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


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.


Nitrogen Histamine Amino Acid Residue Nitrogen Atom Purine 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


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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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