phe-29 --> Ser; Ala-50 --> Thr, Cys-154 --> Gly; Cys-234 --> Phe; Gln-241 --> Leu; Phe-261 --> Val; Thr-266 --> Iso; Val-367 --> Glu; and Ala-369 --> Pro) [12].
  • However, biases for Ala and Arg were commonly observed for the histone 3 and histone 4 gene families, and biases for Ser, Leu, and Glu were observed in a gene-specific manner [13].


  1. Nuclear and chloroplast mutations affect the synthesis or stability of the chloroplast psbC gene product in Chlamydomonas reinhardtii. Rochaix, J.D., Kuchka, M., Mayfield, S., Schirmer-Rahire, M., Girard-Bascou, J., Bennoun, P. EMBO J. (1989) [Pubmed]
  2. In vitro mutagenesis of Caenorhabditis elegans cuticle collagens identifies a potential subtilisin-like protease cleavage site and demonstrates that carboxyl domain disulfide bonding is required for normal function but not assembly. Yang, J., Kramer, J.M. Mol. Cell. Biol. (1994) [Pubmed]
  3. Identification of a nonconserved amino acid residue in multidrug resistance protein 1 important for determining substrate specificity: evidence for functional interaction between transmembrane helices 14 and 17. Zhang, D.W., Cole, S.P., Deeley, R.G. J. Biol. Chem. (2001) [Pubmed]
  4. The design, expression, and characterization of human insulin-like growth factor II (IGF-II) mutants specific for either the IGF-II/cation-independent mannose 6-phosphate receptor or IGF-I receptor. Sakano, K., Enjoh, T., Numata, F., Fujiwara, H., Marumoto, Y., Higashihashi, N., Sato, Y., Perdue, J.F., Fujita-Yamaguchi, Y. J. Biol. Chem. (1991) [Pubmed]
  5. Altering the mouth of a hydrophobic pocket. Structure and kinetics of human carbonic anhydrase II mutants at residue Val-121. Nair, S.K., Calderone, T.L., Christianson, D.W., Fierke, C.A. J. Biol. Chem. (1991) [Pubmed]
  6. The enterotoxin of Bacteroides fragilis is a metalloprotease. Moncrief, J.S., Obiso, R., Barroso, L.A., Kling, J.J., Wright, R.L., Van Tassell, R.L., Lyerly, D.M., Wilkins, T.D. Infect. Immun. (1995) [Pubmed]
  7. Polymorphisms in oxidative stress genes and risk for non-Hodgkin lymphoma. Wang, S.S., Davis, S., Cerhan, J.R., Hartge, P., Severson, R.K., Cozen, W., Lan, Q., Welch, R., Chanock, S.J., Rothman, N. Carcinogenesis (2006) [Pubmed]
  8. Oxazole- and imidazole-based Ser-Leu dipeptide mimetics in potent inhibitors of antigen presentation by MHC class II DR molecules. Sarabu, R., Bolin, D.R., Campbell, R., Cooper, J.R., Cox, D., Gaizband, D., Makofske, R., Nagy, Z., Olson, G.L. Drug design and discovery. (2002) [Pubmed]
  9. Morulin Pm: a modified polypeptide containing TOPA and 6-bromotryptophan from the morula cells of the ascidian, Phallusia mammillata. Taylor, S.W., Kammerer, B., Nicholson, G.J., Pusecker, K., Walk, T., Bayer, E., Scippa, S., de Vincentiis, M. Arch. Biochem. Biophys. (1997) [Pubmed]
  10. Molecular engineering of myoglobin: influence of residue 68 on the rate and the enantioselectivity of oxidation reactions catalyzed by H64D/V68X myoglobin. Yang, H.J., Matsui, T., Ozaki, S., Kato, S., Ueno, T., Phillips, G.N., Fukuzumi, S., Watanabe, Y. Biochemistry (2003) [Pubmed]
  11. Probing the differences between rat liver outer mitochondrial membrane cytochrome b5 and microsomal cytochromes b5. Altuve, A., Silchenko, S., Lee, K.H., Kuczera, K., Terzyan, S., Zhang, X., Benson, D.R., Rivera, M. Biochemistry (2001) [Pubmed]
  12. Suppressor analysis of mutations in the loop 2-3 motif of lactose permease: evidence that glycine-64 is an important residue for conformational changes. Jessen-Marshall, A.E., Parker, N.J., Brooker, R.J. J. Bacteriol. (1997) [Pubmed]
  13. Evolutionary change of codon usage for the histone gene family in Drosophila melanogaster and Drosophila hydei. Matsuo, Y. Mol. Phylogenet. Evol. (2000) [Pubmed]
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