Binding capacities of various analogues of S-adenosyl-L-homocysteine to protein methyltransferase II from human erythrocytes

L Gillet; Y Looze; M Deconinck; J Léonis

doi:10.1007/BF01949909

Binding capacities of various analogues of S-adenosyl-L-homocysteine to protein methyltransferase II from human erythrocytes

Experientia. 1979 Aug 15;35(8):1007-9. doi: 10.1007/BF01949909.

Authors

L Gillet, Y Looze, M Deconinck, J Léonis

PMID: 477857
DOI: 10.1007/BF01949909

Abstract

A series of analogues of S-adenosyl-L-homocysteine, modified mainly in the amino acid portion of the molecule, have been synthesized. All were found to be competitive inhibitors of protein methyltransferase II from human erythrocytes. S-adenosyl-L-homocysteine remains however by far the most effective inhibitor of the methylase.

MeSH terms

Erythrocytes / enzymology*
Homocysteine / analogs & derivatives*
Humans
Protein Binding
Protein Methyltransferases / blood*
Protein O-Methyltransferase / blood*
S-Adenosylhomocysteine / analogs & derivatives*
S-Adenosylhomocysteine / metabolism
Structure-Activity Relationship

Substances

Homocysteine
S-Adenosylhomocysteine
Protein Methyltransferases
Protein O-Methyltransferase