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].

References