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Article

Contribution of the dimeric state to the thermal stability of the flavoprotein D-amino acid oxidase.

Protein science : a publication of the Protein Society - 1 May 2003

Pollegioni Loredano, Iametti Stefania, Fessas Dimitrios, Caldinelli Laura, Piubelli Luciano, Barbiroli Alberto, Pilone Mirella S, Bonomi Francesco

Abstract excerpt

The flavoenzyme DAAO from Rhodotorula gracilis, a structural paradigm of the glutathione-reductase family of flavoproteins, is a stable homodimer with a flavin adenine dinucleotide (FAD) molecule tightly bound to each 40-kD subunit. In this work, the thermal unfolding of dimeric DAAO was compared with that of two monomeric forms of the same protein: a Deltaloop mutant, in which 14 residues belonging to a loop...

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Identifiers

PMID: 12717024
DOI: 10.1110/ps.0234603
PMCID: PMC2323872

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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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