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Article

Catalytic site interactions in yeast OMP synthase.

Archives of biochemistry and biophysics - 15 Jan 2014

Hansen Michael Riis, Barr Eric W, Jensen Kaj Frank, Willemoës Martin, Grubmeyer Charles, Winther Jakob R

Abstract excerpt

The enigmatic kinetics, half-of-the-sites binding, and structural asymmetry of the homodimeric microbial OMP synthases (orotate phosphoribosyltransferase, EC 2.4.2.10) have been proposed to result from an alternating site mechanism in these domain-swapped enzymes [R.W. McClard et al., Biochemistry 45 (2006) 5330-5342]. This behavior was investigated in the yeast enzyme by mutations in the conserved catalytic loop...

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Identifiers

PMID: 24262852
DOI: 10.1016/j.abb.2013.11.004

Genes

OMP

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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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