Agents and Actions

, Volume 4, Issue 3, pp 186–188 | Cite as

Speculations about the binding sites of S-adenosyl-l-homocysteine and some of its synthetic analogues to histamine methyltransferase

  • H. Barth
  • I. Niemeyer
  • W. Lorenz
Article

Conclusions

None of the synthetic analogues ofS-adenosyl-l-homocysteine was a more potent inhibitor of the enzyme thanS-adenosyl-l-homocysteine itself. Several requirements very probably had to be fulfilled for inhibition of gastric histamine methyltransferase by compounds similar in structure to S-adenosyl-l-homocysteine: (1) The side chain linked to the 5′-position of ribose must bear an amino acid residue; (2) the chain-length of this residue must be the same as that of homocysteine; (3) the heterocyclic base has to be a purine base with a nucleophilic center at position 6; (4) this nucleophilic center must not be sterically hindered by substitutes; (5) the purine base must have a nitrogen atom in position 3. These requirements indicate, that the binding sites, proposed byZappia et al. [2] for various methyltransferases were identical with those found for the fixation ofS-adenosyl-l-homocysteine or its analogues to histamine methyltransferase.

Keywords

Nitrogen Histamine Amino Acid Residue Nitrogen Atom Purine 

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Copyright information

© Birkhäuser Verlag 1974

Authors and Affiliations

  • H. Barth
    • 1
  • I. Niemeyer
    • 1
  • W. Lorenz
    • 1
  1. 1.Division of Experimental Surgery and Pathological Biochemistry, Department of SurgeryUniversity of MarburgMarburg an der LahnFederal Republic of Germany

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