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Chemical Compound Review

CTK1J6062     (2R)-2-[[(2S)-2-amino-4- methylsulfanyl...

Synonyms: AC1O532D, 656811-60-8, D-Serine, L-methionyl-
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Disease relevance of Met-Ser

  • However, characteristic and abnormally intense resonances for the amino acids Phe, Tyr, His, Gln, Pro, Ala, Val, Lys, Met, Ser, and Thr are indicative of severe liver failure and disruption of normal deamination and transamination processes [1].
  • A number of other tRNAs (Met, Ser, Glu, Lys and Leu-specific tRNAs both from yeast and Escherichia coli) are also inactivated by epsilon A incorporation [2].

High impact information on Met-Ser

  • However, replacement of both P1 and P1' by Met-Ser produced a variant with no detectable plasminogen activator inhibitor activity [3].
  • There are 29 tRNA species: three for Leu, two each for Arg, Ile, Lys, Met, Ser, Thr and Trp, and one each for the other 12 amino acids as judged from aminoacylation and the anticodon nucleotide sequences [4].
  • Conversion of this bond in alpha(1)-PI from Met-Ser to Arg-Ser in alpha(1)-PI Pittsburgh (M358R) redirects alpha(1)-PI from inhibiting NE to inhibiting thrombin (IIa), activated protein C (APC), and other proteases [5].
  • The reactive center sequence of rat alpha 1-antitrypsin is highly conserved with respect to human alpha 1-antitrypsin, both having Met-Ser at the P1 and P1' residues [6].
  • The uptake was inhibited by > 50% in the presence of a 10-fold excess of His, homocysteine (Hcy), Trp, Leu, Tyr, Ile, Thr, Ala, Phe, Met, Ser, by > 20% in the presence of a 10-fold excess of Val, Arg, Glu, and was not affected by a 10-fold excess of Orn, alpha-ketoglutarate, Tau and Pro [7].

Biological context of Met-Ser

  • The signal peptide sequence is well conserved in the related gene, but the active site for protease inhibition of Met-Ser in alpha 1-antitrypsin has been changed to Trp-Ser [8].
  • The mutant enzymes containing Glu, Gly, Met, Ser, or Tyr at position 130, as well as the wild-type human GDH encoded by the synthetic gene, were efficiently expressed as a soluble protein and are indistinguishable from that isolated from human and bovine tissues [9].
  • The amino acid primary structure deduced from the open reading frame is identical with the protein sequence reported for yeast adenylate kinase (Tomasselli et al. 1986) with the exception of an extension of two amino acids (Met-Ser) at the N-terminus and aspartic acid instead of asparagine at the carboxyl end [10].

Associations of Met-Ser with other chemical compounds

  • Each subject received a 3-h intravenous infusion according to one of the following protocols: study 1, gluconeogenic amino acids (Arg, Gly, Pro, Cys, Met, Ser); study 2, alanine alone; study 3, branched-chain amino acids (BCAA, Leu, Ile, Val); or study 4, 0.9% saline [11].

Gene context of Met-Ser

  • In spite of more than 86% overall aa sequence identity among the five chipmunk alpha1-AT-like proteins, they are highly divergent in the putative reactive center region; the putative P1-P1' sequences are Met-Leu (HP-55 or CM55-ML), Met-Met (CM55-MM), Met-Ser (CM55-MS), Ser-Ile (CM55-SI) and Ser-Thr (CM55-ST) [12].


  1. Metabolic profiling of body fluids by proton NMR: self-poisoning episodes with paracetamol (acetaminophen). Bales, J.R., Bell, J.D., Nicholson, J.K., Sadler, P.J., Timbrell, J.A., Hughes, R.D., Bennett, P.N., Williams, R. Magnetic resonance in medicine : official journal of the Society of Magnetic Resonance in Medicine / Society of Magnetic Resonance in Medicine. (1988) [Pubmed]
  2. Incorporation of 1,N6-ethenoadenosine into the 3' terminus of tRNA using T4 RNA ligase. 1. Preparation of yeast tRNAPhe derivatives. Paulsen, H., Wintermeyer, W. Eur. J. Biochem. (1984) [Pubmed]
  3. Mutational and immunochemical analysis of plasminogen activator inhibitor 1. Shubeita, H.E., Cottey, T.L., Franke, A.E., Gerard, R.D. J. Biol. Chem. (1990) [Pubmed]
  4. Codon recognition patterns as deduced from sequences of the complete set of transfer RNA species in Mycoplasma capricolum. Resemblance to mitochondria. Andachi, Y., Yamao, F., Muto, A., Osawa, S. J. Mol. Biol. (1989) [Pubmed]
  5. Full or partial substitution of the reactive center loop of alpha-1-proteinase inhibitor by that of heparin cofactor II: P1 Arg is required for maximal thrombin inhibition. Filion, M.L., Bhakta, V., Nguyen, L.H., Liaw, P.S., Sheffield, W.P. Biochemistry (2004) [Pubmed]
  6. Molecular cloning and primary structure of rat alpha 1-antitrypsin. Chao, S., Chai, K.X., Chao, L., Chao, J. Biochemistry (1990) [Pubmed]
  7. Modulation of glutamine uptake and phosphate-activated glutaminase activity in rat brain mitochondria by amino acids and their synthetic analogues. Albrecht, J., Dolińska, M., Hilgier, W., Lipkowski, A.W., Nowacki, J. Neurochem. Int. (2000) [Pubmed]
  8. Molecular structure and sequence homology of a gene related to alpha 1-antitrypsin in the human genome. Bao, J.J., Reed-Fourquet, L., Sifers, R.N., Kidd, V.J., Woo, S.L. Genomics (1988) [Pubmed]
  9. Cassette mutagenesis of lysine 130 of human glutamate dehydrogenase. An essential residue in catalysis. Cho, S.W., Yoon, H.Y., Ahn, J.Y., Lee, E.Y., Lee, J. Eur. J. Biochem. (2001) [Pubmed]
  10. The complete nucleotide sequence of the gene coding for yeast adenylate kinase. Magdolen, V., Oechsner, U., Bandlow, W. Curr. Genet. (1987) [Pubmed]
  11. Effect of specific amino acid groups on renal hemodynamics in humans. Castellino, P., Levin, R., Shohat, J., DeFronzo, R.A. Am. J. Physiol. (1990) [Pubmed]
  12. Expression of multiple alpha1-antitrypsin-like genes in hibernating species of the squirrel family. Takamatsu, N., Kojima, M., Taniyama, M., Ohba, K., Uematsu, T., Segawa, C., Tsutou, S., Watanabe, M., Kondo, J., Kondo, N., Shiba, T. Gene (1997) [Pubmed]
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