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Article

Modulation of dimer stability in yeast pyrophosphatase by mutations at the subunit interface and ligand binding to the active site.

The Journal of biological chemistry - 3 May 2002

Salminen Anu, Parfenyev Alexey N, Salli Krista, Efimova Irina S, Magretova Natalia N, Goldman Adrian, Baykov Alexander A, Lahti Reijo

Abstract excerpt

Yeast (Saccharomyces cerevisiae) pyrophosphatase (Y-PPase) is a tight homodimer with two active sites separated in space from the subunit interface. The present study addresses the effects of mutation of four amino acid residues at the subunit interface on dimer stability and catalytic activity. The W52S variant of Y-PPase is monomeric up to an enzyme concentration of 300 microm, whereas R51S, H87T, and W279S...

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Identifiers

PMID: 11854292
DOI: 10.1074/jbc.M200101200

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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