PGDH Inhibitors

16,16-Dimethyl-prostaglandin E2 acts as a potent PGDH by selectively binding to active sites on enzymes, altering their conformation and catalytic efficiency. Its unique steric hindrance and functional group orientation enable it to modulate signaling pathways with precision. The compound exhibits a remarkable ability to stabilize transition states, enhancing reaction rates. Furthermore, its amphipathic nature contributes to its interaction with lipid membranes, promoting effective cellular localization and activity.

5-Aminosalicylic acid functions as a PGDH by engaging in specific hydrogen bonding interactions with enzyme residues, which influences substrate affinity and reaction dynamics. Its unique structural features allow for the formation of stable enzyme-substrate complexes, enhancing catalytic turnover. Additionally, the compound's polar functional groups facilitate solvation effects, optimizing its reactivity in aqueous environments and contributing to its role in metabolic pathways.

5-[[4-(ethoxycarbonyl)phenyl]azo]-2-hydroxy-benzeneacetic acid acts as a PGDH through its ability to form π-π stacking interactions with aromatic residues in the enzyme's active site. This compound's azo group introduces unique electronic properties, modulating the enzyme's catalytic efficiency. Its hydrophilic characteristics promote favorable interactions with water molecules, enhancing solubility and reactivity, while its steric configuration influences substrate binding dynamics.

18 β-Glycyrrhetinic Acid functions as a PGDH by engaging in hydrogen bonding with key amino acid residues within the enzyme's active site, facilitating substrate orientation. Its triterpenoid structure allows for unique hydrophobic interactions, stabilizing enzyme-substrate complexes. The compound's conformational flexibility enhances its ability to adapt to varying substrate geometries, influencing reaction kinetics and promoting efficient catalysis through enhanced molecular recognition.

15(R)-Prostaglandin E1 acts as a PGDH by forming specific electrostatic interactions with the enzyme's active site, which aids in the precise alignment of substrates. Its unique cyclopentane ring structure contributes to distinct steric effects, influencing the enzyme's catalytic efficiency. Additionally, the compound's ability to undergo conformational changes allows it to modulate binding affinities, thereby impacting the overall reaction dynamics and enhancing substrate specificity.

SW033291 functions as a potent PGDH by engaging in selective hydrogen bonding with key residues in the enzyme's active site, facilitating substrate orientation. Its unique structural features, including a rigid backbone, promote enhanced stability during enzyme-substrate interactions. The compound's ability to adopt multiple conformations allows for dynamic adjustments in binding interactions, ultimately influencing reaction rates and selectivity in metabolic pathways.

α-Ketobutyrate acts as a competitive inhibitor of PGDH, targeting its active site and thereby affecting serine biosynthesis.

Phenylhydrazine inhibits PGDH by interacting with the enzyme's substrate-binding site, leading to an alteration in enzyme activity.

Erastin indirectly inhibits PGDH through its action on system xc-, which affects cystine uptake and indirectly impacts serine synthesis.

Sulfasalazine can inhibit PGDH indirectly by affecting cellular redox status, which in turn influences the enzyme's activity.