Mechanism of action of porphobilinogen deaminase. The participation of stable enzyme substrate covalent intermediates between porphobilinogen and the porphobilinogen deaminase from Rhodopseudomonas spheroides.
Highly stable labelled complexes are formed between porphobilinogen deaminase and stoicheiometric amounts of [14C]porphobilinogen. On completion of the catalytic cycle by the addition of excess of substrate, the complexes yield labelled product and display all the properties expected from covalently bound enzyme intermediates involved in the deaminase catalytic sequence.
D000642:Ammonia-Lyases / Q000378:metabolism*; D055598:Chemical Phenomena; D002621:Chemistry; D002850:Chromatography, Gel; D006898:Hydroxylamines / Q000494:pharmacology; D011163:Hydroxymethylbilane Synthase / Q000378:metabolism*; D046911:Macromolecular Substances; D011162:Porphobilinogen / Q000378:metabolism* / Q000494:pharmacology; D011758:Pyrroles / Q000494:pharmacology; D012242:Rhodobacter sphaeroides / Q000201:enzymology*; D012967:Sodium Dodecyl Sulfate / Q000494:pharmacology
D006898:Hydroxylamines; D046911:Macromolecular Substances; D011758:Pyrroles; D012967:Sodium Dodecyl Sulfate; D011162:Porphobilinogen; D011163:Hydroxymethylbilane Synthase; D000642:Ammonia-Lyases