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Article

One ring closer to a closure: the crystal structure of the ES3 hydroxymethylbilane synthase intermediate.

The FEBS journal - 1 Feb 2024

Bustad Helene J, Christie Marthe S, Laitaoja Mikko, Aarsand Aasne K, Martinez Aurora, Jänis Janne, Kallio Juha P

Abstract excerpt

Hydroxymethylbilane synthase (HMBS), involved in haem biosynthesis, catalyses the head-to-tail coupling of four porphobilinogens (PBGs) via a dipyrromethane (DPM) cofactor. DPM is composed of two PBGs, and a hexapyrrole is built before the tetrapyrrolic 1-hydroxymethylbilane product is released. During this elongation, stable enzyme (E) intermediates are formed from the holoenzyme, with additional PBG substrates...

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Identifiers

PMID: 37863644
DOI: 10.1111/febs.16982

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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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