The Remarkable Character of Porphobilinogen Synthase
作者： Eileen K. Jaffe
DOI: 10.1021/ACS.ACCOUNTS.6B00414
关键词: ATP synthase 、 Enzyme 、 Porphobilinogen synthase 、 Biochemistry 、 Dehydratase 、 Allosteric regulation 、 Chemistry 、 Histone octamer 、 Active site 、 Hard metal
摘要: ConspectusPorphobilinogen synthase (PBGS), also known as 5-aminolevulinate dehydratase, is an essential enzyme in the biosynthesis of all tetrapyrroles, which function respiration, photosynthesis, and methanogenesis. Throughout evolution, PBGS adapted to a diversity cellular niches evolved use unusual variety metal ions both for catalytic control protein multimerization. With regard active site, some PBGSs require Zn2+; subset those, including human PBGS, contain constellation cysteine residues that acts sink environmental toxin Pb2+. do not soft ion Zn2+ at site instead are suspected using hard Mg2+.The most unexpected property family enzymes dissociative allosteric mechanism utilizes equilibrium architecturally functionally distinct assemblies. The high-activity assembly octamer intersubunit interactions modulate active-site lid m...
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