Cloning and expression of a heme binding protein from the genome of Saccharomyces cerevisiae.

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Auclair K, Huang HW, Moenne-Loccoz P, Ortiz de Montellano PR

Cloning and expression of a heme binding protein from the genome of Saccharomyces cerevisiae.

Protein Expr Purif. 2003 Apr;28(2):340-9.

PubMed ID

12699699 [ View in PubMed

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Abstract

The YLR205c gene of Saccharomyces cerevisiae does not show significant sequence identity to any known gene, except for heme oxygenase (22% to human HO-1). The YLR205 ORF was cloned and overexpressed in both Escherichia coli and S. cerevisiae. Both expression systems yielded proteins that bound heme tightly. The isolated YLR205c protein underwent reduction in the presence of either NADPH-cytochrome P450 reductase or NADH-putidaredoxin-putidaredoxin reductase but did not exhibit heme oxygenase activity. The protein exhibited modest H(2)O(2)-dependent peroxidase activities with guaiacol, potassium iodide, and 2,2(')-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid (ABTS). Thus, YLR205c codes for a hemoprotein of unknown physiological function that exhibits peroxidase activity.

DrugBank Data that Cites this Article

Drug Targets

Drug	Target	Kind	Organism	Pharmacological Action	Actions
NADH	Heme oxygenase 1	Protein	Humans	Unknown	Not Available	Details