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Article

Tracking the evolution of porphobilinogen synthase metal dependence in vitro.

Journal of molecular biology - 4 Feb 2005

Frère Frederic, Reents Heike, Schubert Wolf-Dieter, Heinz Dirk W, Jahn Dieter

Abstract excerpt

Metal ions are indispensable cofactors for chemical catalysis by a plethora of enzymes. Porphobilinogen synthases (PBGSs), which catalyse the second step of tetrapyrrole biosynthesis, are grouped according to their dependence on Zn(2+). Using site-directed mutagenesis, we embarked on transforming Zn(2+)-independent Pseudomonas aeruginosa PBGS into a Zn(2+)-dependent enzyme. Nine PBGS variants were generated by...

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Identifiers

PMID: 15644204
DOI: 10.1016/j.jmb.2004.10.053

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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