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Identification of an arginine residue important for catalytic activity in the primary structure of D-glyceraldehyde 3-phosphate dehydrogenase. Studies with the rat skeletal-muscle enzyme.

  • N D Vospelnikova
  • M I Safronova
  • E R Shuvalova
  • L A Baratova
  • S P Kniazev
  • N K Nagradova
Publication Date
Dec 01, 1981
  • Biology


The reaction of holo-(D-glyceraldehyde 3-phosphate dehydrogenase) (EC from rat skeletal muscle with [14C]butanedione in 0.05 M-NH4HCO3, pH 8.0, resulted in modification (*) of two arginine residues per subunit with a concomitant loss of catalytic activity. From a tryptic digest of the modified protein two radiolabelled peptides were isolated, with the following sequences: (1)Val-Ile-Ile-Asn-Ala-Pro-Thr-Ala-Asp-Ala(Glx,Met,Leu,Phe,Met)Gly-Val-Asx-Arg- Glx(His,Tyr)Ser-Lys and (2) Asp-Ala-Gly-Ala-Thr-Ile-Ala-Leu(Asx,Glx,Arg,Phe,Val)Lys. By comparison of the data with the known sequences of homologous enzymes, the localization of the modified residues was established. The first peptide was identified as corresponding to residues 116--139, the second to residues 293--306. Experimental evidence from this and previous studies suggests that arginine-134 is important for the catalytic activity of the rat muscle enzyme, being involved in structural rearrangements accompanying the organization of the active centre on the binding of coenzyme and substrate.

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