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Article

Structural insights into E. coli porphobilinogen deaminase during synthesis and exit of 1-hydroxymethylbilane.

PLoS computational biology - 1 Mar 2014

Bung Navneet, Pradhan Meenakshi, Srinivasan Harini, Bulusu Gopalakrishnan

Abstract excerpt

Porphobilinogen deaminase (PBGD) catalyzes the formation of 1-hydroxymethylbilane (HMB), a crucial intermediate in tetrapyrrole biosynthesis, through a step-wise polymerization of four molecules of porphobilinogen (PBG), using a unique dipyrromethane (DPM) cofactor. Structural and biochemical studies have suggested residues with catalytic importance, but their specific role in the mechanism and the dynamic...

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Identifiers

PMID: 24603363
DOI: 10.1371/journal.pcbi.1003484
PMCID: PMC3945110

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

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