Stereochemistry and mechanism of the conversion of 5-aminolaevulinic acid into porphobilinogen catalysed by porphobilinogen synthase.
(3R)- and (3S)-Deuteriated forms of 5-aminolaevulinic acid have been synthesized and the (3R)-form shows a significantly larger isotope effect when incubated with porphobilinogen synthase from bovine liver and from Bacillus subtilis; based on this and on available crystal structures, a modified mechanism for the enzymic reaction is proposed.
Goodwin
Catherine E
CE
University Chemical Laboratory, Lensfield Road, Cambridge, UK CB2 1EW.
Leeper
Finian J
FJ
D000622:Aminolevulinic Acid / Q000031:analogs & derivatives / Q000378:metabolism*; D000818:Animals; D001412:Bacillus subtilis / Q000201:enzymology; D001665:Binding Sites; D002384:Catalysis; D002417:Cattle; D003903:Deuterium; D007700:Kinetics; D008958:Models, Molecular; D011162:Porphobilinogen / Q000378:metabolism*; D000623:Porphobilinogen Synthase / Q000737:chemistry / Q000378:metabolism*; D013237:Stereoisomerism
D011162:Porphobilinogen; D000622:Aminolevulinic Acid; D003903:Deuterium; D000623:Porphobilinogen Synthase