A stable adenosine A1 and A2 receptor agonist. Experimentally, it inhibits cAMP and cGMP phosphodiesterase activity.

An autolytic enzyme bound to the surface of bacterial cell walls. It catalyzes the hydrolysis of the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell wall glycopeptides, particularly peptidoglycan. EC 3.5.1.28.

An N-acyl derivative of neuraminic acid. N-acetylneuraminic acid occurs in many polysaccharides, glycoproteins, and glycolipids in animals and bacteria. (From Dorland, 28th ed, p1518)

An enzyme isolated from the nuclei of a variety of cells. It catalyzes the incorporation of ADP-ribose groups of NAD+ into a homopolymer of repeating ADP-ribose units. EC 2.4.2.30.

An enzyme that catalyzes the transfer of the ADP-ribose moiety from NAD to specific protein substrates with agmatine, arginine-type compounds, or guanidine as acceptors. This reaction can be catalyzed by prokaryotic and eukaryotic enzyme systems. Mono-ADP-ribosylation is a mechanism of action common to several bacterial toxins. It effects profound changes in cellular metabolism, such as activation of adenylate cyclase, regulation of protein synthesis at the level of elongation factor 2, and ion transport across biological membranes. EC 2.4.2.31.

An enzyme that catalyzes the transfer of the ADP-ribose moiety from NAD to specific protein substrates with agmatine, arginine-type compounds, or guanidine as acceptors. This reaction can be catalyzed by prokaryotic and eukaryotic enzyme systems. Mono-ADP-ribosylation is a mechanism of action common to several bacterial toxins. It effects profound changes in cellular metabolism, such as activation of adenylate cyclase, regulation of protein synthesis at the level of elongation factor 2, and ion transport across biological membranes. EC 2.4.2.31.

An enzyme that catalyzes the transfer of the ADP-ribose moiety from NAD to specific protein substrates with agmatine, arginine-type compounds, or guanidine as acceptors. This reaction can be catalyzed by prokaryotic and eukaryotic enzyme systems. Mono-ADP-ribosylation is a mechanism of action common to several bacterial toxins. It effects profound changes in cellular metabolism, such as activation of adenylate cyclase, regulation of protein synthesis at the level of elongation factor 2, and ion transport across biological membranes. EC 2.4.2.31.

An enzyme that catalyzes the transfer of the ADP-ribose moiety from NAD to specific protein substrates with agmatine, arginine-type compounds, or guanidine as acceptors. This reaction can be catalyzed by prokaryotic and eukaryotic enzyme systems. Mono-ADP-ribosylation is a mechanism of action common to several bacterial toxins. It effects profound changes in cellular metabolism, such as activation of adenylate cyclase, regulation of protein synthesis at the level of elongation factor 2, and ion transport across biological membranes. EC 2.4.2.31.

A peroxisome proliferator that is used experimentally to promote liver tumors. It has been used as an antihyperlipoproteinemic agent.

A synthetic 1,8-naphthyridine antimicrobial agent with a limited bacteriocidal spectrum. It is an inhibitor of the A subunit of bacterial DNA gyrase.