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Article

Active site of 5-aminolevulinate synthase resides at the subunit interface. Evidence from in vivo heterodimer formation.

Biochemistry - 9 Jul 1996

Tan D, Ferreira G C

Abstract excerpt

5-Aminolevulinate synthase (EC 2.3.1.37) is the first enzyme in the heme biosynthetic pathway of animals, fungi and some bacteria. It functions as a homodimer and requires pyridoxal 5'-phosphate as an essential cofactor. In mouse erythroid 5-aminolevulinate synthase, lysine 313 has been identified as the residue involved in the Schiff base linkage with pyridoxal 5'-phosphate [Ferreira, G. C., et al. (1993)...

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PMID: 8688429
DOI: 10.1021/bi952918m

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026. Manifest publication-graph-cohort-2026-09-05.1.

Source receipt: pubmed, retrieved 5 Sept 2026.

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