dimethyloxalylglycine and oxalylglycine

dimethyloxalylglycine has been researched along with oxalylglycine* in 2 studies

Other Studies

2 other study(ies) available for dimethyloxalylglycine and oxalylglycine

Article	Year
Synthesis and activity of N-oxalylglycine and its derivatives as Jumonji C-domain-containing histone lysine demethylase inhibitors. Bioorganic & medicinal chemistry letters, 2009, May-15, Volume: 19, Issue:10 N-Oxalylglycine (NOG) derivatives were synthesized, and their inhibitory effect on histone lysine demethylase activity was evaluated. NOG and compound 1 inhibited histone lysine demethylases JMJD2A, 2C and 2D in enzyme assays, and their dimethyl ester prodrugs DMOG and 21 exerted histone lysine methylating activity in cellular assays. Topics: Amino Acids, Dicarboxylic; Cell Line; Enzyme Inhibitors; Humans; Jumonji Domain-Containing Histone Demethylases; Neoplasm Proteins; Oxidoreductases, N-Demethylating; Transcription Factors	2009
Novel inhibitors of prolyl 4-hydroxylase. 3. Inhibition by the substrate analogue N-oxaloglycine and its derivatives. Journal of medicinal chemistry, 1992, Jul-10, Volume: 35, Issue:14 N-Oxaloglycine (3) is an alpha-ketoglutarate (1) analogue that is a competitive inhibitor of prolyl 4-hydroxylase (EC 1.14.11.2). A study of the structure-activity relationships of some other oxalo derivatives shows that substitution on the glycine moiety modulates activity stereoselectively and that if the omega-carboxylate is homologated or replaced by either acylsulfonamides or anilide, then activity is sharply reduced. This sensitivity to these changes is contrasted with the relative insensitivity of another putative alpha-ketoglutarate analogue, pyridine-2,5-dicarboxylic acid (2), and the implication is discussed that compounds of both series are unlikely to bind to prolyl hydroxylase in the same way even though both inhibit the enzyme competitively. Topics: Amino Acid Sequence; Amino Acids, Dicarboxylic; Binding, Competitive; Molecular Sequence Data; Procollagen-Proline Dioxygenase; Structure-Activity Relationship; Substrate Specificity	1992

Article

Year

Synthesis and activity of N-oxalylglycine and its derivatives as Jumonji C-domain-containing histone lysine demethylase inhibitors.

Bioorganic & medicinal chemistry letters, 2009, May-15, Volume: 19, Issue:10

N-Oxalylglycine (NOG) derivatives were synthesized, and their inhibitory effect on histone lysine demethylase activity was evaluated. NOG and compound 1 inhibited histone lysine demethylases JMJD2A, 2C and 2D in enzyme assays, and their dimethyl ester prodrugs DMOG and 21 exerted histone lysine methylating activity in cellular assays.

Topics: Amino Acids, Dicarboxylic; Cell Line; Enzyme Inhibitors; Humans; Jumonji Domain-Containing Histone Demethylases; Neoplasm Proteins; Oxidoreductases, N-Demethylating; Transcription Factors

2009

Novel inhibitors of prolyl 4-hydroxylase. 3. Inhibition by the substrate analogue N-oxaloglycine and its derivatives.

Journal of medicinal chemistry, 1992, Jul-10, Volume: 35, Issue:14

N-Oxaloglycine (3) is an alpha-ketoglutarate (1) analogue that is a competitive inhibitor of prolyl 4-hydroxylase (EC 1.14.11.2). A study of the structure-activity relationships of some other oxalo derivatives shows that substitution on the glycine moiety modulates activity stereoselectively and that if the omega-carboxylate is homologated or replaced by either acylsulfonamides or anilide, then activity is sharply reduced. This sensitivity to these changes is contrasted with the relative insensitivity of another putative alpha-ketoglutarate analogue, pyridine-2,5-dicarboxylic acid (2), and the implication is discussed that compounds of both series are unlikely to bind to prolyl hydroxylase in the same way even though both inhibit the enzyme competitively.

Topics: Amino Acid Sequence; Amino Acids, Dicarboxylic; Binding, Competitive; Molecular Sequence Data; Procollagen-Proline Dioxygenase; Structure-Activity Relationship; Substrate Specificity

1992